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Human Biosciences > Nutrition and metabolism > Flashcards

Nutrition and metabolism Flashcards

1
Q

Basic description of metabolism?

A

Energy for activity comes from food

Need to release energy by oxidation

Metabolism comprises of catabolism and anabolism

Catabolism - break down

Anabolism - building back up

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2
Q

Function of metabolism?

A

Perform vital functions:
Provision of energy required to maintain the internal composition of the cell and support its specialised functions

Provision of metabolites for the biosynthesis of its constituents of the cell and any products released by the cell

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3
Q

Why do we care about metabolism?

A

To understand how nutrition effects performance we need to understand what happens in the body to provide energy

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4
Q

What are essential nutrients?

A

Cannot be synthesised (or not in sufficient quantities) by the body

Examples are vitamins, minerals, essential fatty acids, essential amino acids

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5
Q

What are non essential nutrients?

A

Can be made in sufficient quantities by the body

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6
Q

What are macronutrients?

A

Usually required in gram quantities

CHO, Fat, Protein, Water, Alcohol

Quantitatively largest part of the diet

Provide energy

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7
Q

What are micronutrients?

A

Usually needed in small amounts (smaller than 1g)

Vitamins, minerals, trace elements

Quantitatively largest family of nutrients

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8
Q

Describe carbohydrates?

A

Carbo = carbon, hydrate = hydrogen and oxygen

Hydrated carbons = (CH2O)

Example is glucose C6H12O6

There are monosaccharides, disaccharides, and polysaccharides

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9
Q

Describe the monosaccharide glucose?

A

most common sugar in the body

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10
Q

Describe the monosaccharide Fructose?

A

Cheaper than sucrose

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11
Q

Describe the monosaccharide Galactose?

A

Used in neural tissue development

Found in lactose from milk

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12
Q

Describe the disaccharide Sucrose?

A

Made from Glucose and Fructose

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13
Q

Describe the disaccharide Maltose?

A

Made up from 2 glucose

Fermented to make beer

Found in wheat and barley

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14
Q

Describe the disaccharide Lactose?

A

Made up of glucose and galactose

Widely used in food industry

Found in Milk

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15
Q

Describe the polysaccharide oligosaccharide?

A

Less than 10 monosaccharides

Rapidly ferments in the colon

Found in leek, onion, lentils, beans

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16
Q

Describe the polysaccharide starch?

A

80% amylopectin

20% amylase

Found in potatoes, cereals, beans

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17
Q

Describe the polysaccharide dietary fibre?

A

Non starch polysaccharide

Found in cellulose plant cell walls, which is resistant to digestion

Non cellulose version found in petins, gums, glucans

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18
Q

Describe dietary fats?

A

Triaglycerol comprises up to 95%

3 fatty acids to 1 glycerol

Concentrated source of energy

Usually stored in adipose

Insulating layer under skin

Vehicle for intake and absorption of fat soluble vitamins

Contribute to labour and palatability of food

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19
Q

Describe fatty acid chains?

A

Organic chains of C, H and O

Categorised based on the number and bonding of carbon atoms

Saturated = 0 double bonds

Monounsaturated = 1 double bond

Polyunsaturated = more than 1 double bond

n = omega = number of carbons from methyl end

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20
Q

Describe phospholipids?

A

Contain glycerol backbone and 2 FA (non-polar) and polar head with phosphoric
acid residue and either sugar or amino acids

Amphipathetic acting as interface between aqueous and lipid environments, therefore essential structural components of cell membranes (phospholipid bilayer)

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21
Q

Describe sterols?

A

Arranged in a ring structure with associated side chains

Cholesterol is main sterol, often associated with a fatty acid to form a cholesterol ester

Plays a key role in membrane structure, synthesis of hormones, and bile acids

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22
Q

Where are short chain fatty acids found (C4-C10)?

A

Milk products, butter

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23
Q

Where are SFA found (C14-C18)?

A

Animal foods and fats, palm oil

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24
Q

Where is MUFA, especially C18:1 found?

A

Olive and rapeseed oils

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25
Q

Where are PUFAs, n-6 found?

A

Linoleic and soybean oil

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26
Q

Where are PUFAs, n-3 found?

A

Eicosapentanoic acid and docosahexanoic acid: oily

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27
Q

Where is cholesterol found?

A

Foods of animal origin, organ meats

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28
Q

Where are phospholipids found?

A

Animal foods

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29
Q

Where are trans fats found?

A

Ruminant animals, hydrogenated fats in manufactured goods

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30
Q

Describe dietary protein?

A

Composed of C, H, O and N

N = excreted out as urea in urine, can be used to calculate protein requirements

Made up off amino acids in polypeptide chain, digested and used throughout the body

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31
Q

What does dietary protein provide?

A

Energy

Structural material for all tissues - promotion of growth and development as Muscle, soft tissues and organs consist largely of protein and are constantly turning over

Enzymes, carrier molecules, hormones, neurotransmitters, clotting factors

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32
Q

How is quality of dietary protein determined?

A

Digestibilty, nitrogen retention

(retained/absorbed) x 100

egg protein = 100

beef and fish = 75

Above 70 = sufficient to maintain growth

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33
Q

What’s dependent on vitamin D?

A

Calcium and phosphorus building blocks of skeleton,

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34
Q

What does iron help do?

A

Form components of the red blood cell and mitochondria

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35
Q

What mainly aids provision of energy, warmth and movement?

A

Mainly CHO and Fats

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36
Q

What mainly aids resisting and fighting infection?

A

Mainly vitamins, minerals and proteins

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37
Q

What mainly aids regulation of metabolism?

A

Enzymes are proteins, and require co-factors of vitamins to function

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38
Q

Whats the DRV?

A

Dietary reference values = 40 nutrients

This gives a notional mean requirement or estimated average requirement (EAR)

Reference nutrient intake (RNI) is 2 notional SD above EAR
✦ 2SD below mean is the lower RNI (LRNI) intakes below this line are likely to be deficient for most individuals

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39
Q

Problem with RDA?

A

RDA placed at same point as RNI
✦ But too prescriptive
✦ Suggests level must be taken
✦Implies below = deficiency

DRV much clearer, provides safe intake

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40
Q

Scientific basis for establishing DRV’s?

A

Panel found no single criterion to define requirements for all nutrients

✦ No method is perfect so DRV not reported with great confidence

✦ Some cases DRV cannot be determined especially non-essential nutrients

ome reliable experimental data / some epidemiological data

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41
Q

What should be on your plate?

A 
All nutrients listed in DRV tables 
✦ Supports health, work and
leisure
✦ Provides sufficient reserve to protect during times of illness or deficiency
✦ Some protection from disease
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42
Q

What elements make up ethanol?

A

Carbon, Hydrogen, Oxygen

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43
Q

Need to know the 10 important functional groups in nutrients, the chemical structure, and where they are found

A 
Aldehyde - sugars
Amine - Proteins
Amide - Vitamins
Acyl  - Triglycerides
Carbonyl - Aldehydes, ketones, acids, amides
Carboxyl - Acids
Disulphide - Proteins
Hydroxide - alcohols
Ketone - Ketones
Phosphate - High energy compounds
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44
Q

Need to know the 13 important ions within the body, chemical symbols, what they do?

A

Ammonium - Helps maintain acid-base balance
Bicarbonate - Helps maintain acid-base balance
Calcium - Component of bones and teeth, needed for blood clotting, muscle contraction and nerve transmission
Chloride - Helps maintain acid-base balance
Fluoride - Strengthens teeth and bones
Hydrogen - Helps maintain acid-base balance
Hydroxide - Helps maintain acid-base balance
Iron - RBC formation and function
Iodide - Part of thyroid hormones
Magnesium - Necessary for enzyme function
Phosphate - Helps maintain acid-base balance, Component of bones and teeth, involved in energy exchange
Potassium - Helps maintain membrane potential
Sodium - Helps maintain membrane potential and water balance

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45
Q

How is a triglyceride formed?

A

Glycerol reacts with 3 fatty acid chain via a condensation reaction to form an ester

Provides 3 molecules of water

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46
Q

Need to know the 2 most common co-enzymes?

A

NADH
FADH

non-protein compound necessary for the functioning of an enzyme

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47
Q

Need to know the 4 types of reactions and what they do?

A

hydrolysis - Water added, lactose + water = glucose + galactose

condensation - Water is removed, glucose + galactose = lactose + water

oxidation - reduction reactions (oxidation is loss of electrons) (reduction is gain of electrons)

energy and enzymatic - involves enzymes as catalysts to speed up the reaction as they lower the energy barrier
enzymes can be used repeatedly as they are not consumed by the reaction

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48
Q

Need to know how salts acids and bases differ in their structure?

A

salts - cations (positively charged ions) and anions (negatively charged ions) and are formed with the interaction of acids and bases

acids - higher concentratin of protons so proton donor

bases - higher concentration of electrons so proton acceptor 5

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49
Q

need to know the body’s energy currency and different forms of it?

A

ATP/ADP/AMP

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50
Q

Hormone definition?

A

a regulatory substance produced in an organism and transported in tissue fluids such as blood or sap to stimulate specific cells or tissues into action.

