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1
Q

describe interphase

A

interphase
-G1 - rapid growth, new organelles produced. proteins involved in spindle formation produced.
-S1 - dna replication occurs. Histone proteins synthesised. centrosome replication
-G2 - chromosomes condense and become visible
energy stores accumulate and mitochondria numbers increases

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2
Q

describe mitosis

A

-prophase - chromatin cndenses to give chromosomes
centrosomes nucleate microtubules which migrate to the poles of the nuclues.

-prometaphase
nuclear membrane breaks down
microtubules invade nuclear space
chromatids attach to microtubules

-metaphase
chromosomes line up on equatorial plate

-anaphase
sister chromatids pulled to opposite sides of the nucleus by spindle fibre contraction

-Telophase
nuclear membrane reforms around poles
chromosomes decondense to reform chromatin
cytokinesis

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3
Q

how is genetic variation brought about?

A

recombination between non sister chromatids in meisos as homologous chromosomes pair up. pieces of dna break off and recombine on non sister chromatids.

random assortment. random way in which homologous chromosomes line up on equatorial plane.

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4
Q

what is non disjunction

A

failure of chromosome pairs to separate during meiosis 1 and sister chromatids in meiosis 2

can result in downs syndrome or monosomy ie turners where only one X chromosome

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5
Q

what is gonadal mosaicism? Give an example of a disease caused by this.

A

occurs when the precursor germline cells to ova/spermatazoon are a mixture of two or more genetically different cell lines due to mitotic error.

more than one set of genetic information is found in the sex cell.

example: duchenne muscular dystrophy

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6
Q

what are the classification of genetic disease?

A

mendelian

  • autosomal recessive
  • autosomal dominant
  • X linked

chromosomal
-abnormalities

non traditional

  • mitochondrial (from mother) abnormal
  • imprinting
  • gonadal mosaicism

multifactorial
-genetic and environmental interaction

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7
Q

what is imprinting?

A

when only one out of the 2 genes is active.

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8
Q

what is lyonisation?

A

in the female only one X chromosome is active. The other is inactive and forms a BARR body. This is to prevent having 2 sets of proteins derived from the X chromosomes, would be double that of the males.

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9
Q

what is the negative dominant effect?

A

mutation causing a protein which has a loss of a particular function however can somehow outcompete the endogenous protein.

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10
Q

how can a child have a disease but parents are unaffected?

A

gonadal mosacism

mother may have reduced penetrance / variable expression

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11
Q

define autosomal

A

chromosomes 1-22

excludes sex chromosomes

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12
Q

define locus

A

position of a gene/DNA on geentic map

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13
Q

define genotype

A

genetic constitiution of an individual

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14
Q

define phenotype

A

physical characteristics due to genotype and environment

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15
Q

define allele

A

one of the several alternative forms of a gene at a specific locus

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16
Q

define consanguinity

A

reproductive union between 2 relatives

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17
Q

define autozygosity

A

homozygous by descent. a result of consanguinity.

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18
Q

define homozygous

A

both alleles same at a locus

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19
Q

define heterozygous

A

alleles at same locus different

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20
Q

define hemizygous

A

describes a gene carried on an unpaired chromosome. ie X for men

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21
Q

define penetrance

A

proportion of people with gene or genotype who show expected phenotype.
may be complete (all) or incomplete (not all show it)

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22
Q

define variable expression

A

variation in clinical features of a genetic disorder between individuals with same gene alteration

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23
Q

define sex limitation

A

expression of a particular characteristic limited to one of the sexes

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24
Q

define multifactorial condition

A

diseases due to a combo of genetic and environmental factors

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25
Q

define late onset

A

condition not manifested at birth

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26
Q

define congenital

A

condition is manifested at birth

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27
Q

what are the types of tissue?

A 
epithelium 
supportive tissue (cartilage, bone, tendons,blood)
muscle
nerves
germ cells
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28
Q

describe the haemotoxylin and eosin stain

A

haemotoxylin stains acidic things blue, such as DNA, RNA, cell nuclei.

eosin stains alkaline things red. such as cytoplasm, colloidal proteins.

