Erythropoiesis Flashcards

(41 cards)

1
Q

structure that enables RBCs to function

A

Hb carries O2
no nucleus so deformable and more room for Hb
high SA/ volume ratio
specialised membrane makes it flexible

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2
Q

what does the high oncotic pressure of RBCs risk?

A

draws water in so risks lysis

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3
Q

what does the oxygen rich environment of the RBC risk?

A

oxidation

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4
Q

adverse of RBCs having no nucleus?

A

unable to divide and replace damaged proteins so limited life span

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5
Q

adverse of no mitochondria in the RBC

A

limited to glycolysis for energy

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6
Q

how does the RBC keep water out?

A

Na+/K+ pump (needs ATP)

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7
Q

what makes the RBC membrane flexible?

A

lipid bilayer with lots of proteins makes it flexible

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8
Q

which molecule is a tetrameric globular protein?

A

Hb

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9
Q

what chains are present in adult Hb?

A

2 alpha

2 beta

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10
Q

what does the haem group consist of?

A

Fe2+ in a flat porphyrin ring (one haem per subgroup)

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11
Q

how many oxygen molecules can bind to Fe2+

A

1

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12
Q

how many oxygen molecules are there per Hb?

A

4

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13
Q

how many ml of oxygen can 1g Hb carry when fully saturated?

A

1.34ml

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14
Q

can Fe3+ bind oxygen?

A

no

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15
Q

describe the steps in formation of the Hb molecules

A
  1. iron/Fe2+ is transported to RBC cytosol
  2. combines with porphyrin ring (now called haem)
  3. combines with globin chain (alpha or beta)
  4. subunits combine
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16
Q

role of Hb

A

delivers oxygen to tissues
acts as a buffer for H+ (H+ can stick to it)
CO2 transport

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17
Q

what regulates production of RBCs in the bone marrow?

A

erythropoietin

18
Q

what produces erythropoietin?

19
Q

where does RBC destruction occur?

A

spleen (and liver)

20
Q

average lifespan of a RBC?

21
Q

what takes up aged RBCs?

22
Q

what are globin chains recycled to?

23
Q

what is the haem group recycled to?

A

iron and bilirubin

24
Q

how is bilirubin excreted?

A

taken to the liver, conjugated and excreted in bile (colours faeces and urine)

25
cascade of haem breakdown
haem > porphyrin > biliverdin > bilirubin
26
what can free radicals do to Fe2+?
oxidise it to Fe3+ (metHb)
27
what stops oxidation of Fe2+?
NADH in glycolysis
28
examples of reactive oxygen species
superoxide | hydrogen peroxide
29
what do reactive oxygen species have?
unpaired free electrons that are capable of interacting with molecules and damaging their structure
30
where is glutathione (GSH) found?
in RBCs
31
role of glutathione (GSH)?
protects from hydrogen peroxide by reacting with it to form water and an oxidised glutathione product (GSSG)
32
what replenishes the oxidised glutathione product GSSG?
NADPH generated by the hexose monophosphate shunt
33
what enzyme is involved in the hexose monophosphate shunt?
glucose-6-phosphate dehydrogenase (G6PD)
34
is G6PD X-linked?
yes
35
what happens if there is X-linked deficiency of G6PD?
boys will have low levels leading to impaired defence and oxidative damage
36
what shape is the oxygen dissociation curve?
sigmoidal
37
what is the allosteric effect?
when one oxygen binds to the Hb molecule it becomes easier for others to bind
38
foetal Hb oxygen dissociation curve
saturates more pO2 so shifts curve to the left
39
function of myoglobin?
in muscles it takes O2 from red cells
40
what produces 2,3-BPG?
Rapapoport-Lubering shunt
41
what increases 2,3-BPG?
chronic anaemia leading to increased oxygen release