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51
Q

Enzyme definition?

A

a substance produced by a living organism which acts as a catalyst to bring about a specific biochemical reaction.

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52
Q

What’s glycolysis?

A

breaking down of glucose into energy

occurs in the cytoplasm of the cell and is a set of reactions catalysed by enzymes

uses 2 ATPs -> 4ATPs and 2 NADH

so each cycle produces 2 ATP + 2 NADH + 2 pyruvate (can be used in (an)aerobic respiration)

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53
Q

What’s beta oxidation?

A

beta-oxidation is the catabolic process by which fatty acid molecules are broken down in the mitochondria

As well as to generate acetyl-CoA, which enters the citric acid cycle, and NADH and FADH2, which are co-enzymes used in the electron transport …

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54
Q
  1. What are the products of the electron transport chain?
A

NADH (oxidised) -> 3 ATP
FADH2 (oxidised) -> 2 ATP
each cycle produces 1 H2O

occurs across inner membrane of mitochondria

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55
Q

2 most common bonds in molecules?

A

Covalent - share of electrons

Ionic - attraction between oppositely charged ions

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56
Q

3 steps of protein synthesis?

A
  1. transcription - copying dna to mrna
  2. translation - initiation, elongation and termination reading of mrna to make polypeptide chain
  3. . post translation modifications - folding into useful structures
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57
Q

Facts about paper about importance of the importance of protein intake after exercise upon the development of muscle hypertrophy and strength during resistance training in elderly? (one MCQ)

Gmarck 2001 peer review

A

Primary research

Random control trial

If supplementation straight after changes occur

If 2 hours after it didn’t change

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58
Q

Equation for Work?

A

Force x distance

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59
Q

Equation for Power?

A

Work / Time

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60
Q

Different types of energy?

A 
Chemical
Mechanical
Heat
Electrical
Light
Nuclear
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61
Q

What’s the concept of turnover?

A

Molecules are constantly used (degraded) and restored (synthesised)

eg. energy, protein

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62
Q

What’s protein turnover?

A

Constant and concurrent processes of protein synthesis and breakdown

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63
Q

Features of ATP?

A

Adenosine tri phosphate

Energy currency of the cell

Energy source for cellular processes

24 kJ per mol of ATP

Its an immediate energy system

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64
Q

Describe ATP homeostasis?

A

Maintenance of constant intracellular ATP level

Role as common chemical intermediate

ATP degradation = ATP resynthesis

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65
Q

3 main systems in skeletal muscles to maintain ATP homeostasis?

A

Immediate

Nonoxidative (glycolytic)

Oxidative (aerobic)

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66
Q

Energy source of muscular work for power?

A

Duration: 0-3 sec

Rate of process: immediate

Storage form: ATP, PCr

Oxygen involved: No

Example: weight lifting

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67
Q

Energy source of muscular work for Speed?

A

Duration: 4-60 sec

Rate of process: Rapid

Storage form: Msc glycogen and glucose

Oxygen involved: NO

Example- 100m-400m sprint, 100m swim

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68
Q

Energy source of muscular work for endurance?

A

Duration: More than 1-2 min

Rate of process: slower but prolonged

Storage form: Glycogen, plc, lipid, AA

Oxygen involved: Yes

Example: More than 1500m run, 400m swim

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69
Q

What are ATPases?

A

Enzymes that split ATP by hydrolysis (combination with water) to form ATP + H2O = ADP + pi

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70
Q

Describe creatine phosphate (PCr) the immediate energy system?

A

5-6 greater size than ATP

PCr + ADP = ATP + Cr

High energy phosphorylated compound

PCr = Cr + Pi + Energy

Provides a reserve of phosphate energy to regenerate ATP so ADP + Pi + Energy = ATP

Reforms following exercise

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71
Q

Concentration and time to depletion of ATP?

A

24 mmol/kg dm

2 secs

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72
Q

Concentration, max rate of PCr resynth and time to depletion?

A

80 mol/kg dm

9 mol ATP/kg dm/s

8 secs

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73
Q

Describe the Myokinase reaction?

A

Catalysed by Adenylate kinase (myokinase)

2ADP = ATP + AMP

Myokinase reaction and breakdown of PCr work closely together to maintain intracellular ATP levels

Energy from ATP limited, but real importance of this reaction may be formation of AMP

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74
Q

Are changes in ATP conc good signals for control of metabolic rate?

A

no

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75
Q

Are changes in AMP conc good signals for metabolic control?

A

yes

Large amounts of AMP signal that more ATP needs to be resynthesised

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76
Q

What’s the energy charge of a cell?

A

Relative changes in adenylate determine the energy charge of the cell

Energy charge = ([ATP] + 0.5[ADP]) / ([ATP] + [ADP] + [AMP]

Is an indicator of a cell to do work

If the value is 1, the whole adenylate pool is in the form of ATP, cell has maximum free energy

If it’s 0, all ATP has been hydrolysed to AMP (only theoretically possible)

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77
Q

Normal charge of a cell?

A

0.9-.095

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78
Q

Higher AMP conc represents lower energy charge of the cell, how is it reduced?

A

Add H+ via AMP deaminase

= IMP (inosine monophosphate) + NH4+

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79
Q

What happens to IMP?

A

Either converted to inosine then hypoxanthine

Problem with this is that it leaves the muscle, resulting ni net loss of adenine nucleotides

Or

When exercise stops energy from GTP is used to convert IMP into ATP

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80
Q

Can fuel source such as PCr and CHO be depleted?

A

Yes

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81
Q

Can energy sources such as ATP, GTP and UTP be depleted?

A

No they are regulated

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82
Q

Equation for gross efficiency (%)?

A

(Work accomplished / energy expended) x 100

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83
Q

Equation for net efficiency (%)?

A

(Work accomplished / energy expended - REE) x 100

REE = Rest energy expenditure

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84
Q

Equation for work efficiency (%)?

A

(Work accomplished / energy expended - EE in unloaded) x 100

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85
Q

Equation for delta efficiency (%)?

A

( Change in work accomplished / change in EE) x 100

This is the best one, but most difficult to measure

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86
Q

Features of a bomb calorimeter?

A

The oxidation path of a human and bomb calorimeter differ

However the quantity of energy liberated from the complete breakdown of these foods remain the same

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87
Q

How many kcal per g of lipid?

A

9.45

95% digestibility

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88
Q

How many kcal per g of CHO?

A

4.3

97% digestibility

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89
Q

How many kcal per g of protein?

A

5.65

More nitrogen = more kcal

92% digestibility

Animal protein more digestible

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90
Q

How many kcal per g of alcohol?

A

7

100% digestibility

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91
Q

What do we use energy for?

A

Mainly basal metabolism

Also Physical activity

And thermogenesis

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92
Q

What organ uses most energy rest?

A

Liver - 27%

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93
Q

What’s TDEE?

A

Total daily energy expenditure

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94
Q

What’s ADMR?

A

Average daily metabolic rate

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95
Q

What’s BMR?

A

Basal metabolic rate

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96
Q

What’s RMR?

A

Resting metabolic rate

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97
Q

What’s TEF?

A

Thermic effect of food

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98
Q

What’s DIT?

A

Diet induced thermogenesis

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99
Q

What’s TEE?

A

thermic effect of exercise

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100
Q

What’s EEA?

A

Energy expenditure of physical activity

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101
Q

What are all the abbreviations?

A

components of energy expenditure

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102
Q

What’s a direct calorimetry chamber?

A

Small insulated chamber with adequate ventilation

Water flows through coils - absorbs heat showing metabolic rate

Air is recirculated with CO2 and H2O filtered out

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103
Q

What’s a respiration chamber?

A

No heat exchange measured

Measurement of oxygen in and carbon dioxide out

Food intake accurately measured

Food and urine collected

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104
Q

What’s indirect calorimetry?

A

Can use Douglas bag - sample of expired air collected

Or Breath by Breath systems

Heart rate method using accelerometer

Questionares

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105
Q

What’s doubly labelled water?

A

Has a heavy oxygen and hydrogen

Hydrogen is excreted independent of metabolic rate

Oxygen excreted as carbon dioxide and water

CO2 production = difference in H and O isotopes excretion

More O = increased energy expenditure

It’s expensive but free living

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106
Q

Energy cost of running?

A

1 kcal per kg of body mass per km run

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107
Q

What happens if you don’t intake enough calories?

A 
loss of muscle mass
Anaemia
Secondary amenorrhea
Decreased body mass
Low mineral bone density
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108
Q

For every litre of oxygen used?

A

5kcal available from CHO

4.7 kcal from fat

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109
Q

What’s secretion?

A

water, acids, buffers, enzymes aid breakdown of food

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110
Q

What’s absorption?

A

95% via small intestine

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111
Q

What’s ingestion?

A

Taking food in

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112
Q

What’s motility?

A

Contraction and relaxation of smooth muscle

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113
Q

What’s defecation?

A

Indifestible substances, cells, digested materials not absorbed

if its been in your body it’s called excretion

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114
Q

What’s digestion?

