1992
DOI: 10.1073/pnas.89.20.9524
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Association of protein-tyrosine kinase with phospholipase C-gamma 1 in bone marrow-derived mouse mast cells.

Abstract: Bone marrow-derived mouse mast cells contain phospholipase C-y1 (PLC-yl), which is phosphorylated at tyrosine residues upon cross-ing of cell-bound IgE antibod-

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Cited by 31 publications
(14 citation statements)
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“…In mouse CD36-positive TBC, LCFA binding induces the activation of members of the Src protein tyrosine kinase (SrcPTKs) family (47). Interestingly, PTKs activate PLC␥1 in bone marrow-derived mouse mast cells (54). Since the TBC express PLC␤2 and, both PLC␥1 and PLC␤2 induce the PIP 2 hydrolysis, it is tempting to speculate that PLC␤2 might also be involved in the signaling cascade triggered by LCFA-mediated activation of CD36, as already shown for sweet, bitter, and umami tastes.…”
Section: Receptor-coupled Downstream Signalingmentioning
confidence: 99%
“…In mouse CD36-positive TBC, LCFA binding induces the activation of members of the Src protein tyrosine kinase (SrcPTKs) family (47). Interestingly, PTKs activate PLC␥1 in bone marrow-derived mouse mast cells (54). Since the TBC express PLC␤2 and, both PLC␥1 and PLC␤2 induce the PIP 2 hydrolysis, it is tempting to speculate that PLC␤2 might also be involved in the signaling cascade triggered by LCFA-mediated activation of CD36, as already shown for sweet, bitter, and umami tastes.…”
Section: Receptor-coupled Downstream Signalingmentioning
confidence: 99%
“…PLC-␥1 becomes tyrosine phosphorylated within minutes of FcεRI clustering (2,19,41) and induces the hydrolysis of phosphatidylinositol 4,5-bisphosphate to inositol 1,4,5-triphosphate and diacylglycerol, two important signal mediators. To test whether Syk clustering also induces the tyrosine phosphorylation of PLC-␥1, the 145-kDa PLC-␥1 protein was immunoprecipitated from RBL cells infected with the vaccinia virus vector expressing the Syk chimera.…”
Section: Introduction Of a Chimeric Transmembrane Syk Protein Into Rbmentioning
confidence: 99%
“…Subsequent events include (i) the increased tyrosine phosphorylation and activation of a number of signaling molecules, including Syk (7, 23), phospholipase C-␥1 (PLC-␥1) (2,19,41), Vav (36), and mitogen-activated protein (MAP) kinase (46); (ii) activation of protein kinase C (55, 56) and phospholipase A 2 (20); and (iii) elevation of intracellular calcium levels (6). Tyrosine phosphorylation appears to play a critical role in propagating the signal leading to these events since mediator release is blocked by tyrosine kinase inhibitors (27,57).…”
mentioning
confidence: 99%
“…Tyrosine phosphorylation activates PLC␥1 inducing it to hydrolyze phosphatidylinositol 4,5-bisphosphate to produce two second messengers, inositol trisphosphate and diacylglycerol, these in turn result in the increase in intracellular Ca 2ϩ and the activation of protein kinase C (52). PLC␥1 associates with a tyrosine kinase after Fc⑀RI aggregation (53), and a complex containing Syk, PLC␥1, and a 120-kDa phosphoprotein has been seen in B-cells (54). This 120-kDa protein has been postulated to be a bridge between Syk and PLC␥1.…”
Section: Figmentioning
confidence: 99%