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Medicine UOB > MTM > Flashcards

MTM Flashcards

1
Q

What does RER do?

A

Synthesis and fold proteins

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2
Q

What does SER do?

A

Synthesis of lipid and phospholipid

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3
Q

Golgi apparatus function…

A

Add things in
Fold
Package

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4
Q

Why does mitochondria need a double membrane?

A

Chemiosmotic gradient

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5
Q

Lysosome functions

A

Degrade proteins with enzymes

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6
Q

Peroxisomes function

A

Absorb toxic substances
Hydrogen peroxides
Lipids

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7
Q

Microtubules function

A

Moving organelles around, hold in position
Directing traffic

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8
Q

Why is having a cytoskeleton important?

A

Keep in the right format
And orientation
Eg So villi at top of cell

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9
Q

Protein structure

A

Primary- amino acid sequence
Secondary- initial folding
Tertiary- 3d shape (that required the lowest energy)
Quaternary- more than one polypeptide chain

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10
Q

Side chains can be…

A

Charged (positive and negative)

Non-polar, aliphatic

Polar, uncharged

Aromatic

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11
Q

Aliphatic

A

Not aromatic
Straight or branched chains

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12
Q

Alpha helices structure

A

Helix
Vertical hydrogen bonds between molecules
R groups face outwards

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13
Q

Beta pleated sheets

A

R above or below
Folded sheet
Hydrogen bonds adjacent

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14
Q

What is globular useful for?

A

Secretion

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15
Q

Protein functions

A

Regulatory
Catalytic
Substrate binding/modification
Contact gene expression proteins
Bonds to specific DNA sequence
Etc

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16
Q

Regulation of protein function (the steps)

A

Synthesis
Localisation
Modification
Degradation

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17
Q

How are proteins localised?

A

Mostly all synthesised in rER
Contains sorting signal to direct to correct site
Move via transporters in membrane

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18
Q

The secretory pathway, how are substances secreted?

A

Via transport vesicles
Some have secretory vesicles

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19
Q

where does Protein modification occur?

A

Mostly done in rER (disulphide and glycosylation)
Anything else in Golgi apparatus

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20
Q

What is the four types of tissue?

A

Muscle
Nervous
Epithelia
Connective

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21
Q

Basal lamina is…

A

(Basement membrane)
Specialised form of extracellular matrix

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22
Q

How can the basal lamina be arranged in tissues?

A

Surround cells
Lies under sheets of epithelial cells
Separates two sheets of cells

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23
Q

Functional importance of basal lamina

A

Barrier
Molecular filter/prevent paracellular transport
Separate nerve from muscles at NMJ
Regenerate synapse after injury
Support
Limits contact

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24
Q

what is Mucousa?

A

The lining of different tracts/tubes
Epithelial cells secrete mucus (loose connective tissue)

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25
Q

what is Cell polarity?

A

Intrinsic asymmetry

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26
Q

Two key poles of epithelial cells

A

Base
Apex

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27
Q

Lateral membrane is…

A

Sides of cell contacting neighbouring cells

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28
Q

Types of intercellular junctions:

A
  1. Zonula occuldens
  2. Zonula adherens
  3. Macula adherens
  4. Gap junctions
  5. Hemidesmosomes
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29
Q

What is a Zonula occludens?

A

Cell junction
Most apical (top)
Super tight

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30
Q

What is a Zonula adheren?

A

Belt desmosome
Below ZO not as close as

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31
Q

What is a macula adheren?

A

Spot desmosome
Super common
Spot-welds
ZO and ZA and MA called junction complex

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32
Q

What is a gap junction?

A

Not so much for adhesion
More for allowing ions/molecules to pass

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33
Q

What is a hemidesmosome?

A

Not a cell-cell junction
Cell-basement junction

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34
Q

What are cell membrane composed of?

A

Mainly Phospholipids and proteins
Two sheets- bilayer
Proteins for signalling, communication and selective permeability

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35
Q

Four major phospholipids

A

Phosphatidyl-ethanolamine
Phosphatidyl-serine
Phosphatidyl-choline
Sphingomyelin

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36
Q

Intracellular signal transduction lipids

A

Phosphatidylinositol
Diacylglycerol
Ceramide
Sphingosine-1-phosphate

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37
Q

Transcription direction

A

RNA synthesised in the 5’ to 3’ direction

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38
Q

Template strand

A

Attaches to RNA molecules

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39
Q

Coding strand

A

Has same sequence as RNA (exception of uracil)

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40
Q

Splicing

A

RNA processing
Removed introns

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41
Q

Splicing requires…

A

RNA protein complexes
Called snRNP

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42
Q

RNA cap

A

Added to mRNA

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43
Q

Ribosome structure

A

Large and small subunit
mRNA binding site
P- site
A -site

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44
Q

tRNA carry…

A

Amino acids

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45
Q

P site is for…

A

Peptidyl-tRNA

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46
Q

A site for…

A

Aminoacyl-tRNA

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47
Q

tRNA structure

A

Codon
Anticodon

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48
Q

Polyribosome

A

When multiple ribosome attach to the the mRNA

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49
Q

Start site

A

AUG

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50
Q

The genetic code

A

Read in groups of 3
5’ to 3’
3 possible reading frames
Amino acids coded by a codon
Some have more than one codon
Some codons do not code amino acids(stop codons)
Universal

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51
Q

Mutations

A

Deletion
Insertion
Substitution/point mutations

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52
Q

Genes are transcriptional units made of:

A

Structural information to code for a protein
Regulatory sequences giving instructions for expression

