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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.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1999 by the American Society for Biochemistry and Molecular Biology.
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