DARPP-32