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53
Q

Promoter region

A

A sequence right before the coding sequence

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54
Q

Enhancer region

A

A far from gene (upstream)

Gene regulatory proteins will bind to

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55
Q

Nucleosomes

A

11nm
Beads on a string
Basic units of chromatin
DNA wrapped around protein core

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56
Q

Protein core

A

8 histones

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57
Q

Linker

A

60 base pairs between histones

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58
Q

Histone tails function

A

Chemical modifications
Regulatory information
Acetylation/methylation

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59
Q

Ubiquitilation

A

Ubiquitine added to lysine

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60
Q

Histone acetylene transferases

A

Adds acetyl

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61
Q

Histone de-acetylases

A

Takes off acetyl

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62
Q

Epigenetics

A

Modifications of histones

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63
Q

X-inactivation

A

At blastocyst cells

Some cells inactivate one X chromosome and other cells the other
Random
Passed on to daughter cells

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64
Q

Metabolism definition

A

The chemical processes that occur within a living organism to maintain life

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65
Q

Catabolic pathway

A

Break down complex molecules into simple molecules and release energy

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66
Q

Anabolic pathways

A

Build complex molecules from simple and require energy (usually ATP)

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67
Q

Glucose metabolism

A

A series of reaction involving several metabolic pathways

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68
Q

Where are glycolysis, PPP, fatty acid synthesis conducted?

A

Cytosolic

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69
Q

Where are energy metabolism related pathways located?

A

Mitochondria

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70
Q

Where are TCA enzymes located?

A

Mitochondrial matrix
Apart from sic image dehydrogenase (inner membrane)

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71
Q

Oxidation

A

Gain of oxygen
Loss of electrons

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72
Q

Reduction

A

Loss of oxygen
Add electrons

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73
Q

Hydrolysis

A

Dehydration
Add/remove water

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74
Q

Phosphorylation

A

Add phosphate

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75
Q

Carboxylation

A

Add CO2

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76
Q

Ligation reaction

A

Formation of acetyl-CoA or succinyl-CoA

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77
Q

Where does ATP release its energy?

A

The 2 phosphoanhydride bonds
Releases 7.3 kcal

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78
Q

Steps of ATP production

A

Glycolysis
Oxidative decarboxylation of pyruvate
TCA cycle
Electron transport chain

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79
Q

Overall yield of glycolysis

A

Glucose -> 2 pyruvate
2ADP -> 2ATP
2NAD+ -> 2NADH

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80
Q

glucose to fructose 1,6 bisphosphate
(reaction type and enzyme)

A

two phosphorylations (hexokinase/phosphofructokinase)
one isomerisation (phosphoglucose isomerase)

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81
Q

f16bp is split

A

glyceraldehyde 3 phosphate

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82
Q

oxidoreduction- phosphorylation of GA-3-P to pyruvate (products)

A

GA-3-P
1,3 bisphosphoglycerate
3 phosphoglycerate
2 phosphoglycerate
phosphoenolpyruvate
pyruvate

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83
Q

oxidoreduction- phosphorylation enzymes

A

glyceraldehyde 2-phosphate dehydrogenase
phosphoglycerate kinase
phosphoglyceromutase
enolase
pyruvate kinase

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84
Q

anaerobic respiration

A

pyruvate to lactate
to regenerate NAD+

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85
Q

anaerobic respiration enzyme

A

lactate dehydrogenase

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86
Q

gluconeogenesis in liver and anaerobic respiration

A

cori cycle

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87
Q

gluconeogenesis energy cost

A

2 pyruvate
4 ATP
2 GTP
2NADH
= 1 glucose

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88
Q

reversible steps in glycolysis…

A

use the same enzymes in gluconeogenesis

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89
Q

pyruvate dehydrogenase function

A

mediates pyruvate decarboxylation
coverts pyruvate to acetyl coA

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90
Q

pyruvate decarboxylation net gain

A

1 CO2 produced
NAD+ reduced to NADH

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91
Q

how can acetyl CoA be made?

A

from amino acids
pyruvate
or fatty acids (reversible)

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92
Q

is pyruvate dehydrogenase reversible?

A

no
committed to aerobic

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93
Q

intracellular signal lipids
how do they work?

A

derived from plasma membrane lipids
rapidly generated
destroyed by enzymes in response
highly specific
binds to conversed regions within many different proteins
induce conformational/localised activity

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94
Q

cholesterol function

A

tightens packing
decreases membrane permeability
no effect to fluidity

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95
Q

what is the job of the polar head on cholesterol?

A

orients it in the membrane

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96
Q

why is it important that membranes are fluid?

A

signalling lipids/proteins to rapidly diffuse and interact
ensure membranes are equally shared between daughter cells
allow membranes to use for eg exocytosis

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97
Q

types of transmembrane proteins

A

single pass
multipass
b-barrel

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98
Q

peripheral membrane protein types

A

lipid linked
integrated with integral proteins

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99
Q

membrane protein function

A

transport
enzymatic activity
signal transduction
cell-cell recognition
intercellular joining
attachment to extracellular matrix/cytoskeleton

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100
Q

factors that effect simple diffusion

A

conc gradient
hydrophobicity
charge
size

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101
Q

why do cells maintain electrochemical gradients?

A

drive transport across membranes
maintain osmotic balance

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102
Q

Na+/K+ ATPase mechanism

A

3 Na+ bind
pump hydrolyses ATP and is phosphorylated
undergoes conformational change 3Na+ release
2K+ bind
pump dephosphorylated so returns to original shape

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103
Q

3 types of active transport

A

ATP-driven pumps
coupled transporters
light driven pumps

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104
Q

what is histology?

