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首页> 外文期刊>Journal of Cellular Physiology >Phosphorylated form of MacMARCKS is essential to LFA-1-dependent cell-cell adhesion of U937 monocytic cells.
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Phosphorylated form of MacMARCKS is essential to LFA-1-dependent cell-cell adhesion of U937 monocytic cells.

机译:磷酸化形式的MacMARCKS是至关重要的LFA-1-dependent信息U937的附着力单核细胞的细胞。

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摘要

MacMARCKS (MRP, F52), a protein kinase C (PKC) substrate, is involved in the activation of beta2-integrin. To determine the role of the PKC-mediated phosphorylation of MacMARCKS in this process, human U937 monocytic cells were transfected with cDNAs encoding wild type or mutant MacMARCKS. We observed that the expression of the exogenous wild type MacMARCKS greatly enhanced LFA-1-mediated cell-cell adhesion in U937 cells treated with phorbol 12-myristate 13-acetate (PMA). This MacMARCKS-stimulated adhesion depended on the phosphorylation status of MacMARCKS: whereas phosphorylated MacMARCKS enhanced adhesion, unphosphorylated MacMARCKS inhibited it. However, phosphorylated MacMARCKS alone could not induce LFA-1-mediated cell-cell adhesion unless phorbol esters were added, suggesting that the phosphorylation of other proteins might also be involved. Okadaic acid, a phosphatase inhibitor, induced LFA-1-mediated cell-cell adhesion only in the cells expressing wild type or phosphorylated MacMARCKS and not in the cells expressing unphosphorylated MacMARCKS. Therefore, we conclude that the phosphorylated form of MacMARCKS is essential to LFA-1-mediated cell-cell adhesion. Copyright 1999 Wiley-Liss, Inc.
机译:F52 MacMARCKS (MRP),蛋白激酶C (PKC)衬底,参与激活的beta2-integrin。PKC-mediated MacMARCKS的磷酸化过程,人类U937单核细胞的细胞转染野生型或互补dna编码变异MacMARCKS。外生的野生型MacMARCKS很大增强LFA-1-mediated信息附着力U937细胞接受佛波醇12-myristate13-acetate (PMA)。附着力取决于磷酸化状态MacMARCKS:而磷酸化MacMARCKS磷酸化MacMARCKS增强附着力抑制它。独自一人不可能诱发LFA-1-mediated信息附着力,除非添加了佛波醇酯,这表明其他的磷酸化蛋白质也参与其中。磷酸酶抑制剂,诱导LFA-1-mediated信息只在细胞表达粘附野生型或磷酸化MacMARCKS而不是细胞表达磷酸化MacMARCKS。因此,我们得出这样的结论:磷酸化形式的MacMARCKS对LFA-1-mediated至关重要信息附着力。公司。

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