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29
Q

describe alcian blue

A

stains structures rich in glycosaminoglycans blue

ie mucous goblet cell, mast cell granules and cartilage matrix

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30
Q

describe iron haematoxylin

A

stains nuclei and elastic fibres black

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31
Q

describe periodic acid shift stain

A

stains hexose sugars magenta

stains goblet cell matrix, glycogens, basement membrane, glycocalyx

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32
Q

describe toludine blue

A

stains nuclei, ribosomes, cytoplasm dark blue

stains cartilage matrix, mast cell granules pale blue

stains GAG rich bright purple

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33
Q

describe the components of the cytoskeleton

A

made up of microtubules, intermediate filaments and microfilaments.

microtubules are 25 nm diameter
made from alpha and bets tubulin arranged in groups of 13 to form a hollow tube. all cells have except erythrocytes

intermediate filaments
10 nm diameter
6 types of protein. they are anchored to the transmembrane protein and spread tensile forces though tissues. many different types. ie cytokeratins for epithelial cells.

microfilaments are made from actin.
5 nm diameter
forms a mesh around inner surface of cell membrane

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34
Q

describe the components of the cytoskeleton

A

made up of microtubules, intermediate filaments and microfilaments.

microfilaments 5nm
made of actin filaments
used in muscle contraction
+ and - end. negative end anchored, positive end is able to grow and meet some other some cell structure, gives tensile strength and stability.

intermediate filaments 10nm
made from 6 different protein types. similar role to microfilaments. found in the nuclear lamina and outside the cytoplasm.

microtubules 23nm
made from alpha and beta TUBULIN globular protein filaments arranged in a tube. negative end of tubule attaches to the centrosome.
synthesise the spindle important in DNA replication
involved in transport

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35
Q

which 2 proteins interact to cause cilia bending?

A

tubulin and dynein

form the microtubules of the cilia. 9 peripheral doublets and a pair of central .

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36
Q

what is the general formula for carbohydrates?

A

Cn(H2O)n

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37
Q

what isomers can a monosaccaride form? which is the most common?

A

D & L isomers
D is the most common in sugars.
will rotate plane polarised light right

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38
Q

what is an Unsaturated fatty acid?

A

means it has one or more double carbon bonds. double bond commonly CIS (functional groups on same side of double bond)

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39
Q

what are the purines and pyrimines?

A

Adenine and thymine are purines
have 2 carbon nitrogenous ring

guanine and Cytosine are pyrimines
have only one carbon nitrogenous ring

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40
Q

what is the structure of a nucleotide?

A

ribose sugar in RNA, deoxyribose in DNA
phosphate
nitrogenous base

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41
Q

what bonds are found between the phosphate and sugar?

A

phosphodiester

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42
Q

what form are most amino acids found in?

A

the L enantiomer form

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43
Q

what is the difference between a protein and a peptide?

A

protein
greater than 50 aa
functional
synthesised by the cell

peptide - fragment of a protein
less than 50 aa

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44
Q

describe the structure of a protein

A

primary structure is the sequence of amino acids determined by the base sequence

secondary structure is the folding of the polypeptide chain into either alpha helix or beta pleated sheets.
in the alpha helix, every NH group donates the H to a CO group located 3/4 residues earlier on the protein sequence.

super secondary structure, the combination of secondary structures together

tertiary structure
complex shape formation as a result of bonds. ie disulfide, hydrogen, ionic, VDW, electrostatic, covalent

Quaternary structure is a 3D protein composed of several sub-units. 2 or more tertiary structures.

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45
Q

why can DNA polymerase only synthesis daughter DNA from 3’ to 5’ end?

A

DNA polymerase reads template DNA from 3’ end to 5’ end. Daughter DNA synthesised from 5’ end to 3’ end.
However 3’ end of template does not have a phosphate group, this is needed to provide energy for synthesis. Therefore daughter DNA synthesised starting from the 5’ end, phosphate group able to provide energy.

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46
Q

describe the process of DNA replication

A
  1. tropoisomerase unwinds DNA helix
  2. DNA helicase breaks hydrogen bonds exposing dna nucleotides behind the replication fork
  3. SSB (single strand binding proteins) coat the single strands preventing annealing.
  4. Primase enzyme makes a short DNA single strand primer complementary to each end of the 2 DNA strands.
  5. DNA polymerase can now begin adding free nucleotides to the exposed nucleotides. read strand in the 3’ to 5’ direction so synthesis of new DNA daughter strand from 5’ to 3’.
  6. one leading strang and one lagging strand. leading strand is the one where DNA polymerase is about to synthesis DNA continously and is moving towards replication fork following action of DNA helicase. lagging
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47
Q

