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Haematology Week 1 > Normal Red Blood Cells > Flashcards

Normal Red Blood Cells Flashcards

1
Q

What is the result of red blood cells being full of haemoglobin?

A

They have a high oncotic pressure and an oxygen rich environment

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2
Q

What is the result of red blood cells having no nucleus?

A

They can’t divide or replace damaged proteins so they have a limited lifespan

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3
Q

What is the result of red blood cells having no mitochondria?

A

Limited to glycolysis for energy generation

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4
Q

Describe the membrane of a red blood cell?

A

Contains protein spars and protein anchors to make it flexible

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5
Q

What happens if there is damage to the proteins within a red cell membrane?

A

They will become inflexible and won’t be able to pass through capillaries

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6
Q

Describe briefly what happens in the sodium potassium pump? What is the function of this in red blood cells?

A

K+ in, Na+ out / keeps water out

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7
Q

Describe the basic structure of a haemoglobin molecule?

A

A tetrameric globular protein

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8
Q

Each globular protein of haemoglobin contains what? And this contains what? Which does what?

A

A haem group / Iron / holds onto the oxygen molecule

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9
Q

What chains is a) adult and b) foetal haemoglobin composed of?

A

a) 2 alpha and 2 beta b) 2 alpha and 2 gamma

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10
Q

Within haemoglobin, one oxygen molecule binds to what?

A

One Fe2+ molecule

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11
Q

Why does oxygen not bind to Fe3+?

A

Because this is already oxidised

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12
Q

What are the main functions of haemoglobin?

A

Deliver oxygen to tissues, act as a buffer for H+, involved in CO2 transport

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13
Q

Describe briefly the regulation of RBC production i.e the role of erythropoietin?

A

Hypoxia is sensed by the kidneys which stimulates erythropoietin to be produced. This stimulates more red blood cell development and then erythropoietin levels drop back to normal

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14
Q

Destruction of red blood cells usually occurs where? The red blood cells are taken out of the circulation by what?

A

Spleen / macrophages

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15
Q

How are the contents of red blood cells broken down?

A

Globin chains are recycled to amino acids / haem group is broken down into iron which gets recycled and bilirubin which is taken to the liver and excreted in the urine and faeces as bile

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16
Q

How does a red blood cell get energy? What is the net gain of ATP in this process?

A

Glycolysis / 2 ATP

17
Q

How does an RBC prevent Fe2+ from becoming Fe3+?

A

The process of glycolysis produced NADH which acts as a reducing agent and protects the Fe2+ from oxidation

18
Q

What are some examples of free radicals which could potentially cause damage to enzymes and Hb?

A

Superoxide and hydrogen peroxide

19
Q

What molecule protects us from free radical damage from hydrogen peroxide? How?

A

Glutathione - it reacts with hydrogen peroxide to form water and oxidised glutathione (GSSG)

20
Q

Glutathione which has been oxidised can be replenished via which other molecule? Which process is responsible for producing this?

A

NADPH / hexose monophosphate shunt

21
Q

What is the rate limiting enzyme in the hexose monophosphate shunt?

A

Glucose 6 phosphate dehydrogenase

22
Q

What are the ways that CO2 can travel to the lungs?

A

10% dissolved in solution, 30% bound directly to Hb as carbamino-Hb and 60% as bicarbonate

23
Q

How many oxygen molecules are bound to one Hb?

A

4

24
Q

What is the relationship between oxygen being bound to haemoglobin in a) the lungs (high pO2) and b) the tissues (low pO2)?

A

a) oxygen is bound to Hb (fully saturated) b) haemoglobin gives up oxygen to the tissues (desaturated)

25
Q

What is the shape of the oxygen-haemoglobin dissociation curve? Why is this?

A

Sigmoidal / due to allosteric binding

26
Q

Describe what is meant by allosteric/co-operative binding of oxygen and haemoglobin?

A

Once one oxygen molecule has bound to an Hb subunit, it becomes easier for further units to bind

27
Q

On the oxygen dissociation curve, what way will foetal Hb be shifted compared with adult Hb? Why?

A

Left - it saturates more at the same pO2

28
Q

What does it mean if the oxygen haemoglobin dissociation curve is shifted to the a) right? b) left?

A

a) less oxygen is bound to haemoglobin, more oxygen is being delivered to the tissue b) more oxygen is bound to haemoglobin, less oxygen is being delivered to the tissues

29
Q

What are some factors which may shift the oxygen dissociation curve to the right?

A

Decreased pH, increased 2,3-BPG and increased temperature

30
Q

What are some factors which may shift the oxygen dissociation curve to the left?

A

Increased pH, decreased 2,3-BPG, decreased temperature

Haematology Week 1 (11 decks)

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