Amylin evokes phosphorylation of P20 in rat skeletal muscle

FEBS Letters

Wang, Yu¹  Cooper, Garth J.S¹  Xu, Aimin¹ 

[1] The School of Biological Sciences, Level 4, University of Auckland, Private Bag 92019, Auckland, New Zealand

关键词: Amylin;    P20;    Phosphorylation;    Signal transduction;    ARPP;    amylin-responsive phosphoprotein;    CGRP;    calcitonin gene-related peptide;    2-DE;    two-dimensional gel electrophoresis;    HSP;    heat shock protein;    EDL;    extensor digitorum longus;   

DOI  :  10.1016/S0014-5793(99)01029-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

To investigate the signal transduction events underlying amylin's actions, the amylin-evoked protein phosphorylation cascade was analysed using two-dimensional gel electrophoresis. We found that phosphorylation of three isoelectric variants of P20 (termed ARPP1, ARPP2 and ARPP3) was associated with amylin's actions in rat skeletal muscle. Amylin decreased phosphorylation of ARPP1 and increased phosphorylation of ARPP2 and ARPP3 in a dose-dependent manner. Insulin inhibited amylin-evoked phosphorylation of ARPP2 and ARPP3. The amylin-selective antagonist rat amylin-(8–37) completely reversed amylin's action on ARPP3 and partially decreased phosphorylation of ARPP2. By contrast, the CGRP-selective antagonist, human CGRP-(8–37) blocked phosphorylation of ARPP2 but had little effect on ARPP3. These results suggest that amylin modifies phosphorylation of P20 via two independent mechanisms, and that P20 might be a molecule mediating amylin's biological functions.

【 授权许可】

Unknown