Amylin evokes phosphorylation of P20 in rat skeletal muscle

Yu Wang, Aimin Xu, Garth Cooper

Research output: Contribution to journalArticlepeer-review


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. Copyright (C) 1999 Federation of European Biochemical Societies.
Original languageEnglish
Pages (from-to)149-152
Number of pages3
JournalFEBS Letters
Issue number1
Publication statusPublished - 20 Aug 1999


  • Amylin
  • P20
  • Phosphorylation
  • Signal transduction


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