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IMMS Flashcards

1
Q

what is lipofuscin?

A

a yello-brown pigment granule that is made up of residues from lysosomal digestion

it is thought to be a ‘wear and tear’ pigment

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2
Q

Cell membrane constituents

A
  • phospholipids
  • cholesterol
  • membrane proteins
  • carbohydrates
    • if attached to lipids called glycolipids
    • if attached to proteins called glycoproteins
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3
Q

Membrane composition by mass

A
  • 50% proteins
  • 40% lipids
  • 10% carbs
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4
Q

Functions of the cell membrane

A
  • anchor the cell to the ECM
  • connect cells together
  • regulate incoming and outgoing substances
  • recognise chemical messangers
  • form distinct border of cell
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5
Q

three types of cell junctions:

A
  • Anchoring junctions
  • Gap junctions
  • Tight junctions
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6
Q

Three types of anchoring Junctions

A

Desmosomes

Hemidesmosomes

Adherens

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7
Q

Parts of a G protein coupled receptor

A
  • the receptor
  • alpha
  • beta
  • gamma
  • an enzyme that makes the secondary messanger
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8
Q

Desmosomes: can you draw the diagram?

A
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9
Q

Tight junctions can you draw the diagram

A
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10
Q

Gap junctions - can you draw the diagram?

A

only small molecules and ions can pass through - not proteins

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11
Q

primary and secondary active transport

A
  • primary: energy derived directly from ATP
  • secondary: energy derived from coupling the transport of a substrate down its concentration gradient
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12
Q

3 different types of endocytosis

A
  1. Phagocytosis
    • pseudopodia engulf foreign particles in a phagosome
  2. Pinocytosis
    • Extracellular fluid is engulfed in an invagination of the membrane and fluid is taken into the cell
  3. Receptor mediated
    • Receptor binding causes an invagination of a coated pit
    • When vesicle is taken in to the cell it contains both the particle and its receptors
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13
Q

4 Glucose transporters

A
  • GLUT1:
    • bb barrier
    • erythrocytes
  • GLUT2:
    • renal tubular cells
    • pancreatic beta cells
    • basolateral surface of intestinal epithelia
    • Liver
      • bidirectional to release G during gluconeogenesis and take it up durign glycolysis
  • GLUT3:
    • neurons
  • GLUT4:
    • adipose tissue
    • striated muscle
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14
Q

Polymorphism Definition

A
  • Frequently hereditary variations at a locus - not pathogenic
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15
Q

Hemizygous Definition

A
  • When there is no allelic counterpart to a gene
  • e.g. X chromosome genes in a male
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16
Q

What is imprinting?

A
  • Mostly both alleles of a gene are expressed at once
  • Sometimes they’re imprinted meaning that only one allele is expressed
  • The expression of a gene depends on the parent who passed that gene on
  • It’s a normal part of development
  • prader-willi and angelman show this specific inheritance pattern because of imprinting
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17
Q

how to notate a translocation from band 24 of the q arm of chromosome 1 to band 12 on the q arm of chromosome 2?

A

t(1;2)(q24;p12)

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18
Q

How to notate an inversion between band 11 on the q arm of chormosome 7 and band 21 on the q arm of chromosome 7

A

inv(7)(q11;q21)

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19
Q

how to notate a duplication of a section of chromosome 11 between band 14 on the p arm and band 15 on the p arm?

A

dup(11)(p14;p15)

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20
Q
A
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21
Q

How to denote a deletion of a section of the q arm of chromosome 22 between band 11 and 12

A

del(22)(q11;q12)

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22
Q

FISH

A
  • Fluorescence in situ hybridisation
  • use fluorescent probe to hybridise with complementary sequence and visualise any rearrangements or deletions

microarrays are now used because they have better resolution

<200kb

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23
Q

Cell cycle very simply

A
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24
Q

Stages of Mitosis

A
  1. Prophase
  2. Prometaphase
  3. Metaphase
  4. Anaphase
  5. Telophase
  6. Cytokinesis
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25
Q

Prophase

A
  • centrosomes migrate to opposite poles of the cell
  • chromatin condenses
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26
Q

prometaphase

A
  • Nuclear membrane breaks down
  • microtubules from the centrosomes attach to chromatids
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27
Q

Metaphase

A
  • Chromasomes line up allong the equatorial plane
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28
Q

Anaphase

A
  • sister chromatids seperate and are pulled to opposite poles
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29
Q

Telophase

A
  • nuclear membrane reforms
  • chromosomes unfold
  • cytokinesis begins
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30
Q

When do meiotic divisions commence in males

A
  • they start at puberty
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31
Q

when does meiosis I occur in females

A
  • oogonia enter prophase I by 8th month of intrauterine life
  • meiosis I is only completed at ovulation 10-50 years later
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32
Q

when is meiosis II completed in females?

