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Delivery of an accessory signal for cell activation by exogenous phosphatidylinositol‐specific phospholipase C
Author(s) -
S.M. Jamshedur Rahman,
M. Pu,
Yue Hua Zhang,
Michinari Hamaguchi,
Takashi Iwamoto,
Ryo Taguchi,
Hiroh Ikezawa,
K Isobe,
Tomoaki Yoshida,
Izumi Nakashima
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80517-k
Subject(s) - phospholipase c , phosphatidylinositol , phosphoinositide phospholipase c , biochemistry , microbiology and biotechnology , signal transduction , biology , cell surface receptor , t cell receptor , diacylglycerol kinase , tyrosine phosphorylation , receptor , t cell , protein kinase c , immune system , immunology
Digestion of phosphatidylinositol (PI) or glycosylphosphatidylinositol (GPI) anchors of membrane proteins on the external cell surface with exogenous PI‐specific phospholipase C (PIPLC) from Bacillus thuringiensis was shown to transmit a signal into the thymocyte to modulate the TCR/CD3 complex‐induced signal delivery for cell activation. This was demonstrated for very early protein tyrosine phosphorylation, early c‐ fos transcription and late DNA synthesis. For this effect preincubation of the cells with PIPLC was required, but there was no evidence of involvement of any soluble products released form the cell surface by PIPLC in the signaling, suggesting a crucial role of the membrane‐bound counterpart (diacylglycerol or diradylglycerol) of the PI/GPI hydrolysate. A possible role for this accessory signal in the microorganism‐linked control of the T cell receptor function is discussed.