Red Blood Cells Flashcards

1
Q

Where is blood derived from?

A

Mesoderm

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What are the 3 important functions of RBCs?

A
  1. Transport oxygen and nutrients
  2. Control infection
  3. Hemostasis (osmotic balance, can’t loose blood)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Blood Cell function affects all organs and tissues. Which three organs are the most sensitive to oxygen delivery?

A

Brain, Heart, Kidney

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

List 6 organs/tissues affecting blood function and explain how

A
  1. Spleen-Removes senescent RBC
  2. Kidney-Oxygen sensing
  3. Heart-blood circulation
  4. Liver-makes clotting proteins/albumins
  5. Lungs-oxygen/CO2 exchange
  6. Bone Marrow-source of blood cells, makes them
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Red blood cell life span

A

120 days

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

blood volume?
Red cell count?
Circulating RBC?

A

5 L, 5 million/microliter = 25 trillion circulating RBC

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Hematocrit

A

Volume percentage of RBC in blood
PCV=pack cell volume
ECV= erythrocyte cell volume

If dehydrated, plasma fraction on low side, so hematocrit may go up

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Why do RBCs stain acidophilic (red)

A

filled with hemoglobin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

young RBC

A

reticulocyte

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Why are RBCs anucleate?

A

Nucleus takes up lot of space, it would sacrifice flexibility. Spit out just before they leave bone marrow

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

In addition to non-nucleated, RBCs lose what other important organelles? What are the implications?

A

Mitochondria, golgi apparatus, and ER. With no mitochondria, can’t use the oxygen they transport because can’t do oxidative metbolism. With no nuclei and organelles, they don’t contain DNA and can’t synthesize RNA. = LIMITED REPAIR CAPABILITIES

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Size and shape of RBC

A

7-8 microns diameter; 1 micron tall; biconcave disc

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Variation in size

A

Anisocytosis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Variation in shape

A

Poikilocytosis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

RBC Color

A

Chomicity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Measure of variation in red blood cell volume. Often used together with mean cell volume (MCV)

A

RDW (red cell distribution width)

higher RDW indicate greater variation in size

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Heme contains what sized-membrane rings and how many?

A

4 five membered rings and 4 six membered rings.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What is the state of iron in heme? How many coordinates? Coordinated to what?

A

Ferrous (2+), four coordinates to nitrogen atoms of histidine chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Adult hemoglobin 4 subunits (majority)

A

2 alpha-globin, 2 beta-globin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Hemoglobin, unlike myoglobin, exhibits cooperative binding/release. What is this an example of and how what type of curve does it display?

A

Allosteric binding-uptake of one ligand influences affinities of other binding sites.

Sigmoidal curve

Myoglobin only binds one oxygen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Hemoglobin has a _____ affinity for oxygen than myoglobin. Hemoglobin is a ______ efficient carrier of of oxygen than myoglobin

A

lower affinity, more efficient. (since lower affinity, it has an easier time releasing oxygen to parts of bodies that need it!)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Left shift in oxygen dissociation curve

A

increases hemoglobin affinity for oxygen. holds on tighter to oxygen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Right shift in oxygen dissociation curve

A

decrease affinity for oxygen. hemoglobin gives up oxygen more readily

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

P50

A

the partial pressure of oxygen in the blood where hemoglobin is 50% saturated (PO2 measured in mm Hg)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

An increased P50 signals a _____ affinity and a _____ shift in curve

A

decreased affinity (a larger partial pressure is necessary to maintain 50% oxygen saturation.) and right shift in curve

26
Q

Direction of curve shift when: increase temperature

A

right shift (lower affinity for oxygen)

27
Q

Direction of curve shift when: decrease PCO2

A

left shift (high affinity for oxygen)

28
Q

Direction of curve shift when: decrease pH

A

right shift (lower affinity). Once blow out CO2 in lungs, it no longer binds to hemoglobin, and you increase hemoglobin affinity for oxygen again

29
Q

Direction of curve shift when: increase in 2,3-Diphosphoglycerate

A

right shift (lower affinity). Derived from glycolysis intermediate, signals that body needs oxygen. Lower affinity allows oxygen to dissociate

30
Q

This molecule is produced as a longer adaptation for hypoxia or anemia to regulate Hgb affinity for O2

A

2-3-Diphosphoglycerate (shuttling of 1,3-diphosphoglycerate–>23DPG in glycolysis)

31
Q

Fetal hemoglobin

A

2 alpha-globin, 2-gamma globin

32
Q

Direction of curve shift when: increase CO

A

left shift (CO at one of Hgb binding sites increases the oxygen affinity of the other 3 sites, Hgb affinity increases, holding on to its oxygen tighter)

33
Q

CO Poisoning

A

binds to heme iron, 240 fold higher affinity than O2

34
Q

Hbf (fetal) has ______ affinity than adult

A

higher affinity. needs oxygen, steals from mom

35
Q

Resistant to effects of 2,3-DPG

A

HbF

36
Q

Sickle cell disease is what mutation in which chain? Why is this mutation important?