A

study of tissues to see arrangement/abnormalities/drug action

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105
Q

what are the steps to studying tissues?

A

fixation
dissection
sectioning
staining
visualisation

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106
Q

most common stain

A

haematoxylin
eosin

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107
Q

what does haematoxylin bind to?

A

acidic

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108
Q

what does eosin bind to?

A

basic

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109
Q

masson’s trichrome stains

A

nuc: purple
cyt: brick red
connective: green or blue

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110
Q

elastic van gieson stains

A

nuc: grey-blue
cyt: green-yellow
collagen: red
elastin: black

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111
Q

two types of epithelium

A

covering
glandular

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112
Q

basic structure of epithelial cells

A

apical up
basal down connected to basement membrane
connect adjacent by desmosomes and hemidesmosomes

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113
Q

layers of basement membrane

A

lamina lucida
lamina densa
reticular lamina

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114
Q

nomenclature of epithelial cells

A

number, shape, specialisation

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115
Q

number of epithelial cells

A

1 = simple
>1 = stratified

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116
Q

shape of epithelial cells

A

cuboidal
columnar
squamous

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117
Q

specialisations of epithelial cells

A

ciliated
keratinised

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118
Q

exceptions of epithelial naming

A

pseudo stratified: looks like multiple due to different heights but is only one layer of cells

transitional: eg urothelium
shape of cells change, look for umbrella cells

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119
Q

structure of epithelial cells

A

apical- specialisation
basal- anchor to membrane (receive nutrients/nervous innervation)
lateral- connect cells, cell junctions

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120
Q

cilia overview

A

made of: microtubules
10 micrometers
motile
only in few places- respiratory/reprodcutive

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121
Q

microvilli overview

A

made of actin
1 micrometre
less motile
widespread so not a specialisation that is named

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122
Q

keratinisation

A

certain squamous cells
excess produced
cells mature and keratin then left behind

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123
Q

keratin properties

A

cytoskeleton protein
strong but flexible
impermeable to water

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124
Q

4 phases of the cell cycle

A

G1 phase
S phase
G2 phase
M phase

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125
Q

3 checkpoint locations

A

entering s phase
g2
mitosis

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126
Q

quiescence

A

no activity
G0

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127
Q

restriction point criteria (at G0)

A

growth factors

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128
Q

1st checkpoint criteria

A

check for damaged DNA

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129
Q

2nd checkpoint criteria

A

incomplete DNA replication

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130
Q

3rd checkpoint criteria

A

spindle attachment failure

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131
Q

what is the cell cycle influenced by?

A

growth factors
growth inhibitory proteins
nutrients status

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132
Q

cyclin dependent kinase functions

A

regulate cell cycle checkpoint transitions
regulated by feedback themselves

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133
Q

kinases

A

an enzyme that activates/deactivates a protein by phosphorylating them

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134
Q

m-cdk does what?

A

switches itself off by initiating a process which leads to destruction of cyclin

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135
Q

how does a cyclin get activated?

A

remains inactive until it associates with new cyclin that is synthesised during interphase

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136
Q

restriction point is regulated by which protein?

A

retinoblastoma protein (pRB)

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137
Q

what can happen if pRB is mutated?

A

tumour in retina
as tumour supressor gene not activated

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138
Q

what are the proteins involved checkpoint 1?

A

p53 increase if damaged DNA
activates p21
this inhibits Cdk
so no S phase

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139
Q

what happens if the checkpoints fail?

A

proliferation of cells
replicate damaged DNA
segregation of incompletely replicated chromosomes
division of cells with the wrong number of chromosomes

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140
Q

growth factor signalling pathway

A

attaches to particular RTK (receptor tyrosine kinases)
recruits a RAS-activating protein
stimulates RAS to exchange GDP to GTP

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141
Q

oncogenic

A

involved in the origin or development of cancer/tumours

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142
Q

ways that gf pathways can come oncogenic?

A

receptors over active
signalling/ras protein is always on
over-expression of Mac transcription

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143
Q

carcinoma

A

abnormal cells that divide uncontrollably in epithelium

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144
Q

dysplasia

A

presence of abnormal cells that are not cancerous but could become so

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145
Q

metaplasia

A

one kind go cell transitioning to become another kind

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146
Q

neoplasia

A

mass of tissues that has accumulated when cells do not stop dividing or do not die

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147
Q

classic location of simple columnar

A

stomach

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148
Q

classic location of simple cuboidal

A

kidney tubules

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149
Q

classic location of simple squamous

A

blood vessel endothelium

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150
Q

classic location of ciliated simple columnar

A

respiratory tract

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151
Q

classic location of ciliated pseudo stratified columnar

A

respiratory tract

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152
Q

classic location of transitional

A

bladder

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153
Q

classic location of stratified squamous

A

skin

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154
Q

3 components of connective tissue

A

cells
fibres
ground substance

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155
Q

list the structure of connective tissue

A

-cells
-extracellular matrix: made of ground substance and fibres

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156
Q

what is ground substance made of?

A

gags
water
proteoglycans

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157
Q

what are types of fibres?

A

elastin
collagen
reticular

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158
Q

what is connective tissue?

A

diverse abundant supporting tissue

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159
Q

functions of connective tissue

A

structural support
tensile strength
binding
elasticity
immune response
cushioning
metabolism/energy store

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160
Q

what is connective tissue proper?

A

a type of connective tissue (the basic kind)

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161
Q

what are the types of connective tissue proper?

A

loose
dense

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162
Q

what is specialised connective tissue?