describe the process of DNA replication

A
  1. tropoisomerase unwinds DNA helix
  2. DNA helicase breaks hydrogen bonds exposing dna nucleotides behind the replication fork
  3. SSB (single strand binding proteins) coat the single strands preventing annealing.
  4. Primase enzyme makes a short DNA single strand primer complementary to each end of the 2 DNA strands.
  5. DNA polymerase can now begin adding free nucleotides to the exposed nucleotides. read strand in the 3’ to 5’ direction so synthesis of new DNA daughter strand from 5’ to 3’.
  6. one leading strang and one lagging strand. leading strand is the one where DNA polymerase is about to synthesis DNA continously and is moving towards replication fork following action of DNA helicase. lagging strand is the one where DNA polymerase is moving away from DNA helicase, therefore must keep restarting to synthesise DNA on newly exposed template DNA.
  7. RNAseH removes primers. produced Okazaki fragments on the lagging strand
  8. DNA ligase connects fragements together.
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48
Q

what are the start and stop codons?

A

start AUG

stop UGA UAG UAA

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49
Q

How can one gene code for a variety of proteins

A

exon shuffling after introns are removed

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50
Q

what form are genes that are actively used in a cell in?

A

euchromatin

if not active, in heterochromatin form

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51
Q

describe a deletion mutation

A

deletion - in frame (whole codon is lost/1AA removed) or out of frame (whole sequence after mutation altered)

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52
Q

what is a splice site mutation

A

point mutation which affects the accurate removal of introns. introns may be translated

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53
Q

what is a non sense mutation

A

point mutation forming a stop codon. incomplete non functional protein.

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54
Q

what is a mis sense mutation

A

mis sense mutation - a point mutation, results in codon coding for a diff amino acid.

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55
Q

how many grams/kg is the triglyceride storage?

A

15 kg

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56
Q

how many grams/kg is the glycogen storage?

A

200 g in liver 150 g in muscle

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57
Q

how many grams/kg is the protein storage?

A

6kg

58
Q

at rest, what accounts for ATP production?

A

70% by lipid 30% by carbohydrates

59
Q

describe how fatty acids are brought into the mitochondrial inside the hepatocyte.

A

fatty acids must be activated before they can be used for beta oxidation.
fatty acid + ATP + CoA –> acyl CoA + PPi + AMP

Acyl CoA forms acyl carnitine using enzyme carnitine acyl transferase 1.

acyl carnitine transported into the matric

converted back to acyl CoA via enzyme carnitine acyl transferase 2. carnitine can diffuse back to outer membrane and re used. ‘Shuttle.’

60
Q

describe the beta oxidation of fatty acids

A
  1. double bond formation between alpha and beta carbon of fatty acyl CoA. Enzyme acyl CoA dehydrogenase. FADH2 formed.
  2. H20 added. OH added to beta carbon, H added to the alpha carbon. enzyme enoyl hydratase
  3. oxidation of beta carbon to a ketone. NADH+ H+ formation. enzyme: beta hydroxy acyl CoA dehydrogenase
  4. cleavage of alpha and beta bond. coA addition. acetyl coA formed and a shorter acyl coA which is recycled to start. enzyme beta keto thiolase.
61
Q

why is it debatable that 38 ATP are formed from respiration?

A

assumes all NADH+H+ and FADH2 used in oxidative phosphorylation
assumes all H+ ions are used for chemiosmosis.

62
Q

name 3 ketones

A

acetone
acetoacetate
b-hydroxybutyrate

63
Q

name the process of ketogenesis

A

acetyl coA + acetyl Coa
enzyme thiolase
form acetoacetyl CoA

acetoacetyl CoA forms 3-hydroxy-3-methylglutaryl CoA
enzyme HMG CoA synthase

HMG forms acetoacetate
enzyme HMG CoA lyase

acetoacetate can spontaneously be removed as acetate (people with high ketone count pear smelling breath) volatile so removed quickly.

or can be converted to Beta hydroxybutyrate. by enzyme d-b-hydroxybuyrate dehydrogenase

64
Q

why are liver cells unable to use ketone bodies as an energy source?

A

liver does not have enough of the enzyme succinyl CoA acetoacetate CoA.

this enables extrahepatic tissues to have access to ketone bodies in times of starvation.

65
Q

what happens when fat/carb levels are sparse?

A

muscle and cardiac tissues will use ketone bodies for energy production. this conserves any remaining glucose for the brain.

66
Q

how do extra hepatic tissues utilise ketones?