A
  • it is completed only after fertilisation producing one fertilized mature ovum and one polar body (the 3rd polar body to be produced)
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33
Q

Mendel’s 3 laws

A
  1. Law of segregation
  2. Law of independant assortment
  3. Law of dominance
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34
Q

Mendel’s 1st Law

A
  • the law of segregation
  • “During gamete formation, the alleles for each gene segregate from each other so that each gamete carries only one allele for each gene.”
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35
Q

Mendel’s 2nd Law

A
  • the law of independant assortment
  • “Genes for different traits can segregate independently during the formation of gametes.”
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36
Q

Mendel’s 3rd Law

A
  • The law of dominance
  • “Some alleles are dominant while others are recessive; an organism with at least one dominant allele will display the effect of the dominant allele.”
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37
Q

When does the non-dysjunction happen in trisomy 21?

A
  • mostly non-dysjunction at maternal Meiosis I
  • sometimes at maternal Meiosis II
  • very very rarely it’s paternal non-dysjunction
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38
Q

Gonadal Mosaicism

A
  • two populations of precursor germline cells (that go on to produce sperm or ova)
  • one of these populations is mutated
  • therefore the baby may have a genetic disease but the parent is fine
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39
Q

what is starch?

A
  • A combination of:
    • amylose (glucose 1-4 bonds)
    • amylopectin (1-4 and 1-6 side chains)
  • branched
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40
Q

Glycogen

A
  • Glucose polymer storage in animals
  • 1-4 glycosidic bonds and 1-6 branches
    • so just like amylopectin but glycogen has more branches
  • NB glycogenin is needed to prime the very beginning polymerisations in glycogen production
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41
Q

Steroids: basic structure

A
  • the steroid nucleus is 17 carbon atoms bonded into four rings
  • rings A,B and C are six member (cyclohexane) rings
  • ring D is a five member ring (cyclopentane)
  • carbon 17 on ring D binds to the variable group
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42
Q

Amino Acids

A
  • A central carbon bound to a carboxyl group, an amino group, a hydrogen and an R group
  • change charge depending on solution they’re in
  • make polypeptides by making peptide bonds
  • proteins are always written N terminus to C terminus
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43
Q

Purines and Pyrimidines

A
  • Purines have two rings
    • Adenine
    • Guanine
  • Pyrimidines only have one ring
    • Uracil
    • Cytosis
    • Thymine
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44
Q

number of bonds in base pairs

A
  • Cytosine –> Guanine
    • three bonds
  • Thymine –> Adenine
    • two bonds
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45
Q

where are disulphide bonds typical

A

between cysteine residues

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46
Q

The alpha helix

A
  • A secondary structure
  • helix formed by
    • H bonds between carbonyl group of one amino acid and the amino group of the amino acid 4 residues along
  • R groups look outwards
  • Proline can’t do this cause of its R group so it forms a kink
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47
Q

Beta sheet

A
  • formed by H bonds between linear regions of polypeptide chains
  • this can be between the same polypeptide or between different polypeptides
  • chains can e parallel or antiparallel
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48
Q

what is an isoenzyme

A

two or more enzymes that have identical function but different structure

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49
Q

Michaelis Menten Equation - can you draw the graph

A
  • Vi = initial velocity
  • Km = the substrate concentration when V is 1/2 Vmax
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50
Q

What is Heme

A
  • non-protein part of haemoglobin
  • it is a porphyrin ring with a central Fe
  • This Fe can bind O2
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51
Q

haemoglobin

A
  • the quaternary structure has four globular subunits
  • each subunit can carry one O2
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52
Q

