Induction of apoptosis by human amylin in RINm5F islet beta-cells is associated with enhanced expression of p53 and p21WAF1/CIP1

FEBS Lett. 1999 Jul 23;455(3):315-20. doi: 10.1016/s0014-5793(99)00894-7.

Abstract

Human amylin (10 microM) significantly inhibited RINm5F islet beta-cell proliferation and evoked apoptosis associated with typical degenerative ultrastructural changes and DNA fragmentation, whereas rat amylin did not. Time course analysis showed that human amylin elicited apoptosis in a passage-dependent manner. Expression of the apoptosis-related genes p53, bcl-2 and WAF1/CIP1 was examined using Northern blots. mRNAs corresponding to p53 and to p21WAF/CIP1 were remarkably increased following human amylin treatment, whereas no change in bcl-2 was detected. Our data suggest a role of p53 and p21 in human amylin-induced beta-cell apoptosis. Furthermore, cells with higher proliferative potential (lower passage) were found to be more susceptible to apoptosis and to induction of p53, suggesting that beta-cells with different proliferation rates respond differently to human amylin, and that human amylin may be more toxic to proliferating cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid / pharmacology*
  • Animals
  • Apoptosis / drug effects*
  • Apoptosis / genetics*
  • Base Sequence
  • Cell Division / drug effects
  • Cell Line
  • Cyclin-Dependent Kinase Inhibitor p21
  • Cyclins / genetics*
  • DNA Fragmentation / drug effects
  • DNA Primers / genetics
  • Gene Expression / drug effects
  • Genes, p53 / drug effects*
  • Humans
  • Islet Amyloid Polypeptide
  • Islets of Langerhans / cytology
  • Islets of Langerhans / drug effects*
  • Islets of Langerhans / metabolism*
  • Microscopy, Electron, Scanning
  • Rats

Substances

  • Amyloid
  • CDKN1A protein, human
  • Cdkn1a protein, rat
  • Cyclin-Dependent Kinase Inhibitor p21
  • Cyclins
  • DNA Primers
  • Islet Amyloid Polypeptide