The protein tyrosine phosphatase alpha modifies insulin secretion in INS-1E cells

Biochem Biophys Res Commun. 2003 Nov 14;311(2):361-4. doi: 10.1016/j.bbrc.2003.10.011.

Abstract

Increasing evidence indicates a role of insulin signalling for insulin secretion from the pancreatic beta-cells. Therefore, regulators of insulin signalling, like protein tyrosine phosphatases, could also have an impact on insulin secretion. Here, we investigated a possible role of the negative regulator protein tyrosine phosphatase alpha (PTP alpha) for insulin secretion. RT-PCR analysis confirmed that both splice variants of the extracellular domain of PTP alpha that vary by an insert of 9 amino acids are expressed in human islets and insulinoma cells (INS-1E, RIN1046-38). Overexpression of the wild type PTP alpha splice variant containing the 9 amino acids reduced insulin secretion, as did a mutant form unable to bind Grb2 (Tyr798Phe). By contrast, overexpression of a phosphatase inactive mutant improved insulin secretion. These data reveal a functional relevance of PTP alpha for insulin secretion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line
  • Extracellular Space / metabolism
  • Gene Expression Regulation
  • Glucose / metabolism*
  • Humans
  • Insulin / metabolism*
  • Insulin Secretion
  • Islets of Langerhans / metabolism*
  • Protein Structure, Tertiary
  • Protein Tyrosine Phosphatases / genetics
  • Protein Tyrosine Phosphatases / metabolism*
  • Receptor-Like Protein Tyrosine Phosphatases, Class 4
  • Recombinant Proteins / metabolism
  • Signal Transduction / physiology*

Substances

  • Insulin
  • Recombinant Proteins
  • PTPRA protein, human
  • Protein Tyrosine Phosphatases
  • Receptor-Like Protein Tyrosine Phosphatases, Class 4
  • Glucose