A

Can use ketones in the form of d-B-hydroxybutyrate or as acetoacetate.

d B hydroxybutyrate is converted to acetoacetate by enzyme d B hydroxybutyrate dehydrogenase.

acetoacetate is converted to acetoacetyl CoA by enzyme succinyl CoA acetoacetate CoA transferase.

acetoacetyl can be converted to 2 x acetyl CoA. This can be then used in Krebs.

67
Q

what happens in diabetes mellitus?

A

inability to take in glucose
liver synthesises more ketone bodies to supply tissues
production exceeds tissue ability to oxidise
ketones acidic
ph of blood drops
Hb binding ability decreases

68
Q

describe tight junctions

A

form a water tight connection between 2 adjacent cells. composed of protein CLAUDIN
prevents lateral movement of integral proteins on cell surface. ensures endocytosis and exocytosis occurs on appropriate side.
ensures selective transport as molecules must undergo transport.
found at lungs, bladder, intestine, kidney

69
Q

describe the adhering junctions

A

zonula adherens
lie underneath the tight/occluding junctions. Made of actin filaments. Gap between zona adherens and occluding junction is a protein called E cadherin which helps to join the adjacent cells.

macula adherens (desmosomes)
made up of intermediate filaments and KERATIN protein
usually found in combination with tight junctions
hold 2 cells together tightly, important for regions which undergo constant stretch such as the intestine or skin.
hemidesmosomes connect basal epithelial surface to basal lamina.

70
Q

describe gap junctions

A

connective tunnels, cylindrical. made of proteins called CONNEXINS. 2-4nm between 2 cells connected by a gap junction

found in cardiac cells where it allows Ca2+ to be able to diffuse rapidly between cells and propagate an action potential.

71
Q

name the common reactive oxygen species?

A

superoxide O2•-
hydrogen peroxide H2O2
hydroxl OH•

72
Q

how is superoxide radical formed?

A

from coenzyme Q action

or from metal containing enzyme action ie CP450

73
Q

how is the hydroxl radical formed?

A

Haber weiss

Fenton reaction

74
Q

why can ROS be dangerous?

A

Reactive free radical extract electrons (usually as hydrogen atoms) from other compounds to complete their own orbitals, thereby initiating free radical chain
reactions.

cause oxidative damage to proteins and DNA
damage to cell membranes
tissue damage

directly cause of emphysema, alcoholic liver disease, ageing, acute renal failure…

75
Q

what are the exogenous sources of ROS?

A 
UV 
tobacco 
drugs
pollutants
radiation
76
Q

what are the endogenous sources of ROS?

A 
mitochondria
peroxisomes
neutrophils
NADPH
electron transport chain
77
Q

what are the RNOS?

A

reactive nitrogen oxygen species

hypocholrous acid HOCl and nitric oxide NO

78
Q

how do cells protect themselves against ROS?

A

cell compartmentalization of free radicals
repair processes
defense enzymes
antioxidants which can terminate free radical chain rxn

79
Q

which enzyme can remove superoxide free radical?

A

superoxide dismutase

80
Q

which enzymes can remove H202?

which enzymes can remove hydroxyl radical?

A

catalase

glutathione peroxidase

81
Q

which antioxidants can protect against ROS?

A

C, E vitamins

flavanoids

82
Q

which ROS is most potent?

A

hydroxl OH•
lipid soluble
does lipid peroxidation

83
Q

what is oxidative stress

A

when rate of ROS formation exceeds tissue capability to remove

84
Q

how do you go from O2 to H20

A

O2 + e- → O2•-
O2•- + e- + 2H+ → H2O2
H202 +e- + H+ → OH• + H2O
OH• + e- + H+ → H20

85
Q

what is the fenton reaction

A

H2O2 + Fe2+ → Fe3+ + OH• + OH-

86
Q

what is the haber weiss reaction

A

H2O2 + O2•- → OH- + OH• + O2

87
Q

what is the respiratory burst

A

immune system defence against bacteria
rapid release of ROS superoxide
damages bacterial cell membrane

88
Q

describe the respiratory burst

A
  1. O2 → O2•-
    enzyme NADPH oxidase
    NADPH forms NADP+
  2. O2•- → H202
    sponatenous or via superoxide dismutase
  3. H202 forms HOCl via addition of Cl-
    enzyme myloperoxidase. HOCl kills bacteria
  4. or H2O2 forms OH• via fenton reaction
    (H202 + Fe2+ → Fe3+ + OH• + OH-)
    used to kill bacterium
89
Q

what is the haber weiss fenton cycle

A

Fe2+ + H2O2 → Fe3+ + OH- + OH• [Fenton reaction]

OH• + H2O2 → H2O + O2•– + H+

O2•– + H2O2 → O2 + OH• + OH-[Haber-weiss reaction]

Fe2+ + OH• + H+ → Fe3+ + H2O

90
Q

define karyotype

A

the number and appearance of chromosomes in a cell. spreads are arranged in order. biggest chromosome pair is number 1, smallest is number 22. sex chromosomes are 23.