Red blood cells in the tissues

A
  • CO2 from tissues enters the RBC
  • it combines with H2O and (via carbonic anhydrase) it forms carbonic acid
  • carbonic acid dissociates, releasing protons (and HCO3-)
  • the protons combine with HbO2 and kick off the O2
  • O2 is released into the tissues
  • this is why the curve shifts to the right when it’s acidic
  • in acidic media, high protonation inhibits O2 binding
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53
Q

Red blood cells in the lungs

A
  • O2 enters the red blood cells
  • at such a high pO2 it binds the protonated Hb (HHb) and kicks off the proton
  • the proton combines with bicarbonate (HCO3-) forming carbonic acid
  • carbonic acid is cleaved by carbonic anhydrase into CO2 and H2O
  • the CO2 is exhaled
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54
Q

How does the temperature and arterial carbon dioxide influence the oxygen dissociation curve

A
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55
Q

Simple antibody structure

A
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56
Q

which way does DNA polymerase go?

A
  • it reads the transcript 3’ to 5’ but it prints 5’ to 3’
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57
Q

how much is a kilodalton

A
  • 1000 daltons
  • 1000 atomic mass units
  • one dalton is the mass of one hydrogen atom
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58
Q

start codon

A

AUG

remember there aren’t any start codons in DNA, only in mRNA

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59
Q

what is haploinsufficiency?

A

this is when a pathway is very sensitive to the amount of gene product produced so a loss of function mutation can be inherited in a dominant pattern

haploinsufficiency = half is not enough

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60
Q

stop codons

A

UGA, UAG, UAA

remember: there aren’t any start codons in DNA they’re only in DNA

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61
Q

Initiating transcription

A
  • we need heterochromatin to turn to euchromatin
  • TFs bind promotor sequences which are just 5’ of the first exon
  • transcription complex forms at the TATA box (just 5’ of the first exon)
  • the helix opens and the DNA seperates
  • RNA polymerase II starts to build mRNA
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62
Q

Name a disease caused by a deletion mutation

A
  • duchennes muscular dystrophy
    • caused by an out of frame deletion which results in a severely truncated dystrophin protein
    • this causes progressive muscle damage in boys
  • the much milder becker musclular dystrophy is caused by an in frame deletion
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63
Q

Splice site variations

A
  • splice acceptor sites are either side of the intron that should be excluded
    • remember: coding exons are INterupted by INtrons
  • if these sites are mutated then splicing won’t happen properly and this will result in an included intron
  • this will likely have an effect on protein function
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64
Q

missense mutation

A
  • a point mutation that results in a different amino acid
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65
Q

Non-sense mutation

A
  • out of frame mutation causes a premature stop codon
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66
Q

what is allelic heterogeneity

A
  • it is when many different variants in one gene can cause the same disease
  • this is seen with cystic fibrosis
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67
Q

locus heterogeneity

A

variants in different genes cause the same clinical condition

68
Q

mechanisms of dominance

A
  1. gain of function mutations
  2. dominant negative mutations
    • the abnormal allele affects the functionality of the wild type allele within the same cell
  3. loss of function mutations if:
    • there is only one functional allele present
    • the pathway is very sensitive to the amount of gene product produced
69
Q

Types of Diagnostic Test

A
  • Diagnostic
    • patient has symptoms
  • Predictive
    • no symptoms - testing at risk family members for varient known to be in family
  • Carrier
    • for reproductive decision making
  • Pre-natal
  • Screening
  • Pre-implantation genetic diagnosis
  • Susceptibility
    • testing for increased or decreased risk of a multi-factorial condition
70
Q

Common chromosomal anomalies

A
  • Translocations
  • Inversions
    • paracentric
    • pericentric - crosses centromere
  • Deletions
  • Duplications
    • tandem
    • inverted
  • Ring chromosome
71
Q

what is autozygosity

A
  • homozygosity by inheriting the same mutation through two branches of the same family due to consanguinity
72
Q

what is penetrance

A
  • The percentage of individuals with a specific genotype showing the expected phenotype
73
Q

what is lyonisation

A
  • X inactivation
  • generally, only one of the two x chromosomes is active in a female cell
74
Q

what is homoplasmy

A

when all the copies of mitochondrial DNA in a cell are identical

75
Q

what is heteroplasmy?

A
  • this is when the copies of mitochondrial DNA within a cell are non-identical
  • the levels of heteroplasmy vary from tissue to tissue and from person to person
76
Q

what is the concordance rate?

