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1. Theme 2 > T2 L1: Erythrocytes > Flashcards

T2 L1: Erythrocytes Flashcards

1
Q

Describe the effect of pO2 on how oxygen will bind to haemoglobin

A

High pO2 means more oxygen binds to Hb. It will detach when the pO2 is low

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2
Q

Why does oxygen need haemoglobin to enable its transport?

A

Because oxygen in poorly soluble in plasma. Normal arterial blood carries 70x more oxygen on haemoglobin than dissolved directly in plasma

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3
Q

How many molecules of ATP are produced at the end of oxidative respiration?

A

36

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4
Q

What is produced in anaerobic glycolysis and how many molecules of it?

A

2 lactate and 2 ATP

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5
Q

What % of dry weight of red blood cells is haemoglobin?

A

95%

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6
Q

What are the allosteric properties of haemoglobin with O2?

A

When the first oxygen binds, the affinity increases

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7
Q

Where is myoglobin found?

A

In muscles

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8
Q

What charge is unbound Iron ion in haemoglobin?

A

2+

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9
Q

What is HbA and what is its structure?

A

Adult haemoglobin (maternal haemoglobin). It’s a tetramer made of 2 alpha and 2 beta subunits

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10
Q

What is HbF and what is its structure?

A

Foetal haemoglobin. It’s made up of 2 alpha and 2 gamma subunits

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11
Q

Describe the Bohr effect on oxygen binding when pH is low

A

Low affinity of Hb for O2, high for CO2

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12
Q

Where does O2 bind to Hb compared to CO2 and H+?

A

At a different site of Hb

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13
Q

What % of CO2 is dissolved in blood?

A

10%

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14
Q

What % of CO2 is as carbamino Hb?

A

22%

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15
Q

What % of CO2 is as HCO3-?

A

68%

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16
Q

What is a Band 3 protein and what is its function?

A

A membrane exchange protein that allows bicarbonate to leave in exchange for Cl-

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17
Q

What is HHb?

A

Acidified Hb (has a H+)

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18
Q

Where is a higher concentration of Cl- inside RBC’s, in venous or arterial blood?

A

In venous blood

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19
Q

What type of curve does myoglobin have on a partial pressure and fractional saturation graph?

A

A hyperbolic curve (very steep)

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20
Q

What type of curve does heamoglobin have on a partial pressure and fractional saturation graph?

A

A sigmoidal (s-shape)

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21
Q

What does a rightward shift indicate about the affinity for oxygen?

A

Decreased affinity

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22
Q

What 4 molecules encourage a rightward shift of affinity in muscles?

A

Increased presence of CO2, H+, Cl- and Bisphopho-glycerate

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23
Q

Why does a rightward shift of Hb affinity happen in muscles?

A

To lower affinity so that O2 can dissociate from haemoglobin

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24
Q

What is the function of Bisphospho-glycerate (2,3-DPG) in red blood cells?

A

It facilitates O2 dissociation by binding to Hb and lowering its affinity for O2 (causing a rightward shift)

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25
Q

Why does Foetal Hb (HbF) have a higher affinity for O2?

A

Because it has a low affinity for 2,3-DPG (Bisphospho-glycerate) compared to maternal blood so a rightward shift is not achieved as easily.

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26
Q

What is a myoglobin?

A

A storage molecule for O2 found in muscles

27
Q

In active muscles low O2, high CO2, high blood acidity, high temperature and myglobin cause what to happen?

A

O2 leaves Hb, CO2 and H+ bind to Hb, HCO3- leaves RBC’s and Cl- leaves plasma

28
Q

Why is the body more sensitive to changes in CO2 compared H+?

A

Because the H+ signal is only based from the carotid arch but there are more signals for CO2

29
Q

Concentrations of which molecules control breathing rate?

A

O2, CO2 and acid concentration

30
Q

What is the main driver to increase respiratory rate and why?

A

H+ in CSF. Because once CO2 gets into the CSF, it reacts to produce carbonic acid and H+. Not in the blood because CO2 gets into CSF slower so it’s a better indication of higher acidity

31
Q

Why must plasma O2 drop significantly before the respiratory drive increases?

