Requirement of phospholipase C-gamma 2 activation in surface immunoglobulin M-induced B cell apoptosis.
J Exp Med
; 182(4): 907-14, 1995 Oct 01.
Article
en En
| MEDLINE
| ID: mdl-7561693
ABSTRACT
Surface IgM (sIgM) stimulation induces the tyrosine phosphorylation of multiple cellular substrates, including phospholipase C (PLC)-gamma 2, which is involved in the activation of phosphatidylinositol pathway. DT40 B cells underwent apoptotic cell death when activated through sIgM, a phenomenon that is related to elimination of self-reactive B cells. To examine the roles of PLC-gamma 2 in sIgM signaling, we have generated DT40 cells deficient in PLC-gamma 2 Cross-linking of sIgM on PLC-gamma 2-deficient cells evoked neither inositol 1,4,5-trisphosphate nor calcium mobilization. In PLC-gamma 2- or Syk-deficient DT40 cells, the induction of apoptosis was blocked, but was still observed in Lyn-deficient cells. Src homology 2 domains of PLC-gamma 2 were essential for both its activation and sIgM-induced apoptosis. Since tyrosine phosphorylation of PLC-gamma 2 is mediated by Syk, these results indicate that activation of PLC-gamma 2 through Syk is required for sIgM-induced apoptosis.
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Fosfolipasas de Tipo C
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Inmunoglobulina M
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Linfocitos B
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Receptores de Antígenos de Linfocitos B
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Transducción de Señal
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Apoptosis
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Isoenzimas
Límite:
Animals
Idioma:
En
Revista:
J Exp Med
Año:
1995
Tipo del documento:
Article
País de afiliación:
Estados Unidos