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B细胞激活。IV. 佛波酯诱导细胞膜去极化和I-A高表达表明蛋白激酶C在小鼠B淋巴细胞激活中起作用。

B cell activation. IV. Induction of cell membrane depolarization and hyper-I-A expression by phorbol diesters suggests a role for protein kinase C in murine B lymphocyte activation.

作者信息

Monroe J G, Niedel J E, Cambier J C

出版信息

J Immunol. 1984 Mar;132(3):1472-8.

PMID:6229582
Abstract

Analysis of the effects of phorbol diesters on mouse B lymphocyte kinase C activity, membrane potential, mI-A expression, and cell cycle state are reported. Results indicate that the phorbol diesters PMA and 4 beta-PDD, which are potent tumor promoters, activate partially purified B cell protein kinase C and stimulate B cell membrane depolarization and increased mI-A expression. The analog 4 alpha-PDD has none of these effects. Similarly, none of the phorbol diesters tested promoted G0 to G1 transition of B lymphocytes. Results are consistent with the possibility that the transmembrane signal transduction mediated by cell membrane immunoglobulin, which results in membrane depolarization and increased I-A antigen expression, operates via activation of protein kinase C.

摘要

本文报道了佛波酯对小鼠B淋巴细胞激酶C活性、膜电位、MHC I-A表达及细胞周期状态影响的分析结果。结果表明,强效肿瘤促进剂佛波酯PMA和4β-PDD可激活部分纯化的B细胞蛋白激酶C,刺激B细胞膜去极化并增加MHC I-A表达。类似物4α-PDD则无上述作用。同样,所测试的佛波酯均未促进B淋巴细胞从G0期向G1期的转变。这些结果与细胞膜免疫球蛋白介导的跨膜信号转导通过激活蛋白激酶C发挥作用的可能性一致,该信号转导可导致膜去极化和I-A抗原表达增加。

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