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Red Cells Flashcards

(60 cards)

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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
What process does RBC use to get ATP? | what molecule is generated from glucose? How many ATP used and how many ATP generated?
Glycolysis - glucose to pyruvate, use up 2 ATP, generate 4 ATP, 1 NADH
26
Oxygen free radicals easily generated in RBCs, why are these dangerous? (2)
Can oxidise Fe2+ to Fe3+ which doesn't transport oxygen, | can damage proteins
27
How is Fe2+ stopped from becoming Fe3+?
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
How is oxidative damage to cellular enzymes and Hb from free radicals prevented?
glutathione (GSH) reacts with free radicals (e.g. hydrogen peroxide) to form water and an oxidised glutathione product
29
Glutathione is replenished by what molecule?
NADPH
30
What is the rate limiting enzyme in the NADPH regeneration process?
glucose-6-phosphate dehydrogenase
31
Hexose monophsophate shunt is responsible for what?
Generates NADPH that maintains GSH levels preventing oxidative damage
32
What enzyme is X-linked that can lead to free radical increase and premature haemolysis?
glucose-6-phosphate dehydrogenase (G6PD)
33
How is CO2 buffered for transport by RBCs?
H+ from broken down CO2 buffered by deoxygenated Hb
34
CO2 transported in what 3 forms and percentage of CO2 transported each way?
10% dissolved, 30% bound directly to Hb, 60% as bicarbonate
35
How is tissue oxygen delivery improved when anaemic or high demand for oxygen e.g. metabolic acidosis or high CO2 concentrations?
By small molecules affecting oxygen dissociation curve and thus affecting haemoglobin oxygen binding affinity
36
Oxygen affinity to heme molecule on haemoglobin is changed how?
Globin chain adjusted - as O2 binds to one subunit the Hb shape changes
37
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?
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
Curve for oxygen binding is what type?
Sigmoidal
39
What does steep part of curve for oxygen dissociation being in venous area of blood mean?
That change in PO2 in venous blood means big change in binding affinity so lots of oxygen can be delivered easily
40
What is allosteric effect?
As one oxygen binds to Hb the shape changes and changes binding affinity for next molecule
41
Myoglobin curve also has allosteric effect like haemoglobin curve. T/F?
False - has more straight line up that then levels out (more like Michelis-Mentin)
42
What molecules shift Hb curve to the right thus delivering more oxygen to tissues rather than binding?
H+, CO2, 2,3 BPG
43
Rapapport-lubering shunt is involved in what?
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
What 4 factors shift Hb curve to the right thus delivering more oxygen to tissues rather than binding?
H+, CO2, 2,3 BPG, high temperature,
45
Where does oxygen bind in Hb?
in a haem pocket
46
At the same pO2 HbF and myoglobin bind more/less O2 than Hb | .
Bind more
47
Where are the critical parts of the Hb dissociation curve delineating venous and arterial partial pressures?
Venous 5.3 and arterial 13.3
48
What is Embden-Myerhof Pathway?
anaerobic glycolysis pathway generates ATP (energy) and NADH (for reversal of Fe3+ to Fe 2+)
49
What is the Hexose monophosphate shunt?
generates NADPH which protects against oxidative stress by regenerating glutathione
50
What is the name of the cell before it becomes an erythrocyte/mature red cell?
Reticulocyte
51
Where is haemoglobin synthesised?
in the cytoplasm of red cell precursor (erythroblast)
52
What is name of intact cellular mechanism generating red cells i.e. the machine that makes red cells?
erythron
53
Role of B12 and folate in red cell production?
catalyse biochemical steps allowing cell division
54
Name of red blood cells in first few days after production, what colour are they, what size are they relative to red blood cells?
reticulocytes, purpley, (because still have some nucleus so red and blue together makes purple) bigger
55
Reticulocytes still have remnants of what protein?
RNA
56
Where is hypoxia detected?
Interstitial fibroblast near the peritubular capillaries and the proximal convulsed tubule detect hypoxia in kidney
57
How does kidney respond to hypoxia?
Increases erythropoietin production
58
What is role of erythropoietin?
Results in erythroid hyperplasia -> Stimulates cell division of red cell precursors and recruits more cells to red cell production in the marrow
59
Hypoxia sensor in kidney is sensing amount of oxygen in blood. T/F?
False - Is sensing the capability of carrying oxygen i.e. the Hb amount not the actual oxygen levels
60
Where is iron turned into Fe2+ and porphyria processed in erythroblast in erythropoeisis?
in mitochondria, released to form haem in cytoplasm

Haematology (25 decks)

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