Lectures 6-10 Flashcards

1
Q

When is substrate level phosphorylation important?

A

When we need energy rapidly, without oxygen

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2
Q

Is the electron transport chain an aerobic or anaerobic process?

A

Aerobic

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3
Q

What sort of phosphorylation is glycolysis?

A

Substrate level phosphorylation

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4
Q

When a larger amount of ATP is generated, what sort of phosphorylation is it?

A

Oxidative phosphorylation

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5
Q

What is essentially the process of oxidative phosphorylation?

A

The process of using high energy electron carriers (NADH and FADH2) to generate ATP

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6
Q

What happens to glycolysis during any situation where you need energy instantaneously and rapidly and large amounts of it?

A

It is all guns blazing

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7
Q

What does glycolysis generate a lot of?

A

Pyruvate

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8
Q

Energy production via the ETC relies on what?

A

Redox reactions

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9
Q

Where does the ETC occur?

A

Occurs in the inner mitochondrial membrane

The cristae (folds) (Check this) of the mitochondria

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10
Q

Each molecule of NADH generated in the TCA cycle can generate how many ATP molecules?

A

3 ATP molecules

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11
Q

Each molecule of FADH2 can generate how many ATP molecules?

A

2 ATP molecules

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12
Q

How many ATP molecules can we derive in total from 1 complete oxidation of the TCA cycle?

A

3xNADH = 9ATP
1xFADH = 2ATP
1xATP

Total = 12ATP

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13
Q

How is the ETC regulated?

A

Largely dependent on the energy status of the cell
So it’s all about the amount of ADP and ATP, high ADP encourages energy production but large amounts of ATP means there is sufficient energy in the cell so energy production is not necessary

Slide 19, lecture 6

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14
Q

Why is the ETC not a major pathway for energy production during short duration, HI exercise?

A

Too slow

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15
Q

Why is the ETC very important for energy production in prolonged, endurance exercise?

A

Glycolysis and PCr would start to fail

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16
Q

The ETC is also very important in high intensity, intermittent sports, why?

A

Resynthesis of PCr and glycolysis fails

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17
Q

Look in PE exercise book

A

For diagrams of ATP/PC system, glycolytic system and the aerobic system

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18
Q

Can we metabolise fructose in the muscle?

A

No - the enzymes and transport proteins are not available

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19
Q

What is one of the ways that the body can use ketone bodies?

A

A process called gluconeogenesis

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20
Q

What is gluconeogenesis?

A

Essentially the reverse of glycolysis

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21
Q

Where does gluconeogenesis take place?

A

The liver

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22
Q

What substrates can the liver convert to glucose?

A

Amino acids (glutamine and alanine)

Lactate

Glycerol

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23
Q

When is lactate formed?

A

In glycolysis from the oxidation of pyruvate (which is oxidised to produce Acetyl CoA for the TCA cycle)

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24
Q

The reaction where lactate is formed in glycolysis from the oxidation of pyruvate is catalysed by which enzyme?

A

Lactate dehydrogenase (LDH)

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25
Q

What is lactate needed for?

A

It acts as a ‘safety net’ to be re-concerted back to pyruvate for glucose if aerobic oxidation is not possible

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26
Q

When is lots of lactate produced?

A

When glycolysis is full guns blazing

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27
Q

Only the liver can use glucose to make glycogen but what can muscles convert into glycogen?

A

Glucose-6-phosphate

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28
Q

How many irreversible reactions need to be overcome in gluconeogenesis?

A

3

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29
Q

When is gluconeogenesis activated?

A

When glucose is not consumed, a prime time for this is during sleep

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30
Q

When is gluconeogenesis activated during periods of exercise?

A

After 40-45 minutes of steady state exercise

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31
Q

How can you inhibit gluconeogenesis?

A

Consume a sports drink

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32
Q

What does glucagon do?

A

Causes the liver to convert stored glycogen into glucose

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33
Q

Questions

A

Slide 18, lecture 7

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34
Q

What happens to our ability to use gluconeogenesis with training?

A

It improves

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35
Q

What can the pentose phosphate pathway be used for?

A

To oxidise glucose

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36
Q

The pentose phosphate pathway can be used to oxidise glucose - how much ATP is generated?

A

None

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37
Q

The pentose phosphate pathway can be used to oxidise glucose - what is generated instead of ATP?

