Phospholipase C-gamma, a substrate for PDGF receptor kinase, is not phosphorylated on tyrosine during the mitogenic response to CSF-1.

Phospholipase C-gamma, a substrate for PDGF receptor kinase, is not phosphorylated on tyrosine during the mitogenic response to CSF-1.
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磷脂酶 C-gamma 是 PDGF 受体激酶的底物,在 CSF-1 的促有丝分裂反应期间,酪氨酸不会被磷酸化。

DOI:
10.1002/j.1460-2075.1989.tb08496.x
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发表时间:
1989
期刊:
The EMBO journal
影响因子:
--
通讯作者:
Schlessinger,J
Schlessinger,J
中科院分区:
--
文献类型:
--
作者:
Downing,JR;Margolis,BL;Zilberstein,A;Ashmun,RA;Ullrich,A;Sherr,CJ;Schlessinger,J

文献摘要

相似文献

用促有丝分裂浓度的血小板衍生生长因子(PDGF)或CSF-1刺激表达编码集落刺激因子-1(CSF-1)受体的转导人c-fms基因的静止小鼠NIH 3 T3细胞。用PDGF处理完整细胞后,免疫沉淀磷脂酶C-γ(PLC-γ)在酪氨酸上磷酸化,钙被动员。相比之下,仅痕量的磷酸酪氨酸掺入PLC-γ中,并且在CSF-1刺激后未检测到细胞内钙信号。类似地,CSF-1处理在CSF-1依赖性中不刺激PLC-γ对酪氨酸的磷酸化。表达高水平CSF-1受体的SV 40-永生化小鼠巨噬细胞系。在成纤维细胞中,PLC-γ的抗血清在配体刺激后共沉淀了一部分PDGF受体(PDGF-R)的酪氨酸磷酸化形式,这意味着磷酸化的PDGF-R和PLC-γ在稳定的复合物中相关联。用原钒酸盐预处理细胞也导致PLC-γ的酪氨酸磷酸化,其被PDGF显著增强,但不被CSF-1增强。因此,尽管PDGF和CSF-1受体在结构上相关,并且似乎源自单一祖先基因,但成纤维细胞中只有PDGF诱导的有丝分裂与PLC-γ的酪氨酸磷酸化相关。
Quiescent mouse NIH3T3 cells expressing a transduced human c‐fms gene encoding the receptor for colony stimulating factor‐1 (CSF‐1) were stimulated with mitogenic concentrations of platelet‐derived growth factor (PDGF) or CSF‐1. Immunoprecipitated phospholipase C‐gamma (PLC‐gamma) was phosphorylated on tyrosine and calcium was mobilized following treatment of intact cells with PDGF. In contrast, only trace amounts of phosphotyrosine were incorporated into PLC‐gamma and no intracellular calcium signal was detected after CSF‐1 stimulation. Similarly, CSF‐1 treatment did not stimulate phosphorylation of PLC‐gamma on tyrosine in a CSF‐1‐dependent. SV40‐immortalized mouse macrophage cell line that expresses high levels of the CSF‐1 receptor. In fibroblasts, antiserum to PLC‐gamma co‐precipitated a fraction of the tyrosine phosphorylated form of the PDGF receptor (PDGF‐R) after ligand stimulation, implying that phosphorylated PDGF‐R and PLC‐gamma were associated in a stable complex. Pre‐treatment of cells with orthovanadate also led to tyrosine phosphorylation of PLC‐gamma which was significantly enhanced by PDGF, but not by CSF‐1. Thus, although the PDGF and CSF‐1 receptors are structurally related and appear to be derived from a single ancestor gene, only PDGF‐induced mitogenesis in fibroblasts correlated with tyrosine phosphorylation of PLC‐gamma.