91
Q

what percentage of body weight is water?

A

60% (42L)

92
Q

what is the main ion of ECF and ICF

A

ecf - Na+ (Cl-, HCO3-, Ca2+)

icf K+

93
Q

how is body water compartmentalised?

A

total body water 60% 42L
extracellular fluid 14L 20% Intracellular fluid 40%28L
plasma 3L - interstitial 10L - transcellular 1L

94
Q

what is transcellular fluid?

A

includes CSF and giestive juices

95
Q

what are the 3 types of hormones? describe each

A

peptide - short chain AA. large hydrophilic. bind to receptors. pre made and stored. rapid response. second messenger model. insulin , GH, TSH, ADH

steroid - synthesised from cholesterol. need to be bound to plasma protein to travel. made when needed, not stored. bind to receptor inside cell. slow response. testosterone, oestrogen, cortisol

amino acid derivative
synthesised from tyrosine
T3,T4, adrenaline

96
Q

define osmosis

A

the net movement of solvent molecules through a semi permeable membrane to an area of higher solute concentration

97
Q

define osmolality

A

measure of the number of dissolved particles in 1kg of liquid

98
Q

define osmolarity

A

measure of the number of dissolved particles in 1L of liquid

99
Q

define oncotic pressure

A

a form of osmotic pressure exerted by proteins, notably

albumin, in a blood vessel’s plasma (blood/liquid) that usually tends to pull water into the circulatory system.

100
Q

define osmotic pressure

A

the pressure that would have to be applied to a pure
solvent to prevent it from passing into a given solution by osmosis, often used to express the concentration of the solution.

101
Q

define hydrostatic pressure

A

the pressure difference between capillary blood plasma and interstitial fluid.

102
Q

define oedema

A

excess water in the intracellular space.

103
Q

how much kcal in carbohydrates, proteins,alcohol and lipids?

A

carbohydrate 4kcal/g
protein 4kcal/g
alcohol 7kcal/gram
lipid 9kcal/g

104
Q

what is BMR

A

basal metabolic rate
energy expenditure needed to stay alive at rest state
1kcal/kg body mass/hr

105
Q

what is the daily energy expenditure

A

energy needed to support BMR, physical activity and energy required to process food we eat

106
Q

what is exocytosis?

A

vesicle formed from the golgi apparatus
vesicle fuses with the cell surface membrane
for waste removal or secretion

107
Q

what is endocytosis?

A

energetic process to absorb molecules into a cell.
forms a vesicle (endosome).
ie phagocytes form a phagosome
ie pinocytosis engulfing liquid into a cell

108
Q

define acid and base

A

acid proton acceptor

base proton acceptor

109
Q

define buffer

A

weak acid or base along with its conjugate base or acid.

able to resist changes in pH on addition of a small amount of strong acid / base.

110
Q

what is the henderson hasselbach equation

A

ph = pka + log (HCO3- conc / CO2 conc)

111
Q

what is the optimum pH

A

7.4

range 7.35 - 7.45

112
Q

how is pH kept normal?

A

co2 excretion by lungs

renal function control H+/HCO3-

blood and tissue buffering. HCO3- and proteins act as buffers. ie Haemoglobin

113
Q

how is carbon dioxide transported in the blood

A

carbon dioxide from tissues enters the erythrocyte. Now has 3 options.

  • carboxyhaemoglobin formation with deoxy Hb
  • CO2 dissolves within RBC
  • CO2 combines with H20 to form carbonic acid (via carbonic anhydrase). H2CO3 dissociates to give H+ and HCO3-. HCO3- is transported out of the RBC in exchange for Cl-. This is the chloride shift, important as it maintains electroneutrality.

At tissues, Hb has high affinity for oxygen. Carbon dioxide is released. carbon dioxide diffuses into alveoli along its concentration gradient. removal of carbon dioxide shifts the equation to the left. HCO3- enters the RBC (and Cl- out). combines with H+ to form H2CO3 and co2 and water can be released.