A

Mechanical and chemical

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115
Q

Digestive system organs?

A 
Mouth
Salivary glands
Stomach
Pancreas
Liver
Gall bladder
Small intestine
Large intestine
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116
Q

Features of the oral cavity?

A

Consists of mouth and pharynx

Mastication - chewing of food = mechanical digestion = increased surface area of food

Saliva released from Parotid duct, sublingual gland, submandibular duct.

Mainly water but Contains electrolytes, Proteins (immunoglobin A, Lysozyme), Enzymes (amylase, Lipase)

Tongue aids swallowing and mixing

Deglutition = swallowing

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117
Q

Which duct produces most saliva?

A

Parotid duct

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118
Q

How does salivary gland release saliva?

A

Acinar (mucous cells) produce the saliva which is isotonic with plasma

Duct cells reabsorb Na+ and some Cl-
They also secrete K+ and HCO3- into it

Impermeable to water

Hypotonic saliva for lubricant

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119
Q

3 stages of deglutition?

A

Buccal phase - Bolus of food force to the back of the throat voluntarily

Pharyngeal phase - Respiratory passage closes, and food bolus enter the oesophagus

Oesophageal phase - food goes down the oesophagus

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120
Q

Features of the oesophagus?

A

Moves food from mouth to stomach

Tube with double layer of muscle:
Circular
Longitudinal

Food moves down from pressure and peristalsis

There is a oesophageal sphincter that can open and close just above the stomach - prevents acid reflux

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121
Q

Features of the stomach?

A

3 parts are Corpus, Antrum, Fundus (find locations)

Functions:
Storage
Mixing to create chyme (gastric juices)
Regulation of emptying chyme to duodenum

Once digested pyloric sphincter opens and allows food into small intestine

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122
Q

Formation of gastric juices?

A

Pepsins and Lipases from chief cells

Intrinsic factor (abosorption of vitamin B12) and HCl from parietal cells

Ions from mucous cells - protects lining of stomach

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123
Q

Regulation of gastric secretion?

A

Cephalic phase:
30% of response to meal
Prior to food arrival
Gastrin released - hormone that increase gastric juice release

Gastric phase:
60% of response to meal
Stretch and products of protein digestion in the stomach
Causes Gastrin to be released
All stimulate motility, larger meals increase rate of emptying

Intestinal phase:
Chyme entering duodenum reduces gastrin secretion and motility
Removal of peptide fragments 
pH goes down
Duodenum distends = hormones released
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124
Q

Features of the pancreas?

A

Exocrine cell:
- Acinar cells secrete digestive enzymes (bicarbonate solution to increase pH of stomach acids to 7)
Duct cells

Endocrine cells

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125
Q

Features of small intestine?

A

Main site of digestion and absorption

Has microvilli to increase SA

3 parts are Duodenum, Jejunum, Ileum.

Good blood supply

Outer longitudinal muscle, and inner is circular, propels food over short distances

Segmentation - results in mixing of food and enzymes. Controlled by pacemaker cells and intrinsic enteric nervous system

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126
Q

Features of large intestine?

A

Enters through illeocecal sphincter / valve

Reabsorbs water

Stores faceces

Bacteria ferment remaining CHO, releasing H, CO2 and methane

Peristaltic and segmental movements are slow and non propulsive

Mass movements are infrequent

Chyme remains for a long time

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127
Q

Features of the liver?

A

Portal vein comes from the digestive tract and pancreas to the liver

Produces bile - digestion of fats, bile is from aged red blood cells

Used in metabolism

Processes drugs and hormones

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128
Q

Features of gall bladder?

A

Stores and concentrates bile

Stimulated release by secretin and CCK
90% reabsorbed and recycled

Can be removed

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129
Q

How long is food in each part of digestive system?

A

Mouth - 10 secs

Stomach - 2-4 hours

Small intestine - 3-10 hours

Large intestine - 24-72 hours

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130
Q

What’s diffusion?

A

High conc to low conc

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131
Q

Facillitated diffusion?

A

High conc to low conc with a carrier protein

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132
Q

Facillitated with sodium transport?

A

Requires ATP

Sodium ions usually involved

Can work against concentration gradient

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133
Q

Complex carb we ingest from plants?

A

starch

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134
Q

Complex carb we ingest from meat?

A

Glycogen

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135
Q

Carbohydrate digestion?

A

Polysaccharides, trisaccharides and disaccharides must be hydrolysed into monosaccharides

Collectively enzymes are glycosides or carbohydrases

Digestion starts in the mouth

Most digestion occurs in the small intestine through pancreatic a-amylase

Microvilli start breaking down the disaccharides

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136
Q

Absorption of monosaccharides and a few disaccharides?

A

Facilitated with sodium:
SGLT1 used to get Glucose and galactose into epithelial cell from the lumen, then GLUT 2 to get it into the capillary

Fructose uses facilitated diffusion with GLUT 5 to get fructose from the lumen into the epithelial cell, then GLUT 2 to get into the capillary

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137
Q

Features of protein digestion?

A

Stomach:
Gastrin
HCl
Pepsinogen produces Pepsin

Small intestine:
Endopeptidases (internal bonds broken)
Exopeptidases (external bonds broken)
Trypsin (controls the active form of enzymes above)
(50% used to digest food, 25% break down epithelial cells for new ones, 25% cause gut secretions)

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138
Q

What do proteins break down into?

A

Tripeptides, dipeptides or amino acids

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139
Q

What happens to amino acids in gut?

A

Absorbed into capillary via diffusion and sodium dependent diffusion

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140
Q

Digestion of fat?

A

Fats are hydrophobic

Bile salts emulsify fats (tiny droplets called micelles)

Lipid component of the diet:
Triaglycerols
Phospholipids
Sterols

Enzymes:
Lipase
Phospholipase
Cholesterol esterase

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141
Q

Features of triacyglycerol digestion?

A

Mouth:
Lingual lipase

Oesophagus:
none

Stomach:
Gastric lipase

Duodenum and jejunum:
Lipases
Bile salts
pancreatic lipase
Bicarbonate
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142
Q

What does a triglyceride split into?

A

Monoglyceride + free fatty acids

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143
Q

Describe fat absorption?

A

Micelles move into the space between the microvilli

The fatty acid then diffuse across the membrane

Re-esterified to Triglycerides

Form chylomicrons to allow transport in lymph and blood plasma

SCFA - diffuse onto portal vein bind with albumin

LCFA - chylomicrons - into the lacteal travel in lymph

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144
Q

What happens to glucose conc in blood?

A

Humps up then down

= 100

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145
Q

What happens to starch conc in blood?

A

Long shallow hump

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146
Q

What happens to amino acid conc in blood?

A

Big hump up then down

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147
Q

triglyceride conc in blood?

A

Takes far longer to peak conc

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148
Q

What does alcohol dehydrogenase convert to?

A

Acetaldehyde (less intoxicating)

fatty acids aid this as they slow gastric emptying, so keep the food in your stomach so more alcohol converted

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149
Q

Vitamin absorption?

A

Fat soluble:
Absorbed from micelle mostly in small intestine
Enter chylomicrons and lymph system

Water soluble:
Diffusion (high conc)
Active transport (low conc)

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150
Q

How is water absorbed?

A

Osmotic gradients - hypotonic solution increases water absorption

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151
Q

Describe the hormone Gastrin?

A

Released by stomach and Duodenum

Released as a response to food reaching the stomach/preperation for food

Function is to cause stomach to release HCl + Pepsinogen, and gastric and intestinal motility

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152
Q

Describe the hormone Cholecystokinin (CCK)?

A

Released by small intestine

Released when there is dietary fat in chyme

Causes release of pancreatic enzymes and bile from gall bladder

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153
Q

Describe the hormone secretin?

A

Released by small intestine

Response to acidic cyme as digestion progresses

Stimulates release of pancreatic bicarbonate

these 3 probably are in the exam

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154
Q

2 forms of NAD+?

A

Oxidised (NAD+) and reduced (NADH)

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155
Q

Features of glycolysis?

A

Can generate ATP

Can generate reduced coenzymes which can be used to form ATP

Can generate energy independent of oxygen
Breaks down glucose to precursors for fat and protein synthesis (acetyl-CoA)

Probably can delete glycolysis and tca notes on all the steps, just know the enzymes

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156
Q

Net result of glycolysis?

A

The net result of the breakdown of glucose to pyruvate is two molecules of ATP and 2 molecules of NADH

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157
Q

3 phases of glycolysis?

A

Preparation - glucose to fructose 1,6 biphosphate

Splitting - fructose 1,6 biphosphate to 2 three carbon compounds

Harvest - 3 carbons compounds to pyruvate

158
Q

What happens if glycolysis is slow?

A

Sufficient NAD+ can be obtained from mitochondria respiration to allow the reaction from glucose to pyruvate to proceed

(Step 6 is dependent on NAD+)

159
Q

What happens if glycolysis is fast?

A

Insufficient NAD+ can be obtained from mitochondrial respiration and NAD+ is obtained from the pyruvate to lactate reaction

160
Q

Important control points of glycolysis?