A
  • in a twin study it is the % of twins that both have a condition
  • higher concordance rate in DZ than MZ indicates a genetic factor
77
Q

summarise the liability threshold model

A

At the point an individual accumulates a certain liability they will be affected by the disorder, the level of liability at which this occurs is referred to as the threshold level.

78
Q

Hereditability

A

the proportion of the aetiology of a disease that can be ascribed to genetic factors

79
Q

what do GWAS do

A
  • genome wide association studies
  • compare frequency of certain markers in patient populations and control populations
80
Q

what is the formula for BMI

A

BMI = weight/(height2)

81
Q

how much energy per gram of dietary fuel?

A
  • Lipids = 9kcal/g
  • Alcohol = 7kcal/g
  • Carbohydrates = 4kcal/g
  • Protein = 4kcal/g
82
Q

what is BMR

A

the amount of energy required to carry out the body’s basic functions at rest

these functions include:

  • respiration
  • contraction of heart muscles
  • repairing and regenerating tissues
  • maintaining ion gradients across membranes
83
Q

what are the conditions for measuring BMR

A
  • 12 hr fast
  • lying still and at mental rest
  • no tea, coffee, nicotine or alcohol for the last 12 hours
  • no heavy physical activity the previous day
84
Q

what would decrease BMR?

A
  • being underweight
  • being older
  • hypothyroidism
  • starvation
  • being a woman
  • having a reduced muscle mass
85
Q

Factors that would increase BMR

A
  • higher body weight
  • hyperthyroidism
  • low surrounding temperature
  • fever/infection
  • regular exercise
  • pregnancy and lactation
86
Q

what is normal BMR approximately?

A

1kcal/kg of body mass/hour

87
Q

what is the advised calorie intake per day?

A

25-35 kcal/kg/day

88
Q

how much glycogen is stored in the liver and the muscle?

A

200g in liver

150g in muscle

89
Q

what is malnutrition?

A

A state of nutrition with a

deficiency, excess or imbalance of

energy, protein or other nutrients,

causing measurable adverse effects

90
Q

what are the effects of insulin in the fed state?

A
  • Adipose tissue
    • stops the breakdown of TGs into free fatty acids
  • Liver
    • promotes the conversion of glucose into fatty acids and glycogen
  • Body cells
    • causes uptake of glucose
    • causes uptake of phosphate
91
Q

how many grams of glucose does the brain require per day?

92
Q

refeeding syndrome

A
  • sudden reinstitution of nutrition to starved patients
  • insulin spike causes increased fat and glycogen synthesis
    • requires ATP and therefore phosphates
  • the patient is usually depleted in phosphates
  • BMR increases
  • the patient becomes so depleted in ATP that there is widespread cellular failure
  • cardiac, pulmonary and neuro symptoms
93
Q

what are the essential fatty acids

A

omega 3 and omega 6

94
Q

which are the essential amino acids

A
  • histidine
  • Isoleucine
  • Leucine
  • tryptophan
  • lysine
  • methionine
  • phenylalanine
  • threonine
  • valine

Mnemonic: Help in learning these little molecules proves truly valuable

95
Q

what is the net reaction of glycolysis?

A

Gluc + 2NAD+ +2Pi +2ADP –> 2 Pyruvate +2NADH +4H+ +2ATP + 2H2O

glucose is oxidised

96
Q

where does glycolysis occur?

A
  • glycolysis occurs in the cytoplasm of the cell
97
Q

what is the rate limiting enzyme in glycolysis?

A

phosphofructokinase

98
Q

what is the overall reaction of the Krebs cycle?

A

acetyl-CoA +3NAD+ + FAD + ADP + Pi + 2H2O

–>

2CO2 + 3NADH + FADH2 + ATP + H+ + CoA

99
Q

where does the Krebs cycle occur?

A
  • the matrix of the mitochondria
100
Q

where does oxidative phosphorylation occur?