A

connective tissue that is specialised ie bone, cartilage, adipose, dentine, lymph

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163
Q

what are factors that effect ground substance?

A

hydration
balance of cells

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164
Q

what is a fibroblast?

A

the main type of cell in non-specialised connective tissue

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165
Q

what is the function of a fibroblast?

A

produce and maintain extracellular matrix and ground substance
activated myofibroblasts are involved in wound healing

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166
Q

what is the shape of a fibroblast?

A

spindle shaped, cigar shaped nucleus

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167
Q

what is fibrosis?

A

over activated fibroblast can ‘over heal’

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168
Q

what is a fibrocyte?

A

an inactivated fibroblast

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169
Q

what are the fixed cells in connective tissue?

A

fibroblast
fibrocyte
adipocyte
macrophages

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170
Q

why do adipocytes appear like a signet ring?

A

the stain washes away the lipid deposit in the centre so appears empty

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171
Q

ground substance function

A

viscous
bind high amount of water for hydration
diffusion of nutrients to tissue

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172
Q

what are the wandering cells that can move into connective tissue?

A

plasma cells
eosinophils
neutrophils
lymphocytes
mast cells

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173
Q

what is the appearance and function of plasma cells?

A

oval, clock face nucleus
actively produces antibodies

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174
Q

what is the appearance and function of eosinophils?

A

2 lobe nuclei
eosinophilic granules

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175
Q

appearance and function of neutrophils?

A

multi lobed nuclei

phagocytic functions

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176
Q

appearance of lymphocytes?

A

round nuclei
small cytoplasm

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177
Q

mast cells- appearance and function?

A

basophilic granules

inflammatory reactions
histamine production

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178
Q

histamine production what does it lead to?

A

causes capillaries to loosen
plasma leaves blood through gaps
into connective tissue
causes swelling (-oedema)

179
Q

what does GAG stand for?

A

glycosaminoglycan

180
Q

what are gags made up of?

A

often hyaluronic acid
contains glycoproteins and complex carbohydrates
have negative side chains

181
Q

what are properties/functions of GAGs?

A

negative side chain: acidic and hydrophilic
strong
resistance to compressive forces

182
Q

what are properties of elastin?

A

thin
branched
allows stretching
eosinophilic (pink)

183
Q

how is elastin produced?

A

fibroblasts
secreted as a precursor- tropoelastin
polymerises to become elastin
required glycoprotein fibrillin scaffold

184
Q

where is elastin found?

A

skin
ears
arteries
lungs
bladder

185
Q

what is the most abundant protein in the body?

186
Q

properties of collagen

A

high tensile strength
flexible but can break
eosinophilic (pink)

187
Q

how is collagen produced?

A

fibroblasts
pre-pro-collagen
pro-collagen (triple alphas chain)
tropocollagen

188
Q

types of collagen

A

type 1, 2, 3, 4

189
Q

what is type 1 collagen?

A

bone skin tendons ligaments

190
Q

what is type 2 collagen?

191
Q

what is type 3 collagen?

A

reticular fibres

192
Q

what is type 4 collagen?

A

basement membrane

193
Q

use of reticular fibres?

A

delicate and thin
forms framework of organs/glands/blood vessels

194
Q

what does the basement membrane get stained with?

A

no H&E
PAS- periodic acid-schiff

195
Q

what is loose connective tissue?
ie cells, proportions

A

equal amounts of cells, fibres and ground substance
cells: fibroblasts
fibres: often collagen, but also moderate amounts of others

196
Q

function of loose connective tissue

A

binding tissues
diffusion

197
Q

examples of loose connective tissue

A

lamina propria
mucous membranes
mesentery and dermis of skin

198
Q

what is dense connective tissue?

A

fewer cells/ground substance
more fibres

199
Q

types of dense ct

A

regular
irregular

200
Q

dense regular tissue..

ie structure, function, examples

A

fibres run parallel to each other
high unidirectional resistance to stress
examples: tendons, ligaments

201
Q

dense irregular ct…

ie structure, function, examples

A

interwoven fibres
3d network resistance in all directions

located: capsules/wall of organs, dermis of skin

202
Q

white adipose tissue aka..

A

unilocular

203
Q

white adipose tissue structure

A

single large lipid droplet
washed away with stain
most common in adult

204
Q

function fo adipose tissue

A

storage
metabolism
fill spaces
padding
protection
insulate
energy reserve

205
Q

brown adipose tissue aka…

A

multiocular

206
Q

brown adipose structure

A

many smaller lipid droplets
common in newborn
or around kidneys/adrenals
rich in mitochrondria/capillaries

207
Q

what is thermogenesis

A

use of glucose to produce heat
done by brown adipose
common in neonate

208
Q

ehler danlos

A

type 1,3,5 collagen (genetic mutation)
fragile, extra elastic skin
hyper mobility of joints

209
Q

marfans syndrome

A

fibrillin mutation (elastin scaffold)
affects tissue rich in elastin- aorta
skeletal defects- long digits/arms

210
Q

which steps in glycolysis are irreversible?

211
Q

regulation of metabolism is via which enzymes?

A

glycolysis- phosphofructokinase

gluconeogenesis- 1,6 bisphosphatase

212
Q

at different levels of ATP what happens to the regulating enzymes?

A

low- phosphofructokinase and glycolysis is switched on

high- phosphofructokinase is switched off
1,6 bisphosphatase is switched on so ATP goes to glucose via gluconeogenesis

213
Q

where does the TCA cycle take place?

A

mitochondrial matrix

214
Q

oxygen’s role in metabolism

A

final electron acceptor
for NADH to lose electrons and NAD to return to the cycle

215
Q

TCA starting component? end product?

