描述：
Erythropoietin (Epo) is a 34 kDa glycoprotein hormone in the type I cytokine family and is
related to thrombopoietin. Its three N-glycosylation sites, four alpha helices, and N- to C-
terminal disulfide bond are conserved across species. Glycosylation of Epo is required
for biological activities in vivo. Mature human Epo shares 75% - 84% amino acid
sequence identity with bovine, canine, equine, feline, mouse, ovine, porcine, and rat EPO.
Epo is primarily produced in the kidney by a population of fibroblast-like cortical interstitial
cells adjacent to the proximal tubules. It is also produced in much lower, but
functionally significant amounts by fetal hepatocytes and in adult liver and brain. Epo
promotes erythrocyte formation by preventing the apoptosis of early erythroid precursors
which express the Epo receptor (Epo R). Epo R has also been described in brain, retina,
heart, skeletal muscle, kidney, endothelial cells, and a variety of tumor cells. Ligand
induced dimerization of Epo R triggers JAK2-mediated signaling pathways followed
by receptor/ligand endocytosis and degradation. Rapid regulation of circulating Epo allows
tight control of erythrocyte production and hemoglobin concentrations. Anemia or other
causes of low tissue oxygen tension induce Epo production by stabilizing the hypoxia
induceable transcription factors HIF-1α and HIF-2α. Epo additionally plays a tissue-protective
role in ischemia by blocking apoptosis and inducing angiogenesis.
原厂资料：
Erythropoietin (Epo) is a 34 kDa glycoprotein hormone in the type I cytokine family and is
related to thrombopoietin. Its three N-glycosylation sites, four alpha helices, and N- to C-
terminal disulfide bond are conserved across species. Glycosylation of Epo is required
for biological activities in vivo. Mature human Epo shares 75% - 84% amino acid
sequence identity with bovine, canine, equine, feline, mouse, ovine, porcine, and rat EPO.
Epo is primarily produced in the kidney by a population of fibroblast-like cortical interstitial
cells adjacent to the proximal tubules. It is also produced in much lower, but
functionally significant amounts by fetal hepatocytes and in adult liver and brain. Epo
promotes erythrocyte formation by preventing the apoptosis of early erythroid precursors
which express the Epo receptor (Epo R). Epo R has also been described in brain, retina,
heart, skeletal muscle, kidney, endothelial cells, and a variety of tumor cells. Ligand
induced dimerization of Epo R triggers JAK2-mediated signaling pathways followed
by receptor/ligand endocytosis and degradation. Rapid regulation of circulating Epo allows
tight control of erythrocyte production and hemoglobin concentrations. Anemia or other
causes of low tissue oxygen tension induce Epo production by stabilizing the hypoxia
induceable transcription factors HIF-1α and HIF-2α. Epo additionally plays a tissue-protective
role in ischemia by blocking apoptosis and inducing angiogenesis.
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