A

across the inner mitochondrial membrane

101
Q

Fatty acid activation

A
  • before they can be used for B oxidation, fatty acids must be activated (turned into acyl-CoA)
  • this happens in the cytoplasm
  • Activation:
    1. add adenosine from ATP to create aycl adenylate
      • the ATP provides the energy for the next step
    2. add an CoA (using enzyme acyl-CoA synthetase) to make acyl-CoA
      • the adenyl group is replaced by a CoA so this process releases AMP
102
Q

getting acyl CoA into the mitochondria for B oxidation

A
  • if the acyl CoA has fewer than 12 carbons then it can just diffuse across the membrane
  • most dietary fats have more than 14 carbons
  • SO the Carnitine Shuttle is needed:
    1. Acyl-CoA interacts with an enzyme called carnitine acyl transferase I located on the outer mitochondrial membrane
    2. carnitine acyl transferase I replaces the CoA with a carnitine (making acyl-carnitine) and in so doing moves the acyl into the intermembrane space
    3. acyl carnitine can then pass through the inner membrane through the carnitine transporter
    4. CoA is reattached and the carnitine pulled off (using carnitine acyl transferase II enzyme)
    5. carnitine is shuttled back across the membrane to begin the process again
103
Q

where are ketones made, why, from what and what are they called?

A
  • ketones are made in the liver
  • they are made from acetyl-Coa (when the level of fatty acid oxidation overwhelms the TCA cycle)
  • the ketones produced are:
    • acetone
    • B-hydroxybutyrate
    • acetoacetate
104
Q

which tissues use ketone bodies and how

A
  • ectra hepatic tissues can use ketones by first converting it to acetoacetyl-CoA
  • this conversion requires the enzyme acetoacetate:succinyl-CoA transferase
  • this is found in all tissues but the liver
105
Q

Diabetic Ketoacidosis can you draw the diagram

A

excess ketones cause acidosis because they are acidic in solution

106
Q

alcoholic ketoacidosis - can you draw the diagram?

107
Q

how much water is there in the body in terms of number of litres and % of body weight

A
  • water is 60% of body weight
  • approx 42L
108
Q

how much of the body’s fluid is intracellular and how much is extracellular (in litres)

A

intracellular = 28L

extracellular = 14L

109
Q

how much of the extracellular fluid is intravascular and how much is interstitial?

A

Intravascular = 3L

Interstitial = 11L

110
Q

what are the predominant electrolytes in the ICF

111
Q

what are the predominant electrolytes in the ECF

A

Na+, CL-, HCO3- and Ca2+

112
Q

what are the sequences of events that follow water deprivation

A
  • the ECF osmolality increases
  • this is sensed by osmoreceptors in the hypothalamus
    • these cause the release of ADH from the posterior pituitary
    • it also causes us to increase our water intake
  • the ADH causes renal water retention
  • overall this restores the ECF osmolality
113
Q

Causes of water depletion

A
  • D&V
  • Diuresis
  • Diabetes - glucose moves into lumen of the nephron and water moves with it
  • Elderly
    • loss of ability to reach water
    • loss of drive to drink
114
Q

Consiquences of over hydration

A
  • Hyponatraemia
  • Cerebral over hydration
    • headache
    • confusion
    • convulsions

But a normal healthy adult could drink 24 litres in a day and be fine

115
Q

what is hydrostatic pressure?

A
  • it is the pressure difference between plasma and interstitial fluid
116
Q

what is oncotic pressure

A

it is the pressure caused by the difference in protein concentraton between the plasma and interstitial fluid

117
Q

What are the four different types of oedema

A
  • lymphatic
    • lymphatic system normally returns interstitial fluid to the blood stream
    • if this is compromised it can cause oedema
  • hypoalbuminaemic
    • malnutrition –> loss of oncotic pressure
  • venous
    • water not reabsorbed at the venous end because the high hydrostatic pressure overcomes the oncotic pressure
  • inflammatory
    • histamine release - capillary endothelial cells seperate
    • water AND albumin leave the capillary
      • no oncotic pressure to bring the water back
118
Q

How much liquid is there usually in the pleural space?

119
Q

what is transudate?

A

fluid pushed out of a capillary due to high pressure

this is low protein because it’s just water moving across

120
Q

what is exudate?

