CD43 REGULATES TYROSINE PHOSPHORYLATION OF A 93-KD PROTEIN IN T-LYMPHOCYTES
CD43 REGULATES TYROSINE PHOSPHORYLATION OF A 93-KD PROTEIN IN T-LYMPHOCYTES
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DOI：
10.1182/blood.v86.11.4194.bloodjournal86114194
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发表时间：
1995-12-01
期刊：
影响因子：
20.3
通讯作者：
ARDMAN, B
中科院分区：
文献类型：
--
作者：
MANJUNATH, N;ARDMAN, B
白细胞唾液糖蛋白CD 43具有信号转导分子的特征，被认为对T细胞活化和粘附很重要。然而，CD 43参与的细胞生化事件仍然知之甚少。在这里，我们提供的证据表明，CD 43调节T细胞中的特定底物的酪氨酸磷酸化。在CD 43（+）T细胞系CEM中特异性鉴定了93-kD酪氨酸磷蛋白，但在通过基因靶向获得的CD 43缺陷型对应细胞中未鉴定出。用CD 43 cDNA转染后，在CD 43缺陷型CEM细胞中检测到93-kD磷蛋白，并且通过与从CD 43（+）细胞获得的CD 43免疫沉淀物孵育，可以在来自CD 43缺陷型细胞的裂解物中特异性磷酸化。HeLa细胞转染子中CD 43的表达与新型磷蛋白的出现相关，包括分子量约为93 kD的磷蛋白，证实了细胞底物的酪氨酸磷酸化特异性来自CD 43表达。我们的结论是，CD 43调节酪氨酸磷酸化的93 kD的T细胞底物。(C)1995年，美国血液学会。
The leukocyte sialyloglycoprotein CD43 exhibits features of a signal transducing molecule and is thought to be important for T-cell activation and adhesion. However, cellular biochemical events in which CD43 participates remain poorly understood. Here we provide evidence that CD43 regulates tyrosine phosphorylation of a specific substrate in T cells. A 93-kD tyrosine phosphoprotein was identified specifically in the CD43(+) T-cell line CEM, but not in their CD43-deficient counterparts derived by gene targeting. The 93-kD phosphoprotein was detected in the CD43-deficient CEM cells after transfection with CD43 cDNA, and it could be specifically phosphorylated in lysates from the CD43-deficient cells by incubation with a CD43 immunoprecipitate obtained from the CD43(+) cells. Expression of CD43 in HeLa cell transfectants was associated with the appearance of novel phosphoproteins including one with a molecular weight of approximately 93 kD, confirming that tyrosine phosphorylation of cellular substrates results specifically from CD43 expression. We conclude that CD43 regulates tyrosine phosphorylation of a 93-kD T-cell substrate. (C) 1995 by The American Society of Hematology.