A

pyruvate to CO2

216
Q

carbon net through TCA cycle

A

add two carbon atoms (acetyl group) and release 2 (from oxaloacetate) as CO2

217
Q

overal products in one turn of TCA

A

acetyl CoA -> CoA + 2CO2

3NAD+ -> 3NADH

FAD -> FADH2

GDP + Pi -> GTP

218
Q

what are the hydrogen carriers

219
Q

NAD+ from where? and how many molecules of ATP does its oxidation generate?

A

vitamin niacin (B3)

2.5 molecules of ATP

220
Q

FAD from where? and how many molecules of ATP does its oxidation generate?

A

vitamin riboflavin (B2)

1.5 molecules of ATP

221
Q

how does FAD get oxidised?

A

attached covalently to its enzyme
succinate dehydrogenase contains FAD and is bound to the inner membrane of the mitochondria

222
Q

anaplerotic reactions

A

reactions that fill in missing intermediates for important metabolic pathways

223
Q

examples of anaplerotic reactions in the TCA cycles

A

pyruvate -> oxaloacetate

oxaloacetate <-> aspartate

glutamate <-> a-ketoglutarate

malate <-> pyruvate

224
Q

overal of glycolysis and TCA cycle of hydrogen carriers

A

10 NADH
2FADH2

225
Q

NADH oxidation

A

NADH + H+ -> NAD+ + 2H+ + 2e-

226
Q

final electron acceptor equation

A

2e- +2H+ +1/2 O2 -> H20

227
Q

the transport of 2 e- will pass how many H+ into the inner membrane?

228
Q

how many hydrogen ions are required to make 1 ATP?

A

3

(plus 1 to translocate the ATP in the cystol)

229
Q

what is the job of cytochrome c oxidase?

A

transfer electrons to oxygen

230
Q

what can cytochrome c oxidase be inhibited by?

A

cyanide
carbonmonoxide
azide

231
Q

what is substrate level phosphorylation?

A

transfer of phosphate from substrate to ATP

232
Q

what is oxidative phosphorylation?

A

formation of ATP coupled to oxidation of NADH or FADH2 by O2

233
Q

role of ATPsynthase

A

stop H+ being allowed to flow back and energy then lost as heat
drive synthesis of ATP via conformational change of ATPsynthase

234
Q

the glycerol phosphate shuttle
why? how?

A

why? can only be oxidised inside the mitochondria but cannot cross the membrane

how? NADH to reduce DHAP to form glycol-3-phosphate
diffuses in
oxidised by glycol-3-phosphate dehydrogenase to from DHAP and FADH2

235
Q

malate/aspartate shuttle mechanism

A

cystolic oxaloacetate
malate dehydrogenase reduces OAA to form malate
into mitochondria
reversed by malate dehydrogenase

transaminated to aspartate transported into cystol, back to OAA by aspartate aminotransferase

236
Q

the glutamate aspartate carrier

A

maintains glutamate and aspartate cones
uses 1 h+
so less ATP per NADH

237
Q

thermogenesis how?

A

through uncoupling proteins (UCP) provides proton channel

238
Q

what type of protein is the drug dinitrophenol?

A

uncoupler
useful for thermogenesis

239
Q

what can be used to make ATP?

A

date acids
proteins
lactate
glucose
etc

240
Q

how to control metabolism?

A

enzyme levels
enzyme activity
substrate availability (eg GLUT)

241
Q

GLUT?

A

glucose transporter

242
Q

what is phosphofructokinase regulated by?

A

activated by AMP
activated by F-2,6-BP
inhibited by ATP and citrate

243
Q

control points of the TCA cycle are inhibited by what?
eg. pyruvate dehydrogenase, isocitrate dehydrogenase, a-ketoglutarate dehydrogenase

A

ATP, NADH and acetyl CoA

244
Q

metabolism profile of the brain

A

60% of body glucose consumption at rest
use ketone bodies in starvation

245
Q

metabolism profile of muscles

A

uses fatty acids at rest
anaerobic muscle - glycogen stores

246
Q

diabetes mellitus

A

imbalance of insulin and glucagon
high blood glucose
excessive ketone body production

247
Q

warburg effect

A

coverts to lactate and TCA partly in aerobic conditions
due to a tumour

248
Q

amoeba

A

unicellular organism

249
Q

zygote

A

fertilised egg

250
Q

what are the key cell processes?

A

cell division
cell death
cell differentiation

251
Q

the stages of differentiation

A

maintenance (stem cell)
expansion (progenitors)
differentiation (differentiated cell)

252
Q

pluripotent

A

can differentiate to any type of cell (stem cell)

253
Q

multipotent

A

can different to multiple/not every type of cell (progenitors)

254
Q

unipotent

A

can only be one type of cell

255
Q

oligopotent

A

can form 2+ types of cells

256
Q

why is cell differentiation so important?

A

the requirement for new cells is continuous and huge

257
Q

what makes cells different from each other?

A

functional roles
proteins
-cell type features
-metabolic
-structural
-regulatory

258
Q

platlets form…

A

haemostatic plug

259
Q

DNA binding domsin is..

A

part of a protein where the DNA binds (promoter/enhancer)

260
Q

activation domain is…

A

the part of a protein that interacts with RNA polymerase

261
Q

enhancer vs promoter

A

enhancer- enhances transcription
promoter- initiates transcription

262
Q

different transcription factors can control what?

A

differentiation of cells

263
Q

what causes differentiation?