A
  • fluid that leaks in between cells of the capillary due to their increased spacing

this is why you more associate this word with infection

exudate is high pressure cause protein moves out too

121
Q

autocrine, endocrine and paracrine

A
  • Autocrine – cells messaging themselves
  • Paracrine – cells talking to neighbouring cells
  • Endocrine – cells talking to other cells elsewhere in the body – signals often travel in the blood
122
Q

6 main hypothalamic hormones

A
  • Gonadotrophin-releasign hormone (GnRH)
  • Growth hormone releasing hormone (GHRH)
  • Somatostatin (SS)
  • Thyrotropin releasing hormone (TRH)
  • Corticotropin-releasing hormone (CRH)
  • Dopamine (DA)
124
Q

6 main pituitary hormones

A
  • FSH
  • LH
  • Thyroid stimulating hormone (TSH)
  • Growth hormone
  • Prolactin
  • adrenocorticotrophic hormone (ACTH)
    • causes cortex of the adrenal gland to secrete cortisol
125
Q

where does pyruvate get used (for energy) in aerobic conditions and how does it get there?

A
  • it is used in the mattrix of the mitochondria
  • it is converted into acetyl CoA for the krebs cycle
  • it can pass through the outer mitochondrial membrane quite easily
  • it enters the matrix of the mitochondria through the pyruvate transporter protein
126
Q

how is pyruvate converted into acetyl CoA?

A
  • happens in the matrix of the mitochondria
  • the pyruvate dehydrogenase enzyme complex is used
  • this uses a CoA
  • it also converts NAD to NADH
  • CO2 is given off because:
    • Acetyl-CoA is a two carbon molecule
    • Pyruvate is a 3 carbon molecule
127
Q

draw out full glycolysis

A

add a picture from your notes here or check against notes

128
Q

what is the enzyme used instead of hexokinase in the liver?

A
  • glucokinase
129
Q

what are the inhibitors and activators of PFK1

A
  • Inhibitors
    • ATP
      • we want less glycolysis if we already have lots of ATP
    • Citrate
      • we want less glycolysis if krebs is backed up
  • Activators
    • AMP
      • when cell is low on ATP it converts 2ADP to 1ATP and 1AMP
      • therefore AMP is a marker of low ATP
130
Q

how can glycogen be broken down and used for glycolysis

A
  • glycogen phosphorylase
    • this enzyme breaks off a glucose monomer from glycogen and adds an inorganic phosphate
    • this gives us Glucose-1-phosphate
  • Phosphogluco mutase
    • this enzyme then converts the glucose-1-phosphate into glucose-6-phosphate
  • it can then enter glycolysis
131
Q

Draw out the Krebs Cycle

132
Q

what is the rate limiting enzyme of the krebs cycle

A

isocitrate dehydrogenase

133
Q

citrate synthase is mainly inhibited by what?

A

there being too much citrate

therefore isocitrate dehydrogenase is a key regulator of citrate synthase and the whole krebs cycle

NB because PFK1 is inhibited by citrate, isocitrate dehydrogenase also regulates glycolysis

134
Q

what activates and inhibits isocitrate dehydrogenase

A

it is the irreversable step of krebs so has to be tightly monitored to avoid isocitrate depletion

Activated by substrates:

  • isocitrate
  • NAD

Inhibited by

  • ATP
  • alpha ketoglutarate
  • NADH
135
Q

what is alpha-ketoglutarate dehydrogenase inhibited by

A
  • succonly CoA
  • ATP
  • NADH
136
Q

what is the main regulator of entry into the Krebs cycle and what is it regulated by

A

the main regulator is pyruvate dehydrogenase

it is inhibited by ATP, NADH and Acetyl-CoA

it is activated by pyruvate and ADP

137
Q

electron transport chain overall

A
  • Electrons are donated by electron carriers (NADH or FADH2) and passed along the electron transport chain.
  • Each complex they pass pumps H+ into the intermembrane space.
  • ATP synthetase then allows H+ to come back into the matrix down the electrochemical gradient.
  • For every 4 H+ that pass through the ATP synthetase, one ATP is produced
  • Final electron acceptor is 1/2 O2 which forms H2O with the protons pumped back into the matrix
138
Q

What are the names of the electron transport chain proteins

A
  • Complex I/NADH dehydrogenase
  • Complex II/Succinate dehydrogenase
  • Complex III/Cytochrome C reductase
  • Complex IV/Cytochrome C oxidase
  • There’s also coenzyme Q10 which is associated to complex II
139
Q

how many protons are pumped into the intermembrane space when NADH is used as the electron carrier

