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蛋白激酶C在成纤维细胞向血小板衍生生长因子和纤连蛋白片段趋化过程中的信号转导作用。

Involvement of protein kinase C in signal transduction during fibroblast chemotaxis to platelet-derived growth factor and a fragment of fibronectin.

作者信息

Adelmann-Grill B C, Wach F, Behr J, Krieg T

机构信息

Max-Planck-Institut für Biochemie, Planegg-Martinsried/Bundesrepublik Deutschland.

出版信息

Eur J Cell Biol. 1989 Oct;50(1):128-31.

PMID:2612499
Abstract

The involvement of protein kinase C in chemotaxis of normal dermal fibroblasts to a mitogenic and a non-mitogenic attractant was investigated. Neomycin, an inhibitor of phosphoinositide metabolism, H7, staurosporine, and sphingosine, inhibitors of protein kinase C, as well as amiloride, an inhibitor of the Na+/H+-antiport, all abrogated chemotaxis of fibroblasts to platelet-derived growth factor and to a chemotactically active fragment of fibronectin. Down-regulation of protein kinase C by phorbol ester likewise diminished the capacity of fibroblasts to move directionally to these attractants. Therefore, all three of these signal transduction steps are required for the chemotactic response of this type of cells.

摘要

研究了蛋白激酶C在正常真皮成纤维细胞对有丝分裂原和非有丝分裂原趋化因子趋化作用中的参与情况。新霉素(一种磷酸肌醇代谢抑制剂)、H7、星形孢菌素和鞘氨醇(蛋白激酶C抑制剂)以及氨氯吡脒(一种Na+/H+反向转运体抑制剂)均消除了成纤维细胞对血小板衍生生长因子和纤连蛋白趋化活性片段的趋化作用。佛波酯对蛋白激酶C的下调同样降低了成纤维细胞向这些趋化因子定向移动的能力。因此,这三种信号转导步骤对于这类细胞的趋化反应都是必需的。

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