A

NADPH

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38
Q

The pentose phosphate pathway can be used to oxidise glucose - what are the end products of this pathway?

A

Pentose and phosphate

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39
Q

The pentose phosphate pathway can be used to oxidise glucose - where can it occur?

A

In several tissues - the most important being the cytosol of the liver and adipose

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40
Q

The pentose phosphate pathway can be used to oxidise glucose - what type of reaction is it? What is this reaction essential for?

A

It is an anabolic reaction essential for building things up

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41
Q

What is glutathione?

A

An important antioxidant

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42
Q

What increases free radical production?

A

The ETC and aerobic exercise

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43
Q

What molecule upregulates the pentose phosphate pathway?

A

NADP+

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44
Q

What is NADPH used for? And what do we use NADP+ for?

A

NADPH is used up by building new fatty acids or glutathione - we use NADP+ to get more NADPH

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45
Q

What you really need to know slide

A

Lecture 7, slide 28

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46
Q

What are biological enzymes made of?

A

Protein

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47
Q

What are proteins made of?

A

Made of individual “building block” units called amino acids (AAs) that are linked together by peptide bonds

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48
Q

What is a chain of amino acids (AAs) called?

A

A peptide

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49
Q

Long peptides are called what?

A

Proteins

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50
Q

The order of amino acids (AAs) allows for what?

A

Different proteins to have different functions

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51
Q

How many different amino acids does the body use?

A

20

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52
Q

What is an essential amino acid?

A

An amino acid that must be consumed in the diet - the body cannot make them on its own

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53
Q

How many amino acids are essential amino acids? (Must be consumed in the diet)

A

9 out of the 20 amino acids

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54
Q

What is a non-essential amino acid?

A

One that the body doesn’t have to consume and can make

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55
Q

How many amino acids are non essential amino acids?

A

11 out of the 20 amino acids

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56
Q

Complete proteins contain what? (In terms of amino acids)

A

Complete proteins contain all 9 essential amino acids

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57
Q

What are some key essential amino acids we need to know?

A

Isoleucine
Leucine
Valine

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58
Q

Examples of complete protein sources?

A

Chicken
Beef
Milk
Eggs

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59
Q

Examples of incomplete proteins

A

Nuts, seeds, vegetable proteins

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60
Q

What is the structure of an amino acid?

A

Central carbon atom linked to:

Amino group (positive)
Carboxylic acid group (negative)
Hydrogen 
Distinctive side chain (R)
Makes each amino acid different 

Lecture 8, slide 10 for diagram

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61
Q

Examples of branches chain amino acids

A

Leucine
Isoleucine
Valine

62
Q

Unlike other amino acids, most branches chain amino acid metabolism occurs where?

A

In skeletal muscle

63
Q

Why does BCAA metabolism occur in skeletal muscle and not the liver?

A

Liver lacks the first 2 enzymes in the pathways that break down BCAAs

64
Q

Where does amino acid metabolism occur?

A

Liver

65
Q

Why is Leucine unique among amino acids?

A

It’s ability to stimulate synthesis of new muscle proteins

66
Q

Different protease enzymes present in the gut break the protein into what?

A

It’s amino acids

67
Q

After release into the blood stream from the small intestine what happens to amino acids?

A

They are metabolised primarily in the liver and skeletal muscle

68
Q

Do we store proteins?

A

No

69
Q

What is transanimation?

A

The process by which other amino acids are formed?

70
Q

What does trans animation enable?

A

All amino acids required for life to be formed

71
Q

What does trans animation involve?

A

Transferring an amino group (NH3) to a keto acid (an amino acid without its amino group) to form a new amino acid

72
Q

What enzymes catalyse transamination?

A

Transaminases and aminotranferases

73
Q

Are the reactions during transamination reversible or irreversible?

A

These reactions are reversible

74
Q

Keto acids develop seven products

A

Slide 22, lecture 8

75
Q

What does the glucose alanine cycle do?

A

Converts alanine into glucose for energy

76
Q

What is oxidative deamination?

A

When the amino group is taken from the newly formed amino acid

77
Q

What happens to any amino acids that the body does not use?

A

They are removed via the urea cycle in the liver

78
Q

Degrading amino acids leads to an accumulation of which highly toxic product?

