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Haematology > Red Cells > Flashcards

Red Cells Flashcards

1
Q

RBC has no nucleus but has mitochondria. T/F?

A

False - yes no nucleus but has no mitochondria

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2
Q

What are RBC full of?

A

membrane full of haemoglobin molecules

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3
Q

What is a consequence of RBC being full of haemoglobin? (2)

A

high oncotic pressure so likes to draw water in,

oxygen rich environment so high oxidation risk

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4
Q

What is a consequence of RBC having no nucleus?

A

can’t divide or replace damaged parts so short life span

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5
Q

What is a consequence of RBC having no mitochondria?

A

Limited to glycolysis for energy generation

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6
Q

What is a consequence of RBC having high surface area/volume ratio?

A

need to keep water out

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7
Q

Proteins in RBC membrane help its structure how?

A

help make it flexible

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8
Q

How are ion concentrations maintained by RBC membrane?

A

sodium-potassium pump keeps water out

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9
Q

Haemoglobin structure - what is structure?

A

tetrameric globular protein

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10
Q

What is difference between adult and child haemoglobin structure?

A

Adult has 2 alpha and 2 beta chains whereas child has 2 alpha and 2 gamma chains

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11
Q

Which part (haem or globin) are the discs and which are the protein wormy chain structures?

A

Haem are discs and globin are protein wormy chain structures

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12
Q

There is one heme group per subgroup of haemoglobin. What is a heme group made up of?

A

Fe2+ in a flat porphyrin ring

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13
Q

When one oxygen molecule binds to one Fe2+, it is oxidised to become what?

A

Fe3+ -> therefore Fe3+ cannot take on oxygen

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14
Q

ferrous or ferric meaning?

A

Ferrous good - Fe2+,

ferric bad - Fe3+ so can’t carry oxygen

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15
Q

Haemoglobin functions? (3)

A

deliver oxygen to tissues,
act as a buffer for H+,
CO2 transport

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16
Q

Erythrocytes begin as what type of cell - common myeloid progenitors or common lymphoid progenitor?

A

Common myeloid progenitor

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17
Q

What controls erythropoiesis?

A

Oxygen - sensed by juxtaglomerular cells in kidneys, then produce erythropoietin

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18
Q

What cells sense and breakdown damaged RBCs?

A

Macrophages in the spleen

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19
Q

What happens to nucleus size in RBC production?

A

nucleus size starts out really big then as cell divides more and more it gets smaller and then disappears

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20
Q

Average life span RBC?

A

120 days

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21
Q

Macrophages recycle the products of RBC after breakdown. What does it do with globin?

A

Recycles globin chains in to amino acids,

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22
Q

Macrophages recycle the products of RBC after breakdown. What does it do with heme group?

A

heme group broken down into iron and porphyrin ring, porphyrin ring degraded into bilirubin, bilirubin is then taken to liver and conjugated and excreted in bile (colours faeces and urine)

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23
Q

Iron is stored as what?

A

Ferritin

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24
Q

Iron is transferred bound to what molecule?

A

Transferrin

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25
Q

What process does RBC use to get ATP?

what molecule is generated from glucose? How many ATP used and how many ATP generated?

A

Glycolysis - glucose to pyruvate, use up 2 ATP, generate 4 ATP, 1 NADH

26
Q

Oxygen free radicals easily generated in RBCs, why are these dangerous? (2)

A

Can oxidise Fe2+ to Fe3+ which doesn’t transport oxygen,

can damage proteins

27
Q

How is Fe2+ stopped from becoming Fe3+?

A

NADH from glycolysis pathway acts as an electron donor preventing oxidation of Fe2+ from becoming Fe3+ and generates NAD+ in the process to be uses again

28
Q

How is oxidative damage to cellular enzymes and Hb from free radicals prevented?

A

glutathione (GSH) reacts with free radicals (e.g. hydrogen peroxide) to form water and an oxidised glutathione product

29
Q

Glutathione is replenished by what molecule?

A

NADPH

30
Q

What is the rate limiting enzyme in the NADPH regeneration process?

A

glucose-6-phosphate dehydrogenase

31
Q

Hexose monophsophate shunt is responsible for what?

A

Generates NADPH that maintains GSH levels preventing oxidative damage

32
Q

What enzyme is X-linked that can lead to free radical increase and premature haemolysis?

A

glucose-6-phosphate dehydrogenase (G6PD)

33
Q

How is CO2 buffered for transport by RBCs?

