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CD3刺激可导致人T细胞系中磷脂酶C-γ1的丝氨酸和酪氨酸残基发生磷酸化。

CD3 stimulation causes phosphorylation of phospholipase C-gamma 1 on serine and tyrosine residues in a human T-cell line.

作者信息

Park D J, Rho H W, Rhee S G

机构信息

Section on Signal Transduction, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892.

出版信息

Proc Natl Acad Sci U S A. 1991 Jun 15;88(12):5453-6. doi: 10.1073/pnas.88.12.5453.

DOI:10.1073/pnas.88.12.5453
PMID:1828897
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC51891/
Abstract

The human T-cell line Jurkat was found to contain at least two immunologically distinct isoforms of inositol phospholipid-specific phospholipase C (PLC), PLC-beta 1 and PLC-gamma 1. Treatment of Jurkat cells with antibody to CD3 led to phosphorylation of PLC-gamma 1 but not of PLC-beta 1. The phosphorylation of PLC-gamma 1 occurred rapidly and transiently on both serine and tyrosine residues; tyrosine phosphorylation reached a maximum level less than 1 min after stimulation and decreased rapidly, both in the presence and in the absence of orthovanadate. Two-dimensional phosphopeptide map analysis revealed that the major sites of tyrosine and serine phosphorylation in PLC-gamma 1 from activated Jurkat cells are the same as those in PLC-gamma 1 from cells treated with peptide growth factors such as epidermal growth factor and platelet-derived growth factor. Previously, it has been shown that multiple phosphorylation of PLC-gamma 1 by the growth factor receptor tyrosine kinases leads to activation of PLC-gamma 1. Thus, the current data suggest that inositol phospholipid hydrolysis triggered by the T-cell antigen receptor-CD3 complex is due, at least in part, to activation of PLC-gamma 1 and that the mechanism by which this activation is achieved involves phosphorylation of multiple tyrosine residues on PLC-gamma 1 by a nonreceptor tyrosine kinase coupled to the T-cell antigen receptor-CD3 complex.

摘要

人类T细胞系Jurkat被发现至少含有两种免疫上不同的肌醇磷脂特异性磷脂酶C（PLC）同工型，即PLC-β1和PLC-γ1。用抗CD3抗体处理Jurkat细胞会导致PLC-γ1磷酸化，但不会导致PLC-β1磷酸化。PLC-γ1的磷酸化在丝氨酸和酪氨酸残基上迅速且短暂地发生；在刺激后不到1分钟，酪氨酸磷酸化达到最高水平，并迅速下降，无论是否存在原钒酸钠。二维磷酸肽图谱分析表明，活化的Jurkat细胞中PLC-γ1的酪氨酸和丝氨酸磷酸化主要位点与用表皮生长因子和血小板衍生生长因子等肽生长因子处理的细胞中PLC-γ1的相同。此前已表明，生长因子受体酪氨酸激酶对PLC-γ1的多重磷酸化会导致PLC-γ1活化。因此，目前的数据表明，T细胞抗原受体-CD3复合物引发的肌醇磷脂水解至少部分是由于PLC-γ1的活化，并且这种活化的实现机制涉及与T细胞抗原受体-CD3复合物偶联的非受体酪氨酸激酶对PLC-γ1上多个酪氨酸残基的磷酸化。

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