鉴定一种与人类T淋巴细胞和自然杀伤细胞中的信号受体相关的新型二聚体磷蛋白（PP29/30）。
Identification of a novel dimeric phosphoprotein (PP29/30) associated with signaling receptors in human T lymphocytes and natural killer cells.
作者信息
Schraven B, Ratnofsky S, Gaumont Y, Lindegger H, Kirchgessner H, Bruyns E, Moebius U, Meuer S C
机构信息
Department of Applied Immunology, Deutsches Krebsforschungszentrum, Heidelberg, Germany.
出版信息
J Exp Med. 1994 Sep 1;180(3):897-906. doi: 10.1084/jem.180.3.897.
Two-dimensional gel electrophoresis of in vitro phosphorylated proteins coprecipitated by CD2 monoclonal antibody (mAb) from Brij58 lysates of resting human T lymphocytes and natural killer (NK) cells resulted in the identification of a novel 29/30-kD disulfide-linked dimer (pp29/30). Comparative two-dimensional analysis of CD2, CD3, CD4, CD5, and CD8 immunoprecipitates revealed that pp29/30 associates with these signaling receptor complexes but not with CD18, CD27, and CD29 in human T lymphocytes. Analysis of CD2 immunoprecipitates prepared from T cell antigen receptor/CD3-modulated T lymphocytes indicated that pp29/30 preferentially associates and comodulates with the human T cell antigen receptor (TCR). Since tyrosine phosphorylated pp29/30 selectively interacts with the Src homology type 2 domains (SHZ) of the protein tyrosine kinases p56lck and p59fyn but not ZAP70 the present data suggest that pp29/30 represents a novel signaling receptor associated phosphoprotein likely involved in the activation of human T lymphocytes and NK cells.
利用CD2单克隆抗体（mAb）从静息人T淋巴细胞和自然杀伤（NK）细胞的Brij58裂解物中共沉淀出体外磷酸化蛋白，进行二维凝胶电泳，结果鉴定出一种新的29/30-kD二硫键连接的二聚体（pp29/30）。对CD2、CD3、CD4、CD5和CD8免疫沉淀物进行的二维比较分析显示，pp29/30与人T淋巴细胞中的这些信号受体复合物相关，但与CD18、CD27和CD29不相关。对从T细胞抗原受体/CD3调节的T淋巴细胞制备的CD2免疫沉淀物的分析表明，pp29/30优先与人T细胞抗原受体（TCR）相关并共同调节。由于酪氨酸磷酸化的pp29/30选择性地与蛋白酪氨酸激酶p56lck和p59fyn的Src同源2结构域（SHZ）相互作用，而不与ZAP70相互作用，因此目前的数据表明，pp29/30代表一种新的信号受体相关磷蛋白，可能参与人T淋巴细胞和NK细胞的激活。
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