A 
Glycogen phosphorylase (GP)
Glucose transport (GLUT4 in muscle)
Hexokinase (HK)
Phosphofructokinase (PFK)
Lactate dehydrogenase (LDH)
Pyruvate dehydrogenase (PDH)
161
Q

Functions of the TCA cycle?

A

Decarboxylation of acetyl CoA (CO2 production)
ATP production
FADH2 production
NADH production

162
Q

From one molecule of acetyl-COA entering the cycle?

A

3 NADH and 1 FADH2 are formed

163
Q

Dose substrate level phosphorylation occur in TCA cycle?

A

yes

164
Q

Things that can regulate the TCA cycle?

A

Substrate availability
Product inhibition
Allosteric regulation

165
Q

Features of measuring resting metabolic rate?

A

measured after a 12 hour fast

no smoking or physical activity 24 hours before

Individual rested in supine position for 30 minutes before

BMR is done with overnight stay

166
Q

RQ = ?

A

Volume of carbon dioxide produced / volume of oxygen consumed

167
Q

Frayn equation to estimate carbohydrate and fat oxidation in grams per minute?

A

Carb:
(4.55 x VCO2) - (3.21 x VO2)

Fat:
(1.67 x VO2) - (1.67 x VCO2)

168
Q

Can probably delete glycolysis and tca cycle in depth steps but keep general ones

A

ok

169
Q

Where is CHO stored?

A

Liver and muscle

170
Q

Examples of glycosaminoglycans?

A

Hyaluronic acid - good for skin

Keratan sulfate - Cornea, cartilage and bone

Heparan sulfate - animal tissue

Dermatan / chondroitin sulfate - skin, blood vessels, heart valves, tendons and lungs

Will be a short answer question on this

171
Q

What’s gluconeogenesis?

A

Making of glucose from carbon sources

172
Q

General digestion and absorption of CHO?

A

Monosaccharides absorbed

Transported via hepatic portal vein to liver

Glucose easy for body to use

Fructose and galactose produced

173
Q

What’s more likely to spike then drop glucose or starch?

A

Glucose - also produces a larger area on a graph

174
Q

Fructose metabolism?

A

Mainly occurs in the liver

Important for liver glycogen stores

Can result in triglyceride synthesis - if sedentary can lead to lipid accumulation = insulin resistance

Fructose isn’t insulin dependent - can be taken up by other cells by Glut 5

175
Q

Endocrine functions of the pancreas?

A

Glucagon and insulin

Pancreas releases insulin into blood

Starts when we eat due to increased monosaccharides

Insulin increased glucose uptake in muscle, nerve and adipose tissue

Increases glycogen storage

176
Q

How is some glucose taken up by liver cells?

A

Facilitated diffusion - due to Glut 2

Glucose accumulates

177
Q

How does insulin act on liver?

A

Binds to receptor

GLUT 2

Activates glucokinase

Converts glucose into glucose 6 phosphate

Then glycogen synthesis can occur, or removal of phosphate group and release to blood stream if conc in blood has reduced again

178
Q

Importance of blood glucose?

A

Important for the brain

Turnover that’s constantly happening requires glucose

Neurotransmitter synthesis

179
Q

What are astrocytes?

A

Cells in brain that can store glycogen

180
Q

Features of brain glucose use?

A

2% of body weight but uses 20% of our glucose

181
Q

Where does most glucose go after a meal?

A

Brain heart bladder muscle

182
Q

Describe insulin effect on skeletal muscle?

A

The same as on liver, but stimulates hexokinase

GLUT 4 transporter

Glucose can’t leave once entered, oxidised or stored

Capacity not as great as the liver

Also increased the amount of GLUT 4 going to the cell membrane = intracellular signalling

183
Q

Another way to increase glucose in cell?

A

Exercise

Calcium released by muscle contraction:
Release with contraction
Translocated Glut-4 to membrane 
Increase glucose uptake
Independent of insulin
184
Q

Describe glycogen building?

A

UDP glucose attach initially to glycogenin molecule
After 8-10 glucose units in length = pro glycogen
Glycogen synthase (regulated by insulin) takes over = macro glycogen
Branching enzyme = branched structure
12 residues trek off at about 7 and attach to neighbour

185
Q

Glycogen synthase regulation?

A

Normally in inactive form

Phosphate group blocks catalytic site

Can’t convert UDP glucose to glycogen

Insulin activates protein phosphatase on Glycogen synthase

Glycogen can now be made

Exercise stimulates Adrenaline and calcium ions stimulate protein kinase A

Increase inactive form of Glycogen synthase as need glucose for exercise

186
Q

Describe glycogen breakdown?

A

Glycogen phosphorylase b (inactive form) (no phosphate group

Glycogen phosphorylase a (active form) (has a phosphate group)

Inactive to active occurs during exercise, increased Ca+, increased adrenaline, increased glucagon, and increased AMP+ due to glycogen phosphorylase kinase (Inhibited with ATP and G-6-P)

Active to inactive occurs when there is increased insulin, through glycogen phosphorylase phosphatase

187
Q

Main features of adrenaline in metabolism?

A

Released due to fight of flight

Stimulates glucose breakdown

188
Q

Main features of insulin?

A

Released after CHO ingestion

Reduce breakdwon

Stimulate storage

189
Q

main features of glucagon?

A

Released after periods of no food

Stimulate breakdown

Inhibit storage

190
Q

Describe pyruvate dehydrogenase control?

A

Overall equation is Pyruvate to acetly-CoA to the TCA cycle

Inactive is phosphorylated (PDH b)

Active is PDH a (active)

PDH phosphatase causes the active form, due to Pyruvate (Ca2+ and Mg2+)

PDH kinase causes inactive form, due to NADH/NAD, Acetyl CoA and ATP/ADP

191
Q

Describe the rate limiting factors from glycolysis of Hexokinase?

A

Role is Glucose to Glucose-6- phosphate

Inhibited by Glucose-6- phosphate

192
Q

Describe the rate limiting factors from glycolysis of Phosphofructokinase?

A

Role is Phosphorylates fructose-6- phosphate forming fructose-1,6-biphosphate

Stimulated by ADP, Pi, low pH, NH4+

Inhibited by ATP, PCr, Citrate

193
Q

Describe the rate limiting factors from glycolysis of Pyruvate kinase?

A

Role is Transfers phosphate from PEP to ADP

Inhibited by ATP, PCr

194
Q

Describe the rate limiting factors from glycolysis of Lactate dehydrogenase?

A

Role is Conversion from lactate to pyruvate and pyruvate to lactate

Inhibited by ATP

195
Q

Describe the rate limiting factors from glycolysis of Pyruvate dehydrogenase?

A

Conversion of pyruvate to Acetyl-CoA

Stimulated by Ca2+, ADP, AMP. Pi

Inhibited by ATP, NADH, acetyl- CoA

196
Q

Describe the rate limiting factors from tca cycle of Citrate synthase?

A

Role is Catalyses condensation reaction of acetyl CoA and oxaloacetate to form citrate

Stimulated by reaction of acetyl CoA and oxaloacetate to form citrate
High oxaloacetate Ca2+
ADP

Inhibited by High citrate

197
Q

Describe the rate limiting factors from tca cycle of Isocitrate dehydrogenase?

A

Role is Decarboxylation isocitrate to oxalosuccinate and then alpha ketoglutarate

Stimulated by ADP Ca2+

Inhibited by ATP

198
Q

Describe the rate limiting factors from tca cycle of Alpha ketoglutarate dehydrogenase?

A

Converts alpha- ketoglutarate to Succinyl- CoA giving off Carbon dioxide and NADH

Stimulated by ADP Ca2+

Inhibited by High succinyl-CoA ATP
NADH

199
Q

Describe the electron transport chain?

A

4 large complexes

Electrons pass from electron donors to electron acceptors

Each electron acceptor wants the electron more than the last one

Final stage produces water

200
Q

Describe glujconeogeneis? Liver (kidneys)

A

Once 100g depleted by overnight fast of glucose in the liver (glucostat)

Glucose made from non CHO sources

Fatty acids and glycerol concs go up

Fatty acids can’t be used as precursor directly

PDH and pyruvate kinase reactions are irreversible ( so can’t reverse glycolysis to get glucose)

Acetyl-CoA from fatty acids cannot form glucose

Only carbon backbone that we can use is OAA

However Acetyl Co A stops PDH working

Causes pyruvate to be converted into OAA

Via Malate (aspirate shuttle)

OAA to PEP now reversal to glucose can occur

201
Q

How does factors of gluconeogenesis aid production of glucose?

A

TG break down:
Beta oxidation helps inhibit PDH
Glycerol can be converted to glycerol 3 phosphate and enter reversal process

Muscle breakdown:
Alanine can make pyruvate

Lactate production:
Muscle and Red Blood cell
Converted to pyruvate

202
Q

First slide on lecture 10th of feb has the questions that will be in the exam

A

ok

203
Q

How are complex lipids different to just lipids?

A

Contain other groups as well

eg. phospholipids

204
Q

Features of lipoproteins?