A

extracellular signs
or transcriptional factors

264
Q

erythropoietin does..

A

promotes cell survival and differentiation

265
Q

how does differentiation work?

A

bind to receptor
signalling cascade
causes genes to be switched on/off

266
Q

RNA and DNA structure

A

DNA- double stranded, high molecular weight

RNA- single stranded, heterogeneous in size

267
Q

nucleotide consists of…

A

phosphate sugar base

268
Q

difference between ribose and deoxyribose

A

2nd carbon
DNA - h
RNA- oh

269
Q

nucleotides are joined by…

A

phosphodiester linkages
in the 5’ -> 3’

270
Q

why is RNA unstable?

A

the OH (in the ribose) can react with the phosphate

271
Q

how are DNA bases paired?
direction, type

A

antiparallel, one 5’ to 3’, one 3’ to 5’
by hydrogen bonds
AT, GC
GC have stronger bond as three h bonds

272
Q

chromosomes

A

single molecule of DNA

273
Q

gene

A

sequence of DNA that contains genetic instructions

274
Q

the human genome is diploid/haploid?

275
Q

where is DNA found?

A

nucleus and mitochondria

276
Q

how many genes are in the mitochondria?

A

37
inherited from mother

277
Q

how many chromosomes are there?

278
Q

exons are..

A

coding DNA, expressed

279
Q

introns are…

A

non coding dna

280
Q

where is the promoter region?

281
Q

where is the enhancer region?

A

anywhere
several per gene

282
Q

tandem repeats

A

repeated sequences

283
Q

satellite DNA

A

large arrays of tandem repeats
eg certain repeats at centromeres

284
Q

mini satellite
how many/function…

A

up to 100 copies in one block
found at telomeres
highly polymorphic
no known use

285
Q

micro satellite

A

small arrays of simple repeats (eg CAG)
usually intronic

286
Q

what’s the role of a telomere?

A

allow replication of tip of chromosome
protect end of chromosome

287
Q

what the role of the centromere?

A

segregation during cell division
proteins can bind and recognise the sequence

288
Q

what does microRNA Do?

A

bind to 3/UTR to inhibit translation

289
Q

different types of RNA

A

rRNA
tRNA
snRNA
snoRNA
miRNA
mRNA

290
Q

what is the unit of chromatin

A

nucleosome

291
Q

what is an nucleosome

A

DNA wound round a histone core

292
Q

what is beads on a string

293
Q

how are decondensed chromosome organised?

A

by attachment to nuclear skeleton
by functional role

294
Q

nucleolus role

A

ribosomal RNA is transcribed and ribosomal subunits are assembled

295
Q

euchromatin

A

paler
normally in gene rich areas
allowing access for transcription

is part of DNA in-between genes

296
Q

heterochromatin

A

highly condensed/inactive
generally gene poor
not often transcribed

297
Q

where can extension occur?

A

the 3’ end only

298
Q

where is DNA replication initiated?

A

replication origins
opened with the aid of initiator proteins

299
Q

what are dNTPs

A

building blocks for DNA synthesis/replication

300
Q

Okazaki fragments

A

works in parts to work 5’ to 3’ (of new strand) direction

301
Q

what binds Okazaki fragments together

A

DNA ligase

302
Q

what is the lagging strand?

A

where the fragments take place as DNA polymerase must work backwards

303
Q

what is the leading strand?

A

DNA polymerase can work continuously

304
Q

why are are RNA primers used?

A

so that DNA polymerase can bind

305
Q

how do RNA primers work with Okazaki fragments?

A

primer added
then once used replaced by DNA

306
Q

why is there minimal mistakes in DNA replications?

A

stability of base pairing
proof reading by DNA polymerase

307
Q

DNA polymerase requirements

A

template and RNA primers
dNTPs

308
Q

how is a mutation rectified?

A

mismatch repair system

309
Q

what is depurination?

A

losing a base
addition of water

310
Q

what is deamination?

A

change from cytosine to uracil

311
Q

what does UV do to thymine?

A

forms dimers so two bases join

312
Q

functions of the skin

A

physical protection
thermoregulation
sensation
metabolic functions
indicator of health

313
Q

what are the three main layers of skin?

A

epidermis
dermis
hyperdermis

314
Q

what type of epithelium is the epidermis?

A

keratinised stratified squamous

315
Q

what is the epidermis filled with?

A

mainly keratinocytes

316
Q

what are the layers of the epidermis?

A

stratum corneum
[stratum lucidum - thick skin]
stratum granulosum
stratum spinosum
basal layer/stratum basale

317
Q

stratum basale

A

cuboidal cells
most deep layer
on top of basement membrane
melanocytes present

318
Q

stratum spinosum

A

8-10 cell layers
connected by desmosomes
prickly appearance when dehydrated
produces cytokeratin

319
Q

stratum granulsum

A

3-5 cell layers
towards top are squamous
granules full of keratohyalin (deep stain)

320
Q

keratin maturation steps

A

SB mitosis
SS cytokeratin
SG keratohyaline granules
SC keratin

321
Q

stratum lucidum

A

only in thick skin
no hair

322
Q

stratum corneum

A

mature keratin (cytokeratin+keratohyaline)
squamous
no cytoplasm or organelles

323
Q

role of melanocytes

A

produce melanin in basal layer
UV protections
pigment

324
Q

role of Merkel cells

A

in basal layer
associated with free nerve endings (sensory)

325
Q

rolde od langerhans

A

immune
in all layers

326
Q

other cells in epidermis

A

melanocytes
merkel cells
langerhans

327
Q

what are the layers of the dermis?