A

H+ from broken down CO2 buffered by deoxygenated Hb

34
Q

CO2 transported in what 3 forms and percentage of CO2 transported each way?

A

10% dissolved,
30% bound directly to Hb,
60% as bicarbonate

35
Q

How is tissue oxygen delivery improved when anaemic or high demand for oxygen e.g. metabolic acidosis or high CO2 concentrations?

A

By small molecules affecting oxygen dissociation curve and thus affecting haemoglobin oxygen binding affinity

36
Q

Oxygen affinity to heme molecule on haemoglobin is changed how?

A

Globin chain adjusted - as O2 binds to one subunit the Hb shape changes

37
Q

Hb needs to be able to bind oxygen easily when the pO2 is high/low in the lungs, needs to hold onto it as the pO2 increases/decreases in the blood vessels, needs to then release O2 in the tissues where the pO2 is high/low?

A

Hb needs to be able to bind oxygen easily when the pO2 is high in the lungs, needs to hold onto it as the pO2 decreases a little in the blood vessels, needs to then release O2 in the tissues where the pO2 is low

38
Q

Curve for oxygen binding is what type?

A

Sigmoidal

39
Q

What does steep part of curve for oxygen dissociation being in venous area of blood mean?

A

That change in PO2 in venous blood means big change in binding affinity so lots of oxygen can be delivered easily

40
Q

What is allosteric effect?

A

As one oxygen binds to Hb the shape changes and changes binding affinity for next molecule

41
Q

Myoglobin curve also has allosteric effect like haemoglobin curve. T/F?

A

False - has more straight line up that then levels out (more like Michelis-Mentin)

42
Q

What molecules shift Hb curve to the right thus delivering more oxygen to tissues rather than binding?

A

H+,
CO2,
2,3 BPG

43
Q

Rapapport-lubering shunt is involved in what?

A

generates a 2,3 BPG molecule that can alter the Hb molecule and its oxygen bind affinity by getting in between chains. This lowers oxygen binding affinity and shifts the dissociation curve right

44
Q

What 4 factors shift Hb curve to the right thus delivering more oxygen to tissues rather than binding?

A

H+,
CO2,
2,3 BPG,
high temperature,

45
Q

Where does oxygen bind in Hb?

A

in a haem pocket

46
Q

At the same pO2 HbF and myoglobin bind more/less O2 than Hb

.

A

Bind more

47
Q

Where are the critical parts of the Hb dissociation curve delineating venous and arterial partial pressures?

A

Venous 5.3 and arterial 13.3

48
Q

What is Embden-Myerhof Pathway?

A

anaerobic glycolysis pathway generates ATP (energy) and NADH (for reversal of Fe3+ to Fe 2+)

49
Q

What is the Hexose monophosphate shunt?

A

generates NADPH which protects against oxidative stress by regenerating glutathione

50
Q

What is the name of the cell before it becomes an erythrocyte/mature red cell?

A

Reticulocyte

51
Q

Where is haemoglobin synthesised?

A

in the cytoplasm of red cell precursor (erythroblast)

52
Q

What is name of intact cellular mechanism generating red cells i.e. the machine that makes red cells?

A

erythron

53
Q

Role of B12 and folate in red cell production?

A

catalyse biochemical steps allowing cell division

54
Q

Name of red blood cells in first few days after production, what colour are they, what size are they relative to red blood cells?

A

reticulocytes,
purpley, (because still have some nucleus so red and blue together makes purple)
bigger

55
Q

Reticulocytes still have remnants of what protein?

A

RNA

56
Q

Where is hypoxia detected?

A

Interstitial fibroblast near the peritubular capillaries and the proximal convulsed tubule detect hypoxia in kidney

57
Q

How does kidney respond to hypoxia?

A

Increases erythropoietin production

58
Q

What is role of erythropoietin?

A

Results in erythroid hyperplasia -> Stimulates cell division of red cell precursors and recruits more cells to red cell production in the marrow

59
Q

Hypoxia sensor in kidney is sensing amount of oxygen in blood. T/F?

A

False - Is sensing the capability of carrying oxygen i.e. the Hb amount not the actual oxygen levels

60
Q

Where is iron turned into Fe2+ and porphyria processed in erythroblast in erythropoeisis?

A

in mitochondria, released to form haem in cytoplasm

Haematology (25 decks)

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