A

Point mutation from Glu>Val

insert hydrophobic where shouldn’t be, becomes insoluble because valines will huddle together

37
Q

RBCs obtain energy from which process?

A

Glycolysis, only get 2 lousy ATPs and NADH

38
Q

Relaxed state of hemoglobin has a ________ affinity

A

higher affinity

39
Q

Taut state of hemoglobin has a _______ affinity

A

lower affinity

40
Q

Iron in heme group is in ferric state (+3)

A

Methemoglobin

41
Q

This electron transport hemoprotein enzymes couples with NADH to restore Hb iron to the reduced (+2) state

A

cytochrome b5 oxidase and reductase
cyt(b5ox) +NADH –> cyt(b5red) + NAD
cyt(b5red) + Hb-Fe3+ –> Hb-Fe2+ + cyt(b5ox)

42
Q

What supplies the NADH that restores Hb iron to the reduced state?

A

Glycolysis, it produces NADH and has no better use for it since can’t do metabolism in RBCs!

43
Q

How does glutathione eliminate reactive oxygen species?

A

2GSH (reduced) + H2O2 —> GSSG (oxidized) + 2H2O

GSSG + NADPH —> 2GSH + NADP

44
Q

What is the source of NADPH for reduction of glutathione?

A

Pentose Phosphate pathway

45
Q

Glycated Hb, non-enzymatic

A

Hemogobin A1c

46
Q

Why is measuring HbA1c (called the A1C test) used to diagnose type 1 and 2 diabetes?

A

HbA1c is glycated and proprotional to blood glucose levels. It is an integrated measure of glucose control over prolonged period.

Higher A1C level = poor blood sugar control

47
Q

How many RBCs do we make a day?

A

200 billion!

48
Q

This RBC membrane component (protein) gives RBC its rubber-like flexibility

A

Spectrin (Band 1)

49
Q

These 2 RBC membrane components anchor spectrin to the membrane

A

Ankyrin and protein band 4.1

50
Q

This RBC membrane component is an anion exchanger important for moving bicarbonate in and out

A

AE-1 (Band 3)

51
Q

This structure is what spectrin multimers form beneath the plasma membrane to give RBC cytoskeleton its strength and flexibility

A

Hexagonal lattice

52
Q

Mutation in either of these three components can cause hereditary spherocytosis and consequently a shorter life span.

A

Spectrin, Ankyrin, or Band 3 (AE-1. anion exchanger)

53
Q

Which organ targets abnormally shaped and old red cells?

A

Spleen

54
Q

Why does hereditary spheroctyosis RBCs have lower life span?

A

Can’t properly make membrane, lose it, and can only make a sphere. Contains fragile cell walls, so prone to breakage, lyse more frequently, can’t make it through endothelial cells in spleen. Tend to get eaten by macrophages

55
Q

This hereditary disease is also due to spectrin, confers resistance to malaria, and most patients are asymptomatic

A

Hereditary Elliptocytosis

56
Q

In a patient with hereditary spherocytosis, what would likely increase?

A

Reticulocyte “brand new car”

57
Q

What effect does erythropoietin (EPO) have on reticulocyte count and hematocrit?

A

Increases reticulocyte and maintains hematocrit

58
Q

Why might you see bilirubin levels increase in hereditary spherocytosis? (signs: causing skin and whites of eyes to turn yellow)

A

Bilirbubin is the yellow breakdown product of heme. When RBCs get disposed of in spleen, hemoglobin is released, and heme gets broken down into bilirubin. Bilirubin is insoluble in water, so gets bound to albumin and is sent to liver

59
Q

An osmotic fragility test is done to confirm HS, where patients RBCs are placed in concentrations of saline solution. What would you expect to happen to spherocytes compared to normal RBCs?

A

Spherocytes do not tolerate weak saline solution, they will burst sooner than normal cells. When RBCs are placed in saline solution, they absorb water until the cell membrane bursts.

60
Q

What vitamin supplement would you need to take when treating hereditary spherocytosis?

A

Folic acid

61
Q

NADPH from pentose phosphate pathway comes from this enzyme

A

Glucose-6-phosphate dehydrogenase (G6PD)