A

papillary
reticular

328
Q

papillary layer type

A

loose connective tissue
lots of gs and capillaries

329
Q

reticular layer type

A

dense irregular collagenous tissue
elastin is present but reduces with age

330
Q

neurovascular supply of dermis

A

subpapillary and cutaneous plexus with shunting vessels between

331
Q

why are shunting vessels important?

A

control vasoconstriction
thermoregulation
controlled by ANS

332
Q

what are the five types of mechanoreceptors in the skin
mostly in dermis

A

unencapsulated:
merkel
free nerve endings

encapsulated:
pacinian corpuscle (subcutaneous)
ruffini corpuscle
meissners corpuscle

333
Q

what is hair made of?

334
Q

how does hair get oily?

A

sebaceous glands secrete oily sebum on upper part of hair follicle

335
Q

what do the arrector pili muscles do?

A

make hairs stand on end

336
Q

where are sweat glands found?

A

superficial hypodermis

337
Q

where are sebaceous glands?

A

attached to hair follicles

338
Q

classes of exocrine glands based on their secretion

A

merocrine
apocrine
holocrine

339
Q

two types of sweat glands

A

eccrine
apocrine
[both merocrine]

340
Q

what is a merocrine gland?

A

release secretory products by exocytosis
mostly proteins

341
Q

eccrine sweat gland
where?why?

A

directly on to skin
found everywhere
function = heat loss (ANS)

342
Q

apocrine sweat gland
where? why?

A

open into hair follice
regulated by hormoes
limited to axilla/genitals/areola
smelly

343
Q

psoriasis

A

abnormal epidermal growth

344
Q

malignant melanoma

A

malignant growth of melocytes

345
Q

vitiligo

A

autoimmune destruction of melanocytes

346
Q

cause of atopic dermatitis

A

environment (hay fever)

347
Q

cause of contact dermatitis

A

chemial (hairdressers)

348
Q

cause of seborrheic dermatitis

349
Q

superficial epidermal burn (layers/symptoms)

A

dermis intact, epidermis affected
skin red, painful, non blisters

350
Q

partial thickness- superficial dermal burn (layers/symptoms)

A

epidermis and upper layer of dermis affected
skin pale pink and painful with blisters

351
Q

partial thickness- deep dermal burn
(layers/symptoms)

A

epidermis and all layers of dermis affected
skin apperas dry/moist, blotchy and red
may be blisters
maybe painful

352
Q

full thickness burn (layers/symptoms)

A

through all layers of subcutaneous tissue
dry and white/brown/black skin
no blisters
leathery/waxy
painless

353
Q

autograft

A

own skin moved

354
Q

allograft

A

donor skin used to reconstruct skin

355
Q

what is the purpose of mitosis

A

cell division
growth
genetically identical products

356
Q

kinetochore

A

protein assembly at centrosome for attachment of microtubules

357
Q

different types of mitotic spindle

A

aster microtubules (all way round)
kinetochore microtubules (centromere)
interpolar microtubules (opposite poles to push apart)

358
Q

prophase

A

chromosomes condense
centrosomes move apart

359
Q

prometaphase

A

nuclear membrane breaks down
spindle microtubules attach to kinetochores and move actively

360
Q

metaphase

A

chromosomes align at the equator of the spindle
kinetochores from paired sister chromatids attach to opposite poles of spindle (M PHASE CHECKPOINT)

361
Q

anaphase

A

sister chromatids synchronously separate fast
kinetochore microtubules shorten
spindle poles move apart

362
Q

telophase

A

chromosomes arrive at poles
nuclear envelope reassembles giving two new nuclei
nucleoli reappear (RNA synthesis begins)
initiation of plasma membrane cleavage

363
Q

cytokinesis

A

contractile ring is formed and mediates division of cell into two

364
Q

meiosis function

A

reduction division (becomes haploid)

reassortment of genes:
-independent segregation of chromosomes
-crossing over

365
Q

mechanism of meiosis

A

each homologue replicates to give two chromatids
exchange of material between non sister chromatids

366
Q

chiasmata

A

physical manifestations of crossing over
hold chromosomes together when crossing

367
Q

leptotene

A

chromosomes are unpaired fine threads consisting of two tightly bound sister chromatids

368
Q

zygotene

A

maternal and paternal homologs pair together to form bivalents

369
Q

pachytene

A

chromosomes thicken
crossing over occurs

370
Q

diplotene

A

homologs separate but are held together by chiasmata
crossovers can be counted and positions recorded

371
Q

diakinesis

A

bivalents more contracted

372
Q

stages of reassortment

A

leptotene
zygotene
pachytene
diplotene
diakinesis

373
Q

meiotic metaphase 1

A

kinetochore microtubules of sister chromatids point in same direction
function as one unit

374
Q

meiotic anaphase 1

A

non sister chromatids pulled apart
arms of sister chromatids become unglued

375
Q

meiotic metaphase 2

A

kinetochore of sister chromatids point in different directions

376
Q

meiotic anaphase 2

A

cohesins in centromere degraded
sister chromatids separate

377
Q

which required more cell divisions? sperm or egg?

378
Q

the cell divisions in an human egg produce…

A

polar bodies
to mainatin the amount of cytoplasm

379
Q

what direction is RNA synthesised

A

5’ to 3’

380
Q

ribosomes function

A

assemble strings of amino acids as instructed by mRNA

381
Q

how many codons can a ribosomes read at a time?

382
Q

tRNA structure

A

3 hairpin stem loop

383
Q

polyribosome

A

multiple ribosomes can be reading one strand of mRNA

384
Q

why is it important to define the start of the coding region?