A

Because we are not very sensitive to [O2]. So a bigger change is needed for the body to realise

32
Q

What is meant by anucleate?

A

Lacking organelles

33
Q

What is the height and diameter of erythrocytes?

A

7 micrometres diameter, 2 micrometres height

34
Q

How long do erythrocytes survive?

A

About 100-120 days

35
Q

What is the advantage of erythrocytes being flexible?

A

They can fold in vessels and stack

36
Q

What is the packed cell volume in men compared to women?

A

40-52% in men, 36-48% in women

37
Q

What is the mean cell haemoglobin (MCH) in normal blood?

A

27-34 picograms

38
Q

After the age of 20, where are erythrocytes produced?

A

In membranous bones only like vertebrae

39
Q

Where are erythrocytes produced during embryogenises (4 places)?

A

Liver, spleen, lymph nodes and yolk sac

40
Q

What are the steps of development of stem cells?

A

Multipotent stem cells continue self renewing but some become progenitor cells. Those progenitor cells commit to a lineage and proliferate. Then they all terminally differentiate into mature cells

41
Q

What are progenitor cells?

A

Stem cells that are slightly differentiated and can only develop into cells from only that tissue or organ

42
Q

Which part of erythrocyte production is erythronmycin dependent?

A

Before the stem cells develop into erythroblasts

43
Q

Which part of erythrocyte production is iron dependent?

A

When Erythroblasts are developing into reticulocytes

44
Q

What happens during maturation when the red blood cells are reticulocytes?

A

The cells are getting rid of their nuclear material

45
Q

What is Erythropoetin?

A

A cytokine/hormone that drives erythropoiesis

46
Q

Where is Erythropoetin produced?

A

In the kidney in a hypoxia-inducing way

47
Q

How long do reticulocytes last in the blood?

A

2 days and then becomes a definitive RBC

48
Q

How can a reticulocyte count be used as a diagnostic tool for anaemia?

A

It’s an indicator of bone marrow activity. The reticulocyte count is low when erythrocyte concentrations are low. The reticulocyte count is high in haemolytic anaemias

49
Q

What is methaemoglobinaemia and what causes it?

A

A disease when Hb can’t transport O2 because Fe in Hb is oxidised into Fe3+ when it should be Fe2+. It’s caused by congenital globin mutations, hereditary decrease of NADH and toxic substances

50
Q

What is CO poisoning and what is the treatment?

A

When CO displaces O2 from Hb. The treament is 95% O2 and 5% CO2 (CO2 helps to knock off CO so O2 can displace it)

51
Q

How much stronger is CO’s affinity for HB compared to O2?

A

x250

52
Q

What is cyanosis?

A

When blood turns blue

53
Q

What is Polycythaemia?

A

A high concentration of RBC’s (PCV) leading to thick blood that clogs blood vessels

54
Q

What causes physiologic Polycythaemia?

A

Living in high altitudes

55
Q

What causes Polycythaemia vera?

A

A cancer that’s often asymptomatic. Causes an increased risk of thrombotic events with no cure other than taking blood away (venesection). The chances of developing it increase with age

56
Q

What % of iron is stored intrinsically as ferritin or haemosiderin?

A

30%

57
Q

What is ferritin?

A

A protein that stores and releases iron in a controlled way

58
Q

What is Haemosiderin?

A

An iron storage molecule composed of partially digested ferritin and lysosomes

59
Q

In what cells and organs is Fe stored in the form of ferritin?

A

In the liver, spleen, erythromycin, bone marrow and macrophages/monocytes

60
Q

What is the normal daily loss of iron?

A

About 1 mg/day

61
Q

What dificiency causes megaloblastic (macrocytic) anaemia

A

Vitamin B12 and B9 (folic acid)

62
Q

What is the cause of pernicious anaemia?

A

Failure to absorb Fe (Intrinsic)

63
Q

What cells are sensitive to Folic and B12?

A

All quickly dividing cells

64
Q

What causes hypochromic microcytic anaemia?

A

Iron deficiency (the cells continue living but cannot fill up with Hb)

1. Theme 2 (12 decks)

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