A

Lipids aren’t soluble = coalesce together

Lipoproteins can carry triglycerides and cholesterol esters in t =he core

Hydrophillic shell, hydrophobic core

Apoproteins on surface determine function

205
Q

4 types of blood lipoprotein?

A

Chylomicrons:
TriAcylGlyecerol (TAG) (90%) and Cholesterol esters (CE)
From intestine

VLDL:
TAG and CE carrier
Made in liver

LDL:
Only CE
‘bad cholesterol’

HDL
Only CE
‘Good cholesterol’

206
Q

What happens postprandial (after meal) fatty meal?

A

Want to store the TAG and cholesterol esters

Lymphatics secrete chylomicrons into subclavian vein

Chylomicrons dock onto lipoprotein lipase of non liver tissues (adipose tissue and muscles) - releasing fatty acids and glycerol

Fatty acids that are produced go into adipose tissue and stored and repackaged as TAG as FA binds with Glycerol

Repackaged as TAG (glycerol is from glucose here) Go into muscle cell for fuel use / intramuscular triacylglycerol for later use

When stored esterified with glycerol-3-phosphate

Remnants taken up by liver and recycled to Very low density lipoproteins (VLDL)

207
Q

Functions of cholesterol?

A

Plasma membranes

Helps make bile

Makes steroid hormones

Remnants form cholesterol pool in liver

Taken to other sites via LDL

HDL transfers cholesterol back to liver

If LDL is bigger than HDL a problem occurs

208
Q

What’s de nove syntehsis?

A

Making cholesterol in the body

209
Q

More features of VLDL (very low density lipoprotein)?

A

If eats lots of fat and CHO

Cant store CHO so store as fat

De novo synthesis occurs in liver making TAG

VLDL take the TAGs away from the liver so don’t get fatty liver

Remnants return to the liver

210
Q

Describe the post absorptive state (all food absorbed)?

A

No chylomicrons

Liver produces VLDL to carry TAG

TAG in adipose tissue hydrolysed into FA + glycerol by hormone sensitive lipase

FA out of adipocytesnow

Bind to albumin to prevent coalescing

FA then utilised by other tissues

211
Q

Regulation of fatty acid utilisation control points?

A

Lipolysis of triacylglycerol to form free fatty acids

Re-esterfication of the fatty acids, or mobilisation from adipose tissue

Transport of acyl-CoA into the mitochondria

Availability of FAD and NAD for beta oxidation

212
Q

Features of fatty acid lipolysis and mobilisation from adipose tissue?

A

When stressed/ post absorptive or just done exercise

TAG mobilised for oxidation

Similar to glycogen mobilisation as under similar circumstances and under hormonal control

213
Q

Describe lipolysis enzyme regulation?

A

Hormone sensitive lipase

Hydrolyses TAG into FA and glycerol

There is pancreatic lipase (digestive enzyme)

And Lipoprotein lipase (adipose epithelial cell)

HSL activated by protein kinase

Regulated by phosphorylation, phosphorylated when active

Inactivated by phosphatase

214
Q

Describe when inactive form of HSL occurs?

A

When inactive (anabolic)

More re-esterification

More Insulin about

215
Q

Describe when active form of HSL occurs?

A

Active (catabolic)

Break down of TAG

Exercise

Adrenaline

Growth hormone

Cortisol

216
Q

Lipolysis vs re-esterification?

A

Need fatty acids out the cell

Difficult due to re esterification

Adipose tissue good at making TAG

Glycerol has to leave when released

With exercise there is increased lipolysis (more FA leaves the cell) and reduced glucose uptake so less glycerol for re esterification

217
Q

Describe how fatty acids are mobilised with exercise?

A

Interstitial fluid = between circulation and plasma membrane of muscle cell (sarcolemma)

Fatty acids arise in albumin or VLDL or chylomicrons

LPL acts on the endothelial cell of capillary and Fatty acid is released and transported into the cell down a conc gradient

Hence the conc gradient is a site of regulation

218
Q

Rate limiting steps (not rlly) of mobilisation?

A

Getting fatty acids out of adipose down conc grad and into blood bound to albumin isn’t rate limiting but takes a while

Then getting fatty acids out of blood into cell down a conc grad is slow as well

219
Q

Describe fatty acid transport across cell membranes?

A

Dependent on plasma fatty acid concentration

‘Flip-Flop’ and carrier mediated process

Functional protein carriers are:
Fatty acid binding protein (FABP)

Fatty acid translocate (FAT/CD36)

Fatty acid tranport protein (FATP)

Once inside the cell fatty acids become activated by family of acyl-CoA synthethase enzymes to fatty acyl CoAs

220
Q

Make sure papers from seminar are noted in notes

A

ok

221
Q

Describe fatty acyl CoAs storage in muscle?

A

can undergo incorporation into other lipid pools or oxidation by mitochondria

In lipid pools are intramuscular fat droplets - similar synthesis to adipose tissue triacyglycerol droplets

Intramuscular fat droplets readily available fuel source for mitochondria

Localised with mitochondria

222
Q

In the muscle what hormone sensitive lipase stimulated into it’s active form by?

A

Calcium ions

Adrenaline

AMP

223
Q

Describe the carnitine shuttle?

A

Wan to get Acyl Co-A into the tca cycle in the mitochdonria

In mitochondria outer membrane is permeable to lipids, and the inner is impermeable

CPT 1 sits on outer mitochondria membrane

Carnitine attaches to acyl and coA removed

CACT helps across inner membrane

CPT2 removes carnnitine and attaches CoA

So basically acyl-CoA binds to carnitine to get across membrane

Beta oxidation then occurs

224
Q

Describe beta oxidation?

A

Acyl-CoA to multiple AcetlyCoA

Each carbon cycle removes 2 carbon fragments

Acetyl CoA enters TCA cycle

Continues cycle until no carbons left

Beta HAD is rate limiting enzyme

Cofactors are also rate limiting

225
Q

What’s the problem with LDL?

A

LDL lasts 1.5-2 days

Chylomicrons/VLDL last few hours

So LDL subject to damage

Damage to LDL enables bind to new receptor on macrophages (SR-A)

Good as this clears LDL from blood

Macrophage doesn’t have a cholesterol sensor tho

So it keeps consuming the LDL via endocytosis

This turns the macrophage into a foam cell (due to toxins, free radicals, excess glucose)

226
Q

What’s Atherosclerosis?

A

Foam cells larger than macrophages

And accumulate in the blood vessels

Characterised by:
Vascular inflammation
Infiltration of lipids
Cholesterol in vessel wall
Cellular debris in vessel wall
Plaque formation

So it’s not cholesterol its bad its the environment its in

227
Q

Why is HDL the good cholesterol?

A

Best predictor of cardiovascular disease (more = less chance)

Cells (except macrophages) express SR-B when there is too much cholesterol

HDL attaches to SR-B

Removes excess cholesterol

Transport cholesterol to liver

228
Q

What increases HDL?

A

Exercise

Diet

Drugs

229
Q

What do statins do?

A

Prevent are body creating it’s own cholesterol

Liver can’t make it so intracellular levels drop

The cell will therefore need more C, so it expresses more LDL receptor on its membrane

This means that more LDL leaves the blood and enters the cell

Therefore we have lowered LDL levels in the blood

Great success

230
Q

What are resins?

A

Prevent bile acids being re absorbed

More Cholesterol is excreted

231
Q

What does ezetimbe do?

A

Inactive specific membrane protein

Means you can’t absorb Cholesterol in the first place.

232
Q

Describe carbohydrate oxidation during prolonged exercise?

A

Cycle for 3 hours at 60-70% VO@

CHO oxidation decline over time as deplete glycogen stores

Want to maintain output - ATP demand of contraction, as this isn’t maintain when CHO oxidation falls

So Fat oxidation increases over time, so it’s contribution increases to maintain output

233
Q

kJ energy from CHO oxidation = ?

A

g x 15.6

234
Q

kJ energy from fat oxidation = ?

A

g x 39.4

235
Q

Plasma fatty acid concentration during prolonged exercise?

A

Muscles initially take up fatty acids so there is a decrease in plasma, also slow FA mobilisation from adipose tissue

However it increases over time due to adipose tissue lipolysis

Insulin is reduced

Adrenaline is increased

Overall fatty oxidation is increased

236
Q

How do fatty acids increase drive fatty acid oxidation increase?

A

More fatty acids results in greater efflux

Gives opportunity for muscle to take up fat and it will

Thus fat oxidation increases

Thus, plasma fatty acid availability drives fatty acid oxidation

237
Q

How does “fatty acids increase drive fatty acid oxidation increase?” effect CHO?

A

Increased fatty acid flux will increase acetyl-coA

Increased acetyl-coA inhibits PDH

Increasing citrate accumulation

This inhibits PFK

Therefore G6P accumulates

GLycoggenolysis inhibited

Reduced conc grad for glucose uptake

Therefore reduced CHO oxidation

238
Q

How can a high fat diet effect exercise?

A

Results higher fatty acid flux

Good if you want to spare muscle and liver glycogen stores so good if you are ultra endurance

Not good for high intensity exercise

239
Q

Predominant fuel at low exercise intensity?

