Nephrology Dialysis Transplantation, Vol 14, Issue 90002 22-28, Copyright © 1999 by Oxford University Press
C Lacombe and P Mayeux
Erythropoietin (Epo) controls the proliferation, differentiation and
survival of the erythroid progenitors. Epo exerts its effects by binding to
a cell surface receptor. The Epo receptor includes a p66 chain, which is
dimerized upon Epo activation, and two accessory proteins, which have been
defined by cross-linking. Epo binding induces stimulation of the Jak2
tyrosine kinase. Jak2 activation leads to the tyrosine phosphorylation of
several proteins, including The Epo receptor itself. Different
intracellular pathways are activated: Ras/MAP kinase, phosphatidylinositol
3-kinase and STAT transcription factors. However, the exact mechanisms by
which the proliferation and/or differentiation of erythroid cells are
regulated after Epo stimulation are not known. Target disruption of both
Epo and Epo receptors showed that Epo is not involved in the commitment of
the erythroid lineage; it seems to act mainly as a survival factor. Epo is
synthesized largely by the kidney and the liver, and sequences required for
tissue-specific expression have been localized in The Epo gene. A
3′ enhancer is responsible for hypoxia-inducible Epo gene
expression. Hypoxia-induced factor-1 (HIF-1) protein binds to this
enhancer. In addition to anaemia of renal failure, the indication for
treatment with epoetin has been extended to the anaemia of chronic
diseases. Keywords: erythropoietin; erythropoietin
receptor; hypoxia; signal transduction
ORIGINAL ARTICLES
Plenary lecture. The molecular biology erythropoietin
Institute National de la Sante et de la Recherche Medicale, Unite 363, ICGM, Universite Rene Descartes, Paris, France; Service d'Hematologie, AP-HP, ICGM, Hopital Cochin, 27 rue du Faubourg St Jacques, 75014 Paris, France; Corresponding author and address
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