RBCs Flashcards

1
Q

State why being full of haemoglobin is a problem for RBCs

A
  • high oncotic pressure (water wants to come in)
  • oxygen-rich environment (oxidation risk)
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2
Q

State why having no nucleus is a problem for RBCs

A
  • can’t divide
  • can’t replace damaged proteins
  • limited cell lifespan
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3
Q

State why having no mitochondria is a problem for RBCs

A
  • limited to glycolysis for generation of energy (can’t perform citric acid cycle)
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4
Q

State why having a high surface area/vol ratio is a problem for RBCs

A

need to keep water out

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5
Q

State why being flexible is a problem for RBCs

A

specialised membrane required can go wrong

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6
Q

What keeps the ion concentrations right (& therefore keeps water out) in RBCs

A

sodium-potassium pump (requires significant energy though)

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7
Q

Describe the haem group in haemoglobin

A

Fe2+ in a flat porphyrin ring

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8
Q

State the 3 functions of haemoglobin

A
  • deliver oxygen to the tissues
  • act as a buffer for H+
  • CO2 transport
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9
Q

Where does RBC production occur?

A

bone marrow

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10
Q

What hormone regulates RBC production and where is it released from?

A

Erythropoietin (released from kidneys)

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11
Q

What causes erythropoietin to be released from the kidneys?

A

senses hypoxia (NOT a cell counter)

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12
Q

State the average RBC lifespan

A

120 days

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13
Q

How are RBCs recycled?

A

Aged cells eaten by macrophages
Contents recycled:
- global chains recycled to amino acids
- heme group broken down to iron & bilirubin
- bilirubin taken to liver & conjugated, then excreted in bile

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14
Q

What product of glycolysis is useful to the RBC & why

A

NADH (electron donor)
can recover Fe3+ to Fe2+ (3+ cannot carry oxygen)

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15
Q

What molecule protects us from hydrogen peroxide (reactive O2 species) & how is it replenished

A

GLUTATHIONE (reacts with it to form water)/GSH
Replenished by NADPH (in turn generated by the hexose monophosphate shut)

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16
Q

State the enzyme involved in the shunt to generate NADPH (needed to reform GSH) & its importance

A

G6PD - rate-limiting enzyme

17
Q

How is the majority of CO2 transported?

A

As bicarbonate

18
Q

Describe the unusual kinetics of O2 binding to Hb

A

Allosteric effect - when one binds, others more likely

19
Q

Describe the structural difference between foetal Hb & adult Hb

A

Foetal = alpha2 gamma2
Adult = alpha2 beta2

20
Q

State the difference between saturation with oxygen in foetal and adult haemoglobin

A

foetal saturates more at the same partial pressure of O2 (takes O2 from maternal circulation

21
Q

Describe the role of the Rapapoport-Lubering Shunt

A
  • generates 2,3 DPG
  • this shifts oxygen dissociation curve & allows more O2 to be released