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CD4单克隆抗体B66.6对Jurkat T细胞中磷脂酰丝氨酸合成的抑制作用。

Inhibition of phosphatidylserine synthesis induced by a CD4 mAb, B66.6 in Jurkat T cells.

作者信息

Aussel C, Breittmayer J P, Pelassy C, Carrel S

机构信息

INSERM U210, Faculté de Médecine, Nice, France.

出版信息

J Lipid Mediat. 1992 Sep;5(3):219-25.

PMID:1361369
Abstract

A monoclonal antibody, B66.6, previously classified in the cluster of differentiation 4 (CD4), has been studied and compared with another CD4 monoclonal antibody, IOT4. It was found that B66.6 but not IOT4 was able to mobilize Ca2+ from intracellular stores in the Jurkat T cell line. Ca2+ mobilization was followed by a decrease in the extent of phosphatidylserine synthesis. In the presence of the phorbol ester, phorbol 12,13-dibutyrate, B66.6 induced interleukin-2 synthesis. Altogether, the results indicate that the CD4 monoclonal antibody, B66.6, mimics other T cell activators such as CD3 and confirm that the inhibition of phosphatidylserine synthesis in activated T cells follows the mobilization of Ca2+ from intracellular stores and is independent of the activation of the Ca(2+)-and phospholipid-dependent protein kinase C.

摘要

一种先前被归类于分化簇4(CD4)的单克隆抗体B66.6,已被研究并与另一种CD4单克隆抗体IOT4进行比较。研究发现,B66.6而非IOT4能够从Jurkat T细胞系的细胞内储存库中动员Ca2+。Ca2+动员之后,磷脂酰丝氨酸合成程度降低。在佛波酯佛波醇12,13 - 二丁酸存在的情况下,B66.6诱导白细胞介素-2合成。总之,结果表明CD4单克隆抗体B66.6模拟了其他T细胞激活剂如CD3,并证实活化T细胞中磷脂酰丝氨酸合成的抑制是继细胞内储存库中Ca2+动员之后发生的,且独立于Ca(2 +)和磷脂依赖性蛋白激酶C的激活。

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