首页> 外文期刊>Journal of receptor and signal transduction research >Association of insulin receptor and syndecan-1 by insulin with activation of ERK I/II in osteoblast-like UMR-106 cells
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Association of insulin receptor and syndecan-1 by insulin with activation of ERK I/II in osteoblast-like UMR-106 cells

机译:胰岛素受体和syndecan-1被胰岛素与成骨样UMR-106细胞中ERK I / II活化的关系

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摘要

Insulin plays an important role in various metabolic as well as anabolic actions in cells, including osteoblast cells. In the present study, we explored to determine if insulin receptor could associate with syndecan-1 in response to insulin and such association could lead to the activation of subsequent ERK I/II and alkaline phosphatase (ALP) in osteoblast cells. Insulin rapidly induces the association of insulin receptor with syndecan-1. Synstatin is a specific peptide inhibitor that blocks the binding of syndecan-1 to integrate. In the presence of synstatin, insulin-stimulated ERK I/II activation was dramatically inhibited, suggesting that syndecan-1/integrin interaction is essential in the activation of ERK I/II by insulin. Pretreatment of synstatin also inhibited the insulin-stimulated ALP activity. Taken together, these results suggest that insulin stimulates the association of insulin receptor with syndecan-1 and the complex formation of syndecan-1 and integrin could play an important role in ERK I/II—ALP signaling pathway in osteoblast cells.
机译:胰岛素在细胞(包括成骨细胞)的各种代谢以及合成代谢作用中起着重要作用。在本研究中,我们探索确定胰岛素受体是否可以响应胰岛素而与syndecan-1结合,并且这种结合可能导致成骨细胞中随后的ERK I / II和碱性磷酸酶(ALP)活化。胰岛素迅速诱导胰岛素受体与syndecan-1缔合。 Synstatin是一种特殊的肽抑制剂,可阻断syndecan-1的结合从而整合。在存在synstatin的情况下,胰岛素刺激的ERK I / II激活被显着抑制,这表明syndecan-1 / integrin相互作用对于胰岛素激活ERK I / II至关重要。 Synstatin的预处理也抑制了胰岛素刺激的ALP活性。综上所述,这些结果表明胰岛素刺激了胰岛素受体与syndecan-1的缔合,并且syndecan-1和整联蛋白的复杂形成可能在成骨细胞的ERK I / II-ALP信号通路中发挥重要作用。

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