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RATNA KUSUMAWATI
Erythropoiesis
• controlled by hormones, especially erythropoietin (EPO) from
the kidney
• three phases of RBC maturation
• production of ribosomes
• synthesis of hemoglobin
• ejection of the nucleus and reduction in organelles
• leave bone marrow as reticulocytes mature in the blood
stream to become erythrocytes
NECESSARY SUBSTANCES FOR ERYTHROPOESIS :
1. Iron
2. Cobalt
3. Manganese
4. Vit B1,B2, B6, B12, C, E
5. Folic acid
6. Amino acid
NECESSARY HORMON FOR ERYTHROCYTES REGULATION :
1. Erythropoietin
2. Tyroid hormone
3. Androgen
Nutritional Needs for Erythropoiesis
• iron - key nutritional requirement
• lost daily through urine, feces, and bleeding
• men 0.9 mg/day and women 1.7 mg/day
• low absorption rate of iron requires consumption of 5-20 mg/day
• dietary iron: ferric (Fe3+) and ferrous (Fe2+)
• stomach acid converts Fe3+ to absorbable Fe2+
• gastroferritin binds Fe2+ and transports it to small intestine
• absorbed into blood and binds to transferrin for transport
to bone marrow, liver, and other tissues
- bone marrow for hemoglobin, muscle for myoglobin,
and all cells use for cytochromes in mitochondria
• liver apoferritin binds to create ferritin for storage
Nutritional Needs for Erythropoiesis
MAKROSIT
Erythropoiesis
Regulatioan
ERYTHROPOESIS
REGULATION
ERITROPOIETIN
• dangers of polycythemia
• increased blood volume, pressure, viscosity
• can lead to embolism, stroke or heart failure
Anemia
• causes of anemia fall into three categories:
• inadequate erythropoiesis or hemoglobin synthesis
• kidney failure and insufficient erythropoietin
• iron-deficiency anemia
• inadequate vitamin B12 from poor nutrition or lack of
intrinsic factor (pernicious anemia)
• hypoplastic anemia – slowing of erythropoiesis
• aplastic anemia - complete cessation of erythropoiesis
• hemorrhagic anemias from bleeding
• hemolytic anemias from RBC destruction (hemolitic)
RBC Life Span
HEMOGLOBIN &
MYOGLOBIN
O2 combines with Hgb in lungs
O2 gas not very soluble in H2O
Hemoglobin transports O2 Hemoglobin
• 2 α globin chains & 2 β globin chains
• 4 heme groups (lipid)
• each heme binds an iron ion (Fe²+) that carries 1 O2
O2 binding proteins:
myoglobin and hemoglobin
• oxygen is not water soluble needs to
be transported
• diffusion is not effective
• myoglobin is found primarily in muscle
tissue
• Hemoglobin is in the blood
• Both proteins contain heme
Protein Function
Physiological roles of:
• Myoglobin
Transports O2 in rapidly respiring muscle
Store of O2 in muscle high affinity for O2
keep O2 supplied to muscles
• Hemoglobin
Found in red blood cells
Carries O2 from lungs to tissues and removes CO2
and H+ from blood to lungs
Lower affinity for O2 than myoglobin
Tetrameter - two sets of similar units (22)
Strong form of hemoglobin found in embryos
Takes oxygen from mother’s hemoglobin
Myoglobin, The Muscle’s O2 Store
• Myoglobin is an iron-containing globular protein in
skeletal and cardiac muscle.
• Stores O2 intramuscularly
• Myoglobin contains only 1 iron atom.
• O2 is released at low PO2.
Myoglobin Binding Curve
• Hyperbolic binding curve
• Relatively insensitive to small
changes in oxygen
concentration
• Hb molecules of O2combine max with 4,
in cascade manner (100% saturated)
• Oxygenation each binding facilitates
further binding of O2
• Saturation of Hb refers the number of
O2 molecules combined with Hb
• 50% saturation : means that Hb binds
with 2 molecules of O2
Transport of O2 in the Blood
• Two mechanisms exist for O2 transport
• Dissolved in plasma
• Combined with hemoglobin
• agranulocytes
• lymphocytes (25-33%)
• variable amounts of bluish cytoplasm (scanty to abundant);
ovoid/round, uniform dark violet nucleus
• monocytes (3-8%)
• largest WBC; ovoid, kidney-, or horseshoe- shaped nucleus
Physiological Characteristics and Functions of
Leukocyte
Terminology