A
  • Two electrons are donated to complex 1
  • Complex I pumps out 4 protons
  • Complex III pumps out 4 protons
  • And complex IV passes out 2 protons
  • So overall 1 NADH pumps 10 protons across the membrane
140
Q

how many protons are pumped into the intermembrane space when FADH2 is used as the electron carrier

A
  • Two electrons are donated to complex Q10
  • Q10 passes the electrons to Complex III which pumps out 4 protons
  • They are passed to complex IV which pumps out 2 protons
  • In total 6 protons are pumped across the membrane
141
Q

what’s the reaction sequence of fatty acid synthesis and fatty acid degradation

A
  • synthesis: condensation –> reduction –> dehydration –> reduction
  • degradation: oxidation –> hydration –> oxidation –> thiolysis (cleavage)
142
Q

draw out fatty acid oxidation

A

check against your own diagrams

143
Q

draw out ketogenesis

144
Q

what does topoisomerase do?

A
  • it unwinds the supercoiling of the DNA ahead of the replication fork
145
Q

What does helicase do?

A
  • it breaks down the hydrogen bonds between the two DNA strands and produces single stranded DNA
146
Q

what do ssb proteins do?

A
  • single strand binding protiens attach to single stranded DNA and prevent the two strands from rejoining
147
Q

What does DNA polymerase do?

A
  • it reads strands from 3’ to 5’ and prints the DNA 5’ to 3’
148
Q

what is the leading strand

A

this is the continuous strand of synthesised DNA

149
Q

what is the lagging strand?

A
  • this is the discontinuous strand as DNA polymerase can only read and print in one direction.
  • okozaki fragments are made
150
Q

what joins the okozaki fragments

A

DNA ligase

151
Q

briefly summarise protein synthesis

A

Transcription

  • Takes place in the nucleus
  • Topoisomerase unwinds DNA strand
  • RNA polymerase works across strand of DNA and produces strand of mRNA (this is read 3’ to 5’)
  • mRNA strand passes through nuclear pores into the cytosol and then onto a ribosome to be translated

Translation

  • Takes place on ribosomes
  • tRNA carries a specific anticodon to the corresponding codon on the mRNA – there is a specific amino acid attached to tRNA
  • This produces a chain of amino acids which are held temporarily by hydrogen bonds before peptide bonds are formed
152
Q

how are fatty acids activated and where

A

by acetyl-Coa cynthetase

in the cytoplasm

153
Q

how is acyl coA transported into the matrix of the mitochondria

154
Q

what are the three regions of the nucleolus?

A

the fibrillar centre

the dense fibrillar centre

the granular region

155
Q

3 types of cartilage and where they are found

A

Hyaline - most common found in the trachea ribs and nose

Fibrocartilage - foundin joint capsules and menisci

Elastic cartilage - external ear and epiglottis

156
Q

How many types of collagen are there and which are the ones to learn and where are those ones found?

A
  • there are at least 12 types
  • but we’re only learning 1-5
  • I: skin, bone, teeth and capsules of organs
  • II: cartilage
  • III (reticulin): liver, kidney, spleen, arteries, uterus
  • IV: basement membranes
  • V: placenta
157
Q

spermatogenesis meiosis can you draw the diagram?

158
Q

Oogenesis can you draw the diagram?

159
Q

where is dehydration in the body detected?

A

in the osmoreceptors of the hypothalamus

these then send signals via the supraoptic nuceleus to the posterior pituitary to release ADH

160
Q

what are the net products of glycolysis

A

2 NADH, 2 ATP and 2 Pyruvate

161
Q

Net products of 1 cycle of the krebs cycle

A

1 ATP

3 NADH

1 FADH

2 CO2

162
Q

what is the total theorhetical yield in ATP of one molecule of glucose?

163
Q

Dissociation of acids and bases and what are buffers?

(peer teaching slide)

164
Q

two things that could cause hyponatremia

A

water overload from IV fluids

Na+ loss through diuretics

165
Q

Two things that could cause hypernatremia

A

Too much sodium due to Hyperaldosteronism

dehydration

166
Q

What are ROS and which is the most potent one?

A

they are chemically reactive molecules derived from oxygen that contain a free radical

the most potent is hydroxyl (OH•) which is used in the respiratory burst of phagocytes

167
Q

What is the PAS stain used for

A

to see polysaccharides such as glycogen

EM: (14 decks)

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