114
Q

how is hydrogen transported in the blood?

A

at the cell, Hb02 releases the oxygen.

at the same time, co2 and h20 diffuse into RBC from cell.

formation of H2CO3. HCO3- taken out of cell in exchange for Cl- to maintain electroneutrality.

H+ combines with deoxy Hb to form HbH.

115
Q

what are the causes of respiratory acidosis?

A

hypoventilation - co2 retention
very high metabolic rate and carbon dioxide production - high fever

paCO2 >6kPA

116
Q

what are the causes of respiratory alkalosis?

A

hyperventilation due to anxiety/ pulmonary embolism or asthma
PaCO2 <4.5 kpa

117
Q

what are the causes of metabolic acidosis?

A

renal dysfunction - inability to reabsorb all HCO3- or inability to secrete H+

hypoaldosteroism - aldosterone increases Na+ absorption which is coupled to H+ secretion which ties into HCO3- reabsorption

excess acid production for example due to increased anaerobic acid caused by hypoxia. ie lactic acid.

diabetic acidosis - no insulin/no glucose/fatty acid used/converted to ketone/ketones are acidic/ H+ produced/acidosis

118
Q

what are the causes of metabolic alkalosis?

A

alkali ingestion
vomiting - loss of acid from gastric secretion
excessive HCO3- absorption - linked to Cl-. If Cl- levels fall (vomiting) there will be increased HCO3- reabsorption to maintain electroneutrality.

119
Q

what is the anion gap?

A

the difference in serum concentration between anions and cations.
excludes some ions such as K+ PO4- SO4-

normal: 3-11 mEq/mol

120
Q

how can we use the anion gap?

A

can diagnose cause of metabolic acidosis

121
Q

name the 3 types of cartilage

A

hyaline -trachea, synovial joints, larync
elastic - pinna, epiglottis
fibrous - intervetebral cartilage

122
Q

what are the 3 cell types of bone?

A

osteoblasts - synthesis
osteocytes - maintain and regulate Ca2+
osteoclasts - remodel break down

123
Q

what are the 2 bone types?

A

primary / woven - new bone

secondary - remodeled bone

124
Q

what are the 3 types of epithelium?

A

simple
stratified
pseudostratified

125
Q

name the 3 muscle types

A

cardiac
smooth/visceral
skeletal

126
Q

name 3 contractile cells

A

pericyte
myoepithelial
myofibroblast

127
Q

what is the basement membrane made from

A

collagen type 4

fibronectin

128
Q

what are the 3 types of connective tissue

A

fibrous loose /dense (tendon)
fatty (white adipose brown in babies)
hard (cartilage or bone)

129
Q

how many types of collagen are there?

A

12

130
Q

give an example where type I, II, III, IV, V collagen is found

A 
1 - skin/tendon/organ/bone
2 - cartilage
3- liver
4 basement membrane
5 placenta
131
Q

what is tropocollagen

A

triple helix of peptides

132
Q

what is the cause and consequence of hypernatraemia?

A

Osmotic Diuresis
dehydration
renal failure
diabetes insipidus (little response to ADH, lots of water lost. dehydration)

133
Q

what is the cause and consequence of hyponatraemia?

A

diuresis

134
Q

what is the cause and consequence of hypernatraemia?

A

Osmotic Diuresis (lots of water lost, Na high conc)
dehydration
renal failure
diabetes insipidus (little response to ADH, lots of water lost. dehydration)

cerebellar intracellular dehydration

135
Q

what is the cause and consequence of hyponatraemia?

A

diuresis
addisons disease
IV fluids
oedema

intracellular overhydration
headache
hypertension

136
Q

what is the cause and consequence of hypercalcaemia?

A

hyperparathyroidism
skeletal metastases
Tb

metastatic calcification
kidney stones

137
Q

what is the cause and consequence of hypocalcaemia?

A

vit D deficiency
Mg deficiency
renal disease

tetany (spasms)

138
Q

what is the cause and consequence of hyperkalaemia?

A

diuresis
addisons disease
acidosis

risk of MI, high K+ affects RMP of the myocytes

139
Q

what is the cause and consequence of hypokalaemia?

A

diarrhoea
vomiting
alkalosis
hypomagnesaemia

weakness and cardiac dysarrhythmia

140
Q

name the 4 types of cell surface glycoproteins

A

anchors
receptors
enzymes
transporters

IMMS (1 decks)

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