260b Erythropoiesis Flashcards

1
Q

Erythron

A

progenitor + mature RBC; continuously renew from BM

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2
Q

Erythropoiesis

A

kidneys release EPO based on oxygen tension (low O2 tension increased HIF-1 transcription factor –> activates EPO gene expression)

goes to BM to make new RBCs

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3
Q

reticulocyte

A

early RBC from BM in blood

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4
Q

hematocrit - what is it? what does dehydration do? hemorrhage?

A

packed RBC volume compared to total blood volume (aka RBC concentration)

dehydration increases hemtocrit due to less plasma

hemorrhage - no change in RBC concentration in the first few hours (both plasma and RBC lost), after a few hours the plasma volume increases which decreased Hct for ~ 30 days (until RBC are made again)

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5
Q

anemia

A

decreased hemoglobin/Hct

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6
Q

polycythemia

A

increased RBC count

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7
Q

reticulocytosis

A

increased young RBCs

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8
Q

mean corpuscular volume (MCV)

A

size of RBC

micro/normo/macro

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9
Q

mean corpuscular hemoglobin concentration (MCHC)

A

amount of Hb in RBC

normo/hypo

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10
Q

erythroid precursors in BM - how long does this take?

A

process takes 2 weeks –> reticulocytes 0-3 days in BM –> ~ 1 day in circulation (unless due to anemia then 2-4 days)

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11
Q

mature RBC life cycle

A

120 days in circulation

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12
Q

reticulocytes

A

immature RBCs

no nucleus, but still have mitochondria, ribosomes, golgi, etc

stain with methylene blue OR have solid red color unlike normal RBC with white center

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13
Q

RBC - shape, content, membrane features, E?

A

biconcave w/out nucleus or mito

Hb makes up 33%

membrane allow pliability

E via glycolysis

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14
Q

hemoglobin

A

tetramer with 4 heme groups - each can bind O2 molecule

synthesizes in BM

heme = Fe bound to protoporphyrin in mito

protein globin from cytoplasmic ribosome binds heme to form Hb in cytoplasm

globin determines type of Hb

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15
Q

RBC - shape, content, membrane features, E?

A

biconcave w/out nucleus or mito

Hb makes up 33%

membrane allow pliability

E via glycolysis

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16
Q

hemoglobin

A

tetramer with 4 heme groups - each can bind O2 molecule

heme = Fe bound to protoporphyrin
protein globin binds heme

globin determines type of Hb

17
Q

chromosomes of globins

A

non-a (B) = 11

a = 16

18
Q

RBC degradation

A

Mo in BV, BM, spleen, liver eat old RBCs via phagocytosis

Globin –> reusable aa’s
Fe
heme –> bilirubin –> binds albumin –> liver –> conjugated with glucuronic acid –> bile

19
Q

excess porphyrin is stored how?

A

complexed to zinc

20
Q

RBC degradation

A

Mo in BV, BM, spleen, liver eat old RBCs via phagocytosis

Globin –> reusable aa’s
Fe
heme –> bilirubin –> binds albumin –> liver –> conjugated with glucuronic acid –> bile

21
Q

what increases O2 dissociation from Hb?

A

shifts O2 sat curve to the right (sat on y axis, PO2 on x axis)

increased:
Temp
H+ concentration (lower pH) - Bohr effect
CO2
2,3 - BPG (stimulated by deoxyhemoglobin)

22
Q

normal Hb saturation

A

arterial - 95 mmHg, >97%

venous - 40 mmHg, 75%

23
Q

what increases O2 dissociation from Hb?

A

shifts O2 sat curve to the right (sat on y axis, PO2 on x axis)

increased:
Temp
H+ concentration (lower pH) - Bohr effect
CO2
2,3 - BPG (stimulated by deoxyhemoglobin)

24
Q

fetal Hb vs maternal Hb dissociation curve?

A

fetal is shifted left – much highter affinity for O2

at same PO2, fetal Hb binds more O2 to get a higher percent saturation

24
Q

fetal Hb vs maternal Hb dissociation curve?

A

fetal is shifted left – much highter affinity for O2

at same PO2, fetal Hb binds more O2 to get a higher percent saturation