2. Haemoglobin and RBCs Flashcards

1
Q

what does the RBC not have

A

Nucleus
Mitochondria,
Ribosomes

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2
Q

benefits of giv ing these up

A
  • Efficient and stable – nothing unnecessary
  • Room for haemoglobin
  • Unattractive to infecting organisms
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3
Q

downsides of giving these things up

A

No nucleus: No capacity for to making mRNA – no new protein

No Mitochondria no TCA cycle – limits the capacity to generate ATP or reducing power - vulnerable

No Ribosomes no translation of mRNA no protein synthesis

Cant self repair or go through apoptosis due to lack of protein synth + mitochond (needs to be removed by spleen)

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4
Q

key parts of the RBC memb

A

alpha spectrin
ankyrin

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5
Q

what can shortage of spectrin cause

A

eliptical shape

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6
Q

if cells cant apoptosis or self repair, then what happens to prevent toxicity

A

temporary fixing of the membrane

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7
Q

why is RBC damage toxic

A

Hb leakage is highly toxic = aggregates and blocks kidneys

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8
Q

what can fibrin strands formed by sepsis cause

A

acts like cheese wire
slices RBCs

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9
Q

how does cell repair after slicing damage

A

forms vacules
vacuole will pop but reseal
cytoskeleton forms and seals the membrane

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10
Q

what are these slicing damaged cells called

A

keratocytes

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11
Q

what forms after damage repair caused by diffuse damage

A

spherocytes

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12
Q

what does defect in memb prtoeins e.g. enykrin cause

A

hereditary spherocytosis

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13
Q

hereditary spherocytosis

A
  • unstable cell memb
  • lotsa spherocytes
  • anaemia due to breakdown of RBCs
  • mild jaundice and gall stones (due to release of RBCs)
  • enlarged spleen
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14
Q

2 things that allow the sigmoid curve

A

haem = O2 binding element
globin= surrounding protein element

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15
Q

what kind of structure does haem have

A

porphyrin

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16
Q

what do the 2 remaining interaction sites in Fe allow

A

fixing the molecule to the globin protein
and binding the O2

17
Q

if hb was single chained, what type of O2 release would it be

A

hyperbolic
O2 only released in sever hypoxia

18
Q

loose and tight conform of globin

A
  • loose binds o2 tightly
  • tight gives up O2 easily
19
Q

factors that influence tight and relaxed conforms of globin molecules

A

pH
CO2
metabolic products

20
Q

why does foetal Hb have higher affinity for O2

A

doesnt bind 2,3 DPG
so the HbF can compete with mothers Hb, and win
so O2 goes from mum to foetus

21
Q

2 stages of malaria development you shoud know

A

trophozoites
schizonts

22
Q

when did malaria start affecting humans

A

10,000 yrs ago during agriculture and stuff
but RBC was fully evolved by this time

23
Q

how is malaria able to survive

A

is protected from immune system in RBC
and metabolises the Hb for energy

24
Q

4 things that can provide protection from malaria

A
  • Sickle cell
  • beta thalassaemia
  • G6PD deficiency
  • Hb C (mild form of sickle cell)
25
Q

what ishow does a RBC produce reducing power (NADPH)

A

via hexose monophosphate shunt

26
Q

what is an essential component of hexose monophosphate shuint

A

G6PD

27
Q

how does G6PD deficiency provide malarial protection

A
  • high oxidative stress and the cell cant deal with it (not enough reducing power)
  • so RBC destroyed
  • It is thought that if malaria parasites invade a cell with G6PD deficiency then oxidation occurs leading to early destruction of the infected cell.
28
Q
A