260b Erythropoiesis Flashcards
Erythron
progenitor + mature RBC; continuously renew from BM
Erythropoiesis
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
reticulocyte
early RBC from BM in blood
hematocrit - what is it? what does dehydration do? hemorrhage?
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)
anemia
decreased hemoglobin/Hct
polycythemia
increased RBC count
reticulocytosis
increased young RBCs
mean corpuscular volume (MCV)
size of RBC
micro/normo/macro
mean corpuscular hemoglobin concentration (MCHC)
amount of Hb in RBC
normo/hypo
erythroid precursors in BM - how long does this take?
process takes 2 weeks –> reticulocytes 0-3 days in BM –> ~ 1 day in circulation (unless due to anemia then 2-4 days)
mature RBC life cycle
120 days in circulation
reticulocytes
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
RBC - shape, content, membrane features, E?
biconcave w/out nucleus or mito
Hb makes up 33%
membrane allow pliability
E via glycolysis
hemoglobin
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
RBC - shape, content, membrane features, E?
biconcave w/out nucleus or mito
Hb makes up 33%
membrane allow pliability
E via glycolysis
hemoglobin
tetramer with 4 heme groups - each can bind O2 molecule
heme = Fe bound to protoporphyrin
protein globin binds heme
globin determines type of Hb
chromosomes of globins
non-a (B) = 11
a = 16
RBC degradation
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
excess porphyrin is stored how?
complexed to zinc
RBC degradation
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
what increases O2 dissociation from Hb?
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)
normal Hb saturation
arterial - 95 mmHg, >97%
venous - 40 mmHg, 75%
what increases O2 dissociation from Hb?
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)
fetal Hb vs maternal Hb dissociation curve?
fetal is shifted left – much highter affinity for O2
at same PO2, fetal Hb binds more O2 to get a higher percent saturation