A

Ammonia

79
Q

In a normal day how much urea would an individual approximately excrete?

A

35-55g of urea

80
Q

What you really need to know slide

A

Slide 31, lecture 8

81
Q

What do proteins do each day?

A

Form new muscle cells
Form synthetic pathways
Form plasma proteins, immune cells and haemoglobin
Form new enzymes in the gut and digestive system

82
Q

What does protein turnover involve?

A
Protein synthesis (formation of new proteins)
Protein degradation (breakdown of proteins into amino acids)
83
Q

Approximately how much protein do we lose per day?

A

35-100g

84
Q

The half life of different proteins varies, some are very fast (minutes), such as…

A

Enzymes in the liver

85
Q

The half life of proteins varies, some are slow (days/weeks), such as…

A

Mitochondrial proteins

Myofibrillar proetins

86
Q

How can cardio-respiratory training and resistance training impact skeletal muscles?

A

They can upregulate proteins - leading to hypertrophy, this is part of the reason that we become fitter and stronger

87
Q

What is muscular hypertrophy?

A

An increase in muscle size

88
Q

For growth, muscle protein synthesis must exceed what?

A

Muscle breakdown

89
Q

What do we want to do in transcription?

A

We want to copy the information encoded in a gene and duplicate it to make a new protein

90
Q

In transcription the copy forms a messenger called what?

A

Ribonucleic acid (mRNA)

91
Q

Where does transcription take place?

A

In the nucleus of a cell

92
Q

In transcription (recap what transcription is) what does RNA polymerase II transcribe?

A

The info in the gene to form mRNA

93
Q

What is translation?

A

After transcription, the mRNA can now be taken from the nucleus to form the new protein (translation)

94
Q

Where is the mRNA taken after translation?

A

To ‘protein factories’ called ribosomes

95
Q

What is translation dependent upon?

A

It is dependent on the ‘genetic code’ of the mRNA, in other words what amino acids they are going to form

96
Q

Recap slide 14-19, lecture 9

A

Translation/codon stuff

97
Q

How many possible codons are there?

A

64

98
Q

What happens to mRNA after an exercise bout?

A

There will be an acute increase in mRNA

99
Q

What are the two main pathways for protein degradation?

A

Lysosomal pathway and the ubiquitin pathway

100
Q

What are the ubiquitin and lysosomal pathways used for?

A

To rid the body of damaged or abnormal proteins

101
Q

Proteins can be tagged for degradation by the addition of a chemical marker called what?

A

Ubiquitin

102
Q

Where are ubiquitin-tagged proteins taken to? And what happens there?

A

The proteasome, or “recycling centre”

There they are broken down into their component parts

103
Q

What you really need to know slide

A

Slide 24, lecture 9

104
Q

What are simple lipids?

A

Fatty acids - building blocks

105
Q

What are compound lipids?

A

Triacyglycerols - energy stores (triglycerides)
and
phosphoacylglycerols - membranes (phospholipids)

106
Q

What are derived lipids?

A

Steroids - e.g. cholesterol

107
Q

What are fatty acids composed of?

A

A hydrocarbon tail and a carboxyl group head

Slide 4, lecture 10 for diagram

108
Q

Fatty acids can vary in length from 1-30 carbons, how long are short chain fatty acids (SCFA)?

A

Less than 8 carbons

109
Q

Fatty acids can vary in length from 1-30 carbons, how long are medium chain fatty acids (MCFA)?

A

8-14 carbons

110
Q

Fatty acids can vary in length from 1-30 carbons, how long are long chain fatty acids (LCFA)?

A

More than 14 carbons

111
Q

Where are short chain fatty acids often found?

A

Milk fat

112
Q

Where are medium chain fatty acids often found?

A

Milk fat and coconut

113
Q

Where are long chain fatty acids found?

A

LCFA are the most common in our diet, they are either saturated or unsaturated

114
Q

So saturated fatty acids have any double carbon bonds?

A

No

115
Q

What is the molecule of saturated fatty acids like? What does this mean?

A

Molecule is straight and tightly packed - hence why high saturated fat foods are solid at room temperatures

116
Q

Examples of saturated fatty acids

A

Cheese
Butter
Red meat

117
Q

Do unsaturated fatty acids have any carbon double bonds?

A

Yes, at least one carbon double bond

118
Q

What is the molecule of unsaturated fatty acids like? What does this mean?