A

Fat

240
Q

Predominant fuel at high exercise intensity?

A

Carbohydrates

241
Q

How do you know when the fat oxidation rte = 0?

A

When the RER is bigger than 1 = fatmin

FatMax is the exercise intensity at which the highest rate of fat oxidation was observed.

242
Q

Fat max zone?

A

Range of exercise intensities with fat oxidation rates within 10% of fat oxidation rates at Fatmax. The lower limit will be referred to as “low” and the upper limit as “high.”

243
Q

CHO oxidation = ?

A

(4.55 x VCO2) - (3.21 x VO2)

244
Q

Fat oxidation = ?

A

(1.67 x VO2) - (1.67 x VCO@)

245
Q

3 important digestive hormones?

A

CCK
Secretin
Gastrin

246
Q

Whats a an alpha - ketoacid?

A

Amino acid without the amine group

247
Q

What can happen to amino acid pools that are made from dietary protein?

A

Turned into body proteins and other N (excreted as sloughed hair and skin), then also converted back into amino acid pools (very small amount in urinary excretion)

Can be turned into CHO and Fat by the removal of NH3, which is converted into urea, and excreted in urine

Non essential amino acids can be formed from CHO and Fat

248
Q

Features of amino acids?

A

20 amino acids in human protein

Contain:
Carbon
Hydrogen
Oxygen
Nitrogen (amino group)

They are R group specific

249
Q

What happens to amino acid digestion when your in the fed state?

A

Insulin is already elevated

Amino acids arrive at the liver

Transport to other tissues

Storage as Tri acyl glycerides or glycogen

250
Q

What happens to amino acid digestion when your in the fasted state?

A

Body needs to make energy

Breakdown of amino acids to get their carbon skeletons

The breakdown of muscle occurs to reach these amino acids

251
Q

Amino acid fates?

A

Feed into the TCA cycle

Glucogenic = stored as CHO

Ketogenic = Stored as fat

Leucine and lysine are the only ketogenic ones

252
Q

Describe alpha keto acids in more detail?

A

Don’t have the nitrogen amine group

To convert into an alpha keto acid:

Transanimate the amino acid (AA) with alpha keto acid

Move nitrogen from amino acid to alpha keto acid

Deamination through dehydrogenase:
Remove nitrogen

253
Q

More features about transaminase’s?

A

Important for the production of non essential amino acids

Needed to expose amino acid carbon backbone to be used for energy

Transaminases enzymes are freely reversible - depends on substrate availability

Often include use of glutamate (Glu)

Occurs in most tissue including muscle

254
Q

Describe Alanine (amino acid) transaminase reaction?

will be an mcq

A

Alanine + alpha keto acid = (reverisble, enzyme is alanine aminotransferase) Pyruvate + Glutamate (amino acid)

255
Q

Describe Aspartate (amino acid) transaminase reaction?

will be an mcq

A

Aspartate + a-keto glutarate = (reversible, enzyme is aspartate aminotransferase) Oxaloacetate + glutamate (amino acid)

256
Q

What is Aspartate important for?

A

Nitrogen excretion

257
Q

Alanine impoirtant for?

A

Uptake from the blood into the liver

258
Q

Describe oxidatative demainition in more detail?

A

Occurs in mitochdonrial matrix of the liver

Results in an alpha keto acidand ammonia

Example:
Glutamate = (glutamate dehydrogenase is enzyme) Alpha keto glutarate + Ammonia

Reversible

Substarte dependent

259
Q

Which amino acid contains 2 nitrogens? in the exam

A

GLutamine

260
Q

Describe glutamine?

A

It’s glutamate + another nitrogen group

It’s the most abundnant free amino acid in skeletal muscle and blood

Used in ammoina transport

its a gluconeogenic precursor

Important in carbon + nitrogen transport between skeletal muscle and the kidneys

USed as fuel for immune cells and GI tract

261
Q

If glutamine leaves muscles its known as?

A

Cataplerotic loss

262
Q

Describe nitrogen excretion?

A

Catabolic

Purine njcelotide cycle produces ammonia

ammonia is toxic

Ammonia is converted into urea, then urine then excreted

Urea cycle occurs in the liver:
Involves energy and enzymes

263
Q

Describe the urea cycle in more detail?

A

Carbomoyl phosphate creation from CO2 and ammonia:
Irreversible and requires energy

Asparate enters

Fumarate created - in the TCA cycle

flux relies on the amount of ammonia put in

Urea created

Urea leaves as sweat or urine

264
Q

3 branched chain amino acids?

A

Leucine

Isoleucine

Valine

Can be oxidised in skeletal muscle (only ones that are)

Occurs in mitochondria

Not in liver

265
Q

Describe Leucine oxidation in skeltal muscle?

A

Transaminate with alpha ketoglutarate (remove amino group)

Enzyme is aminotransferase

= glutamate + which can be converted into alanine by alanine aminotransferase, works both ways

So alanine can be converted into glutamate and a-ketoisocaproate

The a-ketoisocaproate then has it’s hydrogen and carbon removed by ketoisocaproate dehydrogenase with NAD+ to form Isovaleryl CoA + CO2 and NADH

This reaction is irreverisble and highly regulated

Wont have to known this in detail for the exam, so can simplify it, just know the big products

Then through ATP isovaleryl CoA is turned into acetoacetate then acetly CoA which is fed into the TCA cycle

266
Q

What can aid in BCAA oxidation?

A

Vitamin B12 and Biotin are involved in the energy pathways

267
Q

Why is alanine impoirtant?

A

Important for inter tissue transport

Released from muscles

Taken up by liver

268
Q

Describe the glucose alanine cycle?

A

Glycogenolysis results in glucose 6 phosphate in muscle from the stored glycogen

Glycolysuis occurs and pyruvate is made

Go through transamination with an amino acid to form alanine

Alanine is transported into the blood

Alanine is taken up by the liver

Alanine undergous transamination with alpha keto glutarate to form pyruvate and glutamate

Pyruvate goes through gluconeogeneis

Glucose is released back into the blood

glucose is taken back into the muscle

Glutamate is demainiated

Amminoia is lost thoigj urea or creates plasma proteins

269
Q

What is muscle protein synthesis?

A

Building up of amino acids into functioning muscle

270
Q

What is muscle protein breakdown?

A

Degradation of polypeptide chains within a muscle

271
Q

What is net balance?

A

Relationship between synthesis and breakdown

272
Q

What is protein turnover?

A

Constant use and restoration of protein, how much breakdown and building up is happening

so not the same as net balance

273
Q

Changes in tissue protein result from?

A

Amino acids in blood going to amino acids in cell which can be made into proteins in the cell

274
Q

Net protein balance=?

A

Protein synthesis - protein breakdown

275
Q

How much energy used on protein turnover?

A

20% of basal energy

Formation of RNA

Making peptide chain

Selective Gene expression, then the activation (or modification or conversion) of the proteins

276
Q

Why are some enzymes used in proteins have less than 1< half life?

A

So can respond to changing conditions

277
Q

Overview of protein synthesis?

A

Sense strand and a non sense strand are in the double helix

Sense strand binds to another strand to form mRNA via RNA polymerase via complementary base pairing

This is transcription, occurs in the nucleus

Translation occurs, ribosome attaches, tRNA attach via complementary base pairing

All MRNA chains start with AUG, so UAC tuna binds so amino acid MET binds

the amino acids bind together to form a polypeptide

Then post translational modification and targeting to ensure proteins are activated

278
Q

Describe transcriptional control?

A

Transcription factors:

Activators:
Bind to enhancer sites and cause transcription

Coactivator proteins:
Make signals that aid the activators bind

Repressors:
Bind to silencer sites, reduce rate of transcription

Regulation of RNA polymerase:
General factors
Specific factors
Hormones - specific steroids, secondary messengers such as cAMP

279
Q

Describe tRNA charging?

A

Amino acid + ATP + tRNA = aminoacyl-tRNA + Amp + Pi

Each tRNA has a specific anti codon, which binds to specific amino acids

tRNA synthesise contains proofreading site

tRNA charging is an irreversible process

280
Q

3 steps of translation?

A

Initiation

Elongation

Termination

281
Q

Describe translation initiation?

A

Involves 40S and 60S ribosomal subunits, mRNA molecule, the initial aminoacyl-tRNA (tRNA molecule with methionine attached), a number of protein factors to control the initiation process and energy from GTP

282
Q

Describe elongation in transaltion?

A

Involves the addition of amino acids to the carboxyl terminal end of the polypeptide chain

The process occurs because the anticodon of aminoacyl-tRNA recognises the second codon on the mRNA

A peptide bond occurs between the carboxyl group of MET and the second amino acid which is still attached to its tRNA

283
Q

Describe termination translation?

A

Stops when stop codon is reached

A termination factor releases the complete polypeptide chain from the last tRNA and the 80s disassociates to its tow 40S and 60S subunits

284
Q

Describe post translational processing?

A

After the polypeptide is released from the translational apparatus, it requires further processing it is in:

Physiologically active form and the cell location where it becomes functional

A growing protein will begin to fold as it is being made and proteins have the capacity to self fold, however many complex proteins need help to fold out

Such as:

Molecular chaperones or chaperonins, eg heat shock proteins (Hip)

Scaffolding proteins

285
Q

Control sites of translation?