A

it can shift the reading frame

385
Q

the genetic code is…

A

read in groups of 3 bases
read in 5’ to 3’
3 possible reading frames
amino acids are coded by codons
degenerate
universal

386
Q

mutation types

A

deletion
insertion
substitution/point mutation

387
Q

epigenetics effects…

388
Q

what are genes composed of?

A

structural information for a protein
regulatory sequences to expression

389
Q

general transcription factor mechanism

A

recognise and bind to gene promotor
recruit RNA polymerase
allow basal level transcription

390
Q

rates of transcription are controlled by…

A

enhancers
gene-specific transcription factors

391
Q

what signals from the environment interact with RNA polymerase

A

hormones
nutritional signals
environmental signals

392
Q

nucleosome structure

A

8 histones
approx 200 bp
high numbers of arginine and lysine to neutralise negative DNA

393
Q

histone tails can be modified by…

A

acetyl
methyl

(regulatory)

394
Q

the histone code

A

a layer of information overlaying the DNA
involved in turning genes on or off

395
Q

which enzymes families modify histone tails

A

histone acetyl transferases
histones de-acetylases

396
Q

factors that effect histone acetylation

A

therapeutic drugs
environmental factors
cell metabolism

397
Q

x-inactivation

A

random
occurs in inner cell mass of the blastocyst
passed onto cell generations
heritable epigenetic

398
Q

radio-

A

image using radiation

399
Q

graph/gram

400
Q

angio-

401
Q

arterio-

402
Q

veno-

403
Q

salpingo-

A

Fallopian tubes

404
Q

medium

A

different states of matter

405
Q

attenuation

A

anything that decreases the amplitude of a sound wave

406
Q

cholangio-

A

bile ducts

407
Q

hystero-

408
Q

arthero-

409
Q

cyst-

410
Q

non-ionising imaging

A

ultrasound
mri
doppler
endoscopy

411
Q

ionising imaging

A

x-rays
nuclear imaging
ct

412
Q

X-rays mechanism

A

bombarding tungsten anode with electrons

dense tissues- lighter
soft tissues- darker

413
Q

radiopaque

A

dense, white

414
Q

radiolucent

A

soft, dark

415
Q

posteroanterior projection

416
Q

anteroposterior radiographs

417
Q

contrast medium must be…

A

water soluble
non toxic
high density

418
Q

contract medium is used for

A

differentiating soft tissues
usually barium salts

419
Q

angiography uses…

A

iodine substances into blood

420
Q

ct mechanism

A

narrow beam of xrays aimed at patient and quickly rotated around the body
allows for soft tissues to be viewed
often contrast medium needed for abdomen or chest

421
Q

ultrasound mechanism

A

high frequency sound waves
travel through medium until hit one of a different consistency then echoed back
real time 2d image
bone reflects waves therefore white on uss

422
Q

attenuation

A

loss of energy from the system
greater = less signals received

423
Q

MRI mechanism

A

creates static magnetic field around patient
a secondary energy field is added perpendicular
this flips/rotates protons
secondary field then switched off
causes relaxation (return to original)
protons emit energy
is detected by machine and used to determine distribution
-no metal allowed
-contrast sometimes used

424
Q

fMRI used for

A

determines blood flow through brains

425
Q

endoscopy mechanism

A

via mouth
mucosa visualised
see gastric or duodenal ulcers

426
Q

bronchoscopy

A

trachea and bronchi

427
Q

nuclear imaging

A

most common radionuclides are technetium-99m (bones), iodine-123 (thyroid)
emit gamma rays which are detected
reflect function and morphology

428
Q

emission computer tomography

A

moving detector nuclear imaging

429
Q

radiography advantages

A

Bone and joint injuries shown clearly
Relatively cheap
Quick & portable
Patients relatively comfortable position

430
Q

radiography disadvantages

A

Safe however use of radiation may not be suitable for some
Lack of detail on soft tissues

431
Q

CT advantages

A

Better for soft tissue than conventional radiography
3D image
good clarity

432
Q

CT disadvantages

A

More radiation used than x- rays so shouldn’t be done too frequently.
Contrast media needed for abdomen and chest study
Relatively expensive & loud
claustrophobic

433
Q

USS advantages

A

Non-invasive
No harmful effects so can be used to evaluate growth & development of foetus
images viewed in real time
Good for soft tissue
Cheap & quick
Portable

434
Q

USS disadvantages

A

Fat & gas cause poor image quality.
Skilled operator needed for good image
Restricted to superficial structures

435
Q

MRI advantages

A

Good for tissue differentiation & soft tissue
No radiation
High resolution
non-invasive
No biological hazard

436
Q

MRi disadvantages

A

Expensive
Cannot be used on those with pacemakers or metal implants (magnetic)
Loud and long scan
Claustrophobic

437
Q

endoscopy advantages

A

real time
good detail

438
Q

endoscopy disadvantages

439
Q

nuclear advantages

A

can produce images that reflect function an morphology
Target particular tissues

440
Q

nuclear disadvantages

A

High radiation involved may not be suitable for some
Can not be used too often
Invasive due to administration of radionuclides

441
Q

intravenous anti peristaltic agents

A

minimise motion
delay clearing of contrast agent

442
Q

interventional radiography

A

minimally invasive treatment/diagnosis using small incisions

443
Q

What does the star protein regulate?

Hint-steroid hormone synthesis

A

Movement of cholesterol into the mitochondria
Where it is converted to pregnenolone

444
Q

What regulates star activity?

A

ACTH via cAMP

Medicine UOB (8 decks)

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