A

It is less tightly packed, meaning it is a liquid at room temperature

119
Q

What is an unsaturated fatty acid with one double carbon bond called?

A

A mono-unsaturated fatty acid (MUFA)

120
Q

What is an unsaturated fatty acid with more than one double carbon bond called?

A

Poly-unsaturated fatty acid (PUFA)

121
Q

Examples of unsaturated fatty acids

A

Avocado
Salmon
Olive oil

122
Q

How are lipids stored?

A

Stored as triacylglycerides or triglycerides in adipose tissue and muscle

123
Q

What happens when fatty acids are broken from their glycerol back bone?

A

They can be used by the liver and muscle to produce energy

124
Q

Why are lipids surrounded by a carrier protein?

A

Because they are hydrophobic and the protein helps transport lipids around the body to different tissues

125
Q

When can lipids be metabolised?

A

After a meal containing fat (not immediately however)

126
Q

Where can lipids be broken down from?

A

Adipose tissues (large stores)

127
Q

When is lipid metabolism the major metabolic pathway?

A

At rest and when hungry

128
Q

What hormone activates lipid metabolism at rest?

A

Glucagon

129
Q

What is the main hormone that activated lipid metabolism during exercise?

A

Adrenaline

130
Q

Slide 15

A

Lecture 10

131
Q

What is lipolysis?

A

The breakdown of a triglyceride into one glycerol and three free fatty acid molecules

132
Q

In lipolysis, each fatty acid is broken down by a different hormone

A

Adipose triglyceride lipase (ATGL)

Hormone sensitive lipase (HSL)

Monoacylglycerol lipase (MGL)

133
Q

Lipolysis is regulated by several hormones, such as…? What do these stimulate?

A

Glucagon
Epinephrine
Stimulate lipase enzymes to split the TAGs into glycerol and free fatty acids

134
Q

Albumin is transported to the cell cytosol by 3 different transporter proteins, what are they?

A

Fatty acid binding protein
Fatty acid transport protein
Fatty acid translocase (CD36)

135
Q

How can the number of transport proteins be increased?

A

By aerobic exercise and/or a high fat diet

136
Q

Once transported to tissues, fatty acids can be used to generate energy via a process called what?

A

Beta-oxidation

137
Q

What is the process of beta-oxidation?

A

Chemically, beta-oxidation is a process whereby the carbon chains of fatty acids are removed, therefore, shortening the molecule

138
Q

What is the aim of beta-oxidation?

A

Derive Acetyl CoA for use in the TCA cycle

139
Q

Where does beta-oxidation occur? And what does it require?

A

Occurs in the mitochondrial matrix and required oxygen

140
Q

Why is the energy yield from lipids greater than carbohydrates?

A

Because they contain more carbons

141
Q

However, because lipids have more carbons what does this mean about the rate of fat metabolism?

A

More carbons enquires more oxygen to become oxidised for energy; hence, fat metabolism is slower

142
Q

Despite fat metabolism being slower, what is an advantage of fat metabolism?

A

More ATP can be produced

143
Q

Why is Malonyl CoA decreased during exercise?

A

To allow for beta-oxidation to occur

144
Q

When does Malonyl CoA increase?

A

When there is an abundance of Acetyl CoA in the cytoplasm - inhibiting beta-oxidation

145
Q

What is Acetyl CoA availability dependent on?

A

Carbohydrate availability in the cell

146
Q

Are there any differences in the metabolism of saturated and unsaturated fatty acids?

A

Yes, two different enzymes are used to produce Acetyl CoA (not really important)

Saturated fatty acids are oxidised more quickly than unsaturated fatty acids

147
Q

Recap

A

Slide 28, lecture 10

148
Q

There is a decrease in fat oxidation in HIE due to several changes

A

Inadequate blood flow in adipose tissue inhibiting blood FFA delivery to the muscles

Lactate build up inhibits oxidation

149
Q

What you really need to know slide

A

Slide 36, lecture 10

150
Q

What is substrate level phosphorylation?

A

Generating ATP from glycolysis / TCA cycle

151
Q

What is oxidative phosphorylation?

A

The process of using high energy electron carriers (NADH and FADH2) to generate ATP

152
Q

How many H+ ions are needed to create 1 ATP?

A

Approx. 3