A

Elongtion factors and initation factors

286
Q

Control sires of post translational processing?

A

Chaperones and scuffling proteins

287
Q

Describe protein breakdown?

A

Quality control:
Remove mutants
Remove damaged proteins

Turnover:
Short life
Lost activity / not needed

Provision of AA
Energy (Alpha ketoacids)
Protein synthesis

288
Q

5 main pathways for protein synthesis breakdown ?

A

ubiquitin - proteasome:
Specific protein marked for degradation
Marking = ubiquitin

Lysosomal:
Endocytosis

Caspases:
Programmed cell death

Matrix metalloproteinases:
Remove extracellular matrix

Calpain:
Calcium activated

289
Q

Measurement of muscle growth/loss?

A

Fractional synthetic rate (FSR)
✦ Fractional breakdown rate (FBR)

At rest breakdown rate larger than synthesis rate

290
Q

What does exercise do to muscle protein synthesis and breakdown?

A

Increases synthesis more than breakdown (both still increase)

Synthesis stays higher, and far more prominent in untrained individuals

Eccentric and concentric exercise both works

291
Q

Net balance before and after exercise of muscle protein balance?

A

Negative before exercise

Becomes less negative after exercise

In untrained can see up to 48h

Will only go positive with extra amino acids

292
Q

How do you maximal protein synthesis?

A

Work to failure

In longer term, strength not defiently related to strength

293
Q

Is there evidence in humans muscle protein synthesis goes down with exercise?

A

No, can’t recreate an exercise intensity that would do that

294
Q

What muscle proteins do we have?

A

Mitochondrial proteins

Sarcoplasmic proteins

Myofibrillar proteins

Collagen

Normally resistance training increases myofibrillar proteins, and endurance increased mitochondrial

295
Q

Difference in muscle protein synthesis between trainined and untrained?

A

Trained will peak earlier but decrease sooner

296
Q

How to get most net muscle protein balance?

A

Exercise rest and amino acids

297
Q

What does exercise do to protein balance over a day?

A

Go less into negative balance when hungry

And go into a larger positive balance after a meal

Nutrient consumption following exercise stimulates muscle protein synthesis and inhibits the exercise-induced rise in protein breakdown

is way muscle mass is gradually increased

298
Q

What is appetite?

A

Desire to eat

External and psych factors

Driven by senses

299
Q

What is hunger?

A

Internal drive to eat

Central:
Hypothalamus
Vagus nerve

Peripheral:
Blood glucose
Hormones

300
Q

Which Hormones make you not hungry?

A

CCK

Pancreatic Polypeptide

Peptide YY

Glucagon like peptide 1

Leptin

301
Q

What hormones makes you hungry?

A

Excess glucocorticoids

Ghrelin

Insulin (some people says it decreases)

Neuropeptide y

302
Q

What’s adiponectin?

A

Energy regulating hormone but doesn’t effect hunger

303
Q

Neural drives for the hypothalamus?

A

Taste of food
Smell of food
Nutrients

Memory
Time of day
Social situation
Stress

Exercise physical activity

304
Q

Describe the gut hormone Ghrelin?

A

Released from stomach

It’s Orexigenic = hungry

Only appetite stimulator outside the brain

Lower in obese, rise in during diet induced weight loss

Active / inactive form

Stimulates release of Neuropeptide y

305
Q

Describe process of Ghrelin release?

A

Hunger stimulates the release of gherkin from the stomach

Ghrelin travels in the blood to the hypothalamus where it acts

Stimulates appetite

Eating causes blood levels of gherlin to decrease

306
Q

Describe Leptin?

A

Released from white adipose tissue

Stimulates release melanocyte - stimulating hormone (MSH) (stops you feeling hungry)

Controls level of stored body fat, so more is released the higher your fat stores

Dosent work as well when obese

Decreases release of Neuropeptide y

307
Q

Describe the Hut hormone CCK?

A

Released from small intestine

Rises 15 after eating

Urge to eat is decreased

When applied to rodents decreasing feeding centrally, and decreases meal size and duration of time eating peripherally

308
Q

Describe gut hormone PP?

A

Acts on hypothalamus

Supresses hunger after eating

309
Q

Describe PPY?

A

Influenced by energy and composition

Released 1 h post feeding

It decreases want to eat

310
Q

Describe GLP-1?

A

Released from small intestine and colon

Proportional to energy intake

Promotes weight loss

311
Q

Describe OXM?

A

Co released with GLP-1

Proportional to Energy intake

Supresses hunger

312
Q

What does adiponectin do?

A

Role in energy homeostasis

313
Q

What does insulin do to leptin?

A

stimulates its release

314
Q

What does glucocorticoids do?

A

Defiency = anorexia

Excess = hyperphagia

315
Q

Hormonal response to exercise in lean and obese?

A

GLP-1 increase greater in Obese
Supression of circulating deacylated ghelin greater in obese

PYY increase was greater in lean

No effect on food intake - so hormones not all that is important

Problem with ad lib buffet could have problems

316
Q

Is energy intake greater in the cold?

A

yes - mainly carbs

could be a problem for obese people trying to lose weight

317
Q

Does hypoxia supress appetite?

A

yes

Hypoxia has lower acylated ghrelin

Appetite responses to exercise do not appear to be influenced by exercise modality

318
Q

Does hypoxia supress appetite?

A

yes

Hypoxia has lower acylated ghrelin

Appetite responses to exercise do not appear to be influenced by exercise modality

319
Q

How to test for a reducing sugar?

A

Benedict’s reagent

Add to the food and boil in a water bath

Initial colour is blue goes to a brick red precipitate if positive

320
Q

How to test for starch?

A

Add iodine reagent

Just add it to the food

Initial colour is yellow/brown, goes blue/black if positive

321
Q

How to test for protein / amino acids?

A

Add biuret reagent

Just add it to the food

Initial colour is blue goes lilac/purple if positive

322
Q

How to test for fat?

A

Add ethanol to the food to dissolve the fat then add water

Initially colourless then white emulsion appears if positive

323
Q

What are vitamins?

A

Essential organic molecules

Not made in the body

13 identified

Water soluble = B and C

Fat soluble = A , D, E and K

324
Q

Vitamins as antioxidants?

A

A, C and E (ACE!)

During exercise there is free radical production (oxidative damage) and maybe tissue damage

Antioxidants protect you from free radical production

Large doses of them are not needed just get them from diet

325
Q

Features of water soluble vitamins?

A

All of the vitamin B’s and C

Dissolve in water

Consume daily

Destroyed by high heats and bright light

Excreted if excess

326
Q

Role of water soluble B vitamins?

A

Needed for energy release (1, 2, 3 ,5 ,6, 7)

Hematopoietic = red blood cell production (5, 6, 9 and 12)

327
Q

Describe B vitamins acting as a co enzyme?

A

Binds to inactive enzyme making it an active enzyme

Role in energy metabolism

328
Q

What could exercise increase need for energy metabolism related B vitamins?

Probably not true so idk if need to know

A

Altered absorption

Increased turnover

Biochemical adaptations

Increased mitochondria

Increased tissue repair

Higher intakes of macronutrients

329
Q

What could make athletes need more Haemopoietic B vitamins?

Probably not true so idk if need to know

A

Altered absorption

Increased turnover, metabolism loss

Biochemicals adaptations

Increased tissue repair

Altering RBC fragility

330
Q

A deficiency in Vitamin B1 results in?

A

Beriberi

331
Q

A deficiency in vitamin B2 results in?

A

Ariboflavinosis

332
Q

A deficiency in vitamin B3 results in?

A

Pellagra

333
Q

A deficiency in vitamin B9 or B12 results in?

A

Megaloblastic anemia

334
Q

Do deficiency in B vitamins result in decrease in exercise performance?

A

yes

They don’t need more just need enough

335
Q

Describe vitamin C (Ascorbic acid)?

Name is in the exam

A

Antioxidant

Aids synthesis in body

Aids catabolism

Required for normal iron absorption

Facilitattes cytochrome P450 enzyme function

Immune function

336
Q

Vitamin C dosage?

A

10-1000mg a day

Too much results in GI distress and kidney oxalate stone formation

Too little results in scurvy and poor health

337
Q

Describe Vitamin A?

Fat soluble

A

Retinol

Vision, reproduction, bone, immune, skin

Stored as retinal esters = pre form

Obtain from plant (beta carotene) and animal sources (retinol)

338
Q

Describe Vitamin D?

Fat soluble

A

Calciferol

Absorb calcium, bone, immune

Made from the sun in the skin from cholesterol

Activated in kidney and liver

Regulates calcium balance:
Urinary excretion and intestinal absorption

339
Q

Describe Vitamin E?

Fat soluble

A

Tocopherol

Antioxidant, Immune, toxins

Potent antioxidant, aids selenium metabolism

Founds in nuts

No clear deficiency disease just feel ill

High dose can interfere vitamins absorption

340
Q

Describe vitamin K?

Fat soluble

A

Medanione

Blood clotting factors, bone health

Does clotting

Synthesised by gut bacteria - antibiotics reduce it

Blood clotting

Formation of bone

341
Q

Deficiency in vitamin A?

A

Loss of vision and skin issues

Toxicity can result if too much

342
Q

Vitamin D deficiency?

A

Rickets, osteomalacia, osteoporosis

Toxicity if too much results in hyper;caemia and bone demineralisation

343
Q

Deficiency in vitamin K?

A

Bloody vomit, bleeding into joint capsules, bruising or bleeding gums

Too much (toxicity) Jaundice anaemia or hyperbilirubinemia

344
Q

Does taking more vitamins aid performance?

A

no sufficient is fine

There is no energy in them

345
Q

Difference between macro and micro nutrients?

A

Macro need more than 100mg a day

Ca, Cl, Mg

micro is less than 100mg a day

Fe, Zn, Cu

346
Q

Describe mineral absorption?

A

Some minerals such as calcium and iron are difficult to absorb

Excess can be harmful

Calcium stops Fe and Zn

Zn stops Cu

Moderate excess the kidneys will excrete

347
Q

Role of Iron in the body?

A

Oxygen transport and utilisation

Components:
Haemoglobin
Myoglobin
Cytochromes

In immune cells

Males need more - females loss more in menustration

348
Q

How do we store iron?

A

Stored with a protein called Ferritin

In Lier, sleep and bone marrow

There is soluble ferritin (dependent on ferritin conc), and transferrin (ingested foods to tissues)

349
Q

Normal iron status male and females?

A

Hb (g/L) - males 140, females 120

Serum ferritin (ug/L) - males 110, females 30

Serum transferrin - 20-40 for both

350
Q

What’s Iron depletion?

A

Low serum ferritin everything else is normal

Common in athletes and there is no performance effect

Lots of Iron can be loss through sweat and only 25% absorbed in gut

351
Q

Features of Sodium?

A

Maintain normal body fluid balance, osmotic pressure and blood pressure

Can be lost in swear

High intake can result in hypertension

Increase in extracellular fluid volume as water is pulled from cells to maintain normal sodium concentrations

RDA = 2.4 g (6g of salt)

352
Q

Features of Zinc?

A

Energy production as co enzyme

Macronutrient metabolism

Enzyme roles - LDH and ADH

Allows you to consume alcohol

Roles in nucleic acids and hormones

Aids protein synthesis and wound healing

Most present in muscle then some in bone (bone most responsive to changes in diet)

353
Q

Zinc and appetite?

A

Zn not consumed a lot in athletes who are not already meeting energy requirement

Can cause anorexia as Zn has a role in reduced appetite

354
Q

Features of magnesium?

A

Essential cofactor of enzymes in energy metabolism

Mg is also required for maintenance of electrical potentials in muscles and nerves

Too much fibre stops Mg absorption

Vitamin D aids Mg absorption

355
Q

Mg too high or too low?

A

400-420mg for males

310-320 mg for females

Defiency neuromuscular abnormalities, muscle weakness, cramps, bad mood

Too high = diarrhoea

356
Q

Features of calcium?

A

Osteoblasts and osteoclasts are responsible for bone modelling

Turnover -calcitonin and parathyroid hormones

Inadequate Ca results in osteoporosis eventually protected by 1000-1200 mg/day Ca

357
Q

Locating graves?

A

Vegetation disturbance
Topography - dips and rises
Geophysics

358
Q

How to tell age from bones?

A 
Bone fusion state
Tooth eruption 
Tooth wear
Tooth cementum annuli
Tooth amino acid racemization
359
Q

How to determine sex with bones?

A 
Pelvis
Facial features
Statures
Robusticity
DNA
Protein peptide markers in teeth
360
Q

2 general groups of immune systems?

A

Innate

Acquired

361
Q

Describe innate system?

A

Born with, activated when infected

Anatomical barriers eg. skin

Chemical barriers

Phagocytes:
Neutrophils, Eosinophils, Basophils, Monocytes, Macrophages

Natural killer cells

362
Q

Describe acquired immune system?

A

Develops through age, and past infections

Specific

Cells:
Cell-mediated
Cytptoxic t lymphocytes

Humoral:
Antibodies (B-Lymphocytes)

Immunoglobulins

363
Q

Function and blood count (x10^9/L) of neutrophils?

A

Phagocytosis

2-8

364
Q

Function and blood count (x10^9/L) of Eosinophils?

A

Destroy parasites

0.04-0.4

365
Q

Function and blood count (x10^9/L) of Basophils?

A

Trace

Inflammation

366
Q

Function and blood count (x10^9/L) of Lymphocytes?

A

Immune response

1.5-3

367
Q

Function and blood count (x10^9/L) of Monocytes?

A

Phagocytosis

0.2-0.8

368
Q

Does running a marathon increase your risk of a respiratory infection and worse symptoms?

A

yes

Moderate is least amount of risk (in the exam)

Low is bad as well (not as bad as high)

This is the J shaped curve

It becomes an S shaped curve if the individual is trained (not as bad)

369
Q

What is Biphasic leukocytosis during exercise composed of?

A

Neutrophils and lymphocytes increase

Then neutrophils increase again (but they have reduced function)

Due to more blood flow hence shear stress

Shear stress decrease adherence of white blood cells

Catecholamines also decrease adherence this is called demmargination

370
Q

What does the hypothalamus release to in turn cause mobilisation of neutrophils from the bone marrow?

A

Cortisol by stimulating the adrenal cortex

371
Q

What is lymphoctopenia?

A

Fall in lymphocytes after exercise bellow basal level, they then increase again

Gives you a window of time for you to be infected

372
Q

How to measure how well neutrophils are working?

A

Elastase release

373
Q

Overview on what exercise does to neutrophils?

A

Acute:
Increase neutrophils
Inhibit function

Chronic:
Reduce function
Deplete bone marrow reserves

374
Q

Whats selective proliferation?

A

Producing T cell or B cell with specific surface antigen receptor to foreign agent

Exercise decreases this ability in lymphocytes during the window of more likely infection

Addition of Cortisol can prevent this

375
Q

Describe lymphocytes?

A

Start as T helper cells then turn into T or B lymphocytes

T:
Release cytotoxins target viruses

B:
Release antibodies and target bacteria

Also exercise causes inhibitory responses and counter regulation so you are more likely to produce B cells

376
Q

Does decrease in salivary IgA represent more risk of infection?

A

yes

40% decrease does

377
Q

What can you do if you are training intensely to maintain your immune function?

A

CHO during exercise prevents rise in cortisol and adrenaline hence reduces secondary rise in neutrophils which is good?

Also maintains your blood glucose levels

Prevents fall in IFN-y, good as IFN-y released from t lymphocytes (so keeps there levels high), (go back and check this interaction between B and T lymphocytes)

Can take Querectin, maybe reduces infection rate

Maybe beer

Probiotics help

Protein is important for immune cells (maybe intense training)

Vitamin C and D is good

378
Q

How is nitric oxide produced?

A

L-argine + O2 is turned into NO via nitric oxide synthase

NO then turns into Nitrite NO2-

This is then turned into Nitrate NO3-

379
Q

Why is NO important in exercise?

A

Control/regulation of:

Vascular tone and blood flow
Mitochondrial respiration
Muscle excitation-contraction coupling
Glucose and calcium homeostasis
Neurotransmission
380
Q

Where do we get nitrate from?

A

Green leafy vegetables and beetroot

381
Q

What reduces NO3- into NO2- in the body?

A

Faculative bacteria

382
Q

What happens when nitrite enters your body?

A

GO across intestinal wall into systemic circulation

Gets into your saliva gland

On our tongue is where the bacteria live which cause the reduction

Swallowed NO2- reaches systemic circulation

Circulating NO2- forms NO and other reactive nitrogen species

NO causes bioactivity

383
Q

Does antibiotic mouthwash decrease benefit of eating salads?

A

YES

384
Q

Does nitrate improve muscle efficiency?

A

yes

8mmol is best amount to take

385
Q

In athletes are the effects less of beetroot juice?

A

yes

This could be due to:
Higher NOS activity
Higher baseline plasma [Nitrite]
Better muscle oxygenation
Higher mitochondrial volume and efficiency
Nitrate dose already high and duration of supplementation
Higher proportion of type 1 fibres

386
Q

Does Nitrate improve cognitive decisions?

A

yes

387
Q

Mechanisms in which nitrite aids performance?

A

Maybe mitochondria become more efficient

ATP requirement for mitochondria goes down

More blood flow so more oxygen, directed to muscle region that is oxygen deficient

388
Q

Nitrate supplementation and training together?

A

Improved exercise tolerance/performance:
Mitochondrial biogenesis
Angiogenesis
Change your muscle fibre type

Training is better than just having beetroot juice (both still improve)

It’s also better to take natural nitrite as has other benefits

389
Q

23-30 describes where things are found

A

ok

390
Q

83-91 are just equations or numbers that can be looked up

A

ok

391
Q

156-165 is glycolysis

A

ok

Human Biosciences (69 decks)

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