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J Biol Chem, Vol. 274, Issue 48, 33966-33972, November 26, 1999

Erythropoietin Induces Glycosylphosphatidylinositol Hydrolysis
POSSIBLE INVOLVEMENT OF PHOSPHOLIPASE C-₂

Cédric Boudot, Emmanuelle Petitfrère, Zahra Kadri, Stany Chretien^§, Patrick Mayeux^¶, Bernard Haye, and Claudine Billat

From the  Laboratoire de Biochimie, CNRS UPRES-A 6021, IFR 53 Biomolécules, UFR Sciences Exactes et Naturelles, BP 1039, Université de Reims Champagne-Ardenne, F 51687 Reims Cedex 2, the ^§ Institut National de la Transfusion Sanguine (INTS), 6 Rue Alexandre Cabanel, F 75014 Paris, and ^¶ Institut Cochin de Génétique Moléculaire, INSERM U363, Hôpital Cochin, Université René Descartes, 27 Rue du Faubourg Saint Jacques, F 75014 Paris, France

We showed that erythropoietin induced rapid glycosylphosphatidylinositol (GPI) hydrolysis and tyrosine phosphorylation of phospholipase C (PLC)-₂ in FDC-P1 cells transfected with the wild-type erythropoietin-receptor. Erythropoietin-induced tyrosine phosphorylation of PLC-₂ was time- and dose-dependent. By using FDC-P1 cells transfected with an erythropoietin receptor devoid of tyrosine residues, we showed that both effects required the tyrosine residues of intracellular domain on the erythropoietin receptor. Erythropoietin-activated PLC-₂ hydrolyzed purified [³H]GPI indicating that GPI hydrolysis and PLC-₂ activation under erythropoietin stimulation were correlated. Results obtained on FDC-P1 cells transfected with erythropoietin receptor mutated on tyrosine residues suggest that tyrosines 343, 401, 464, and/or 479 are involved in erythropoietin-induced GPI hydrolysis and tyrosine phosphorylation of PLC-₂, whereas tyrosines 429 and/or 431 seem to be involved in an inhibition of both effects. Thus, our results suggest that erythropoietin regulates GPI hydrolysis via tyrosine phosphorylation of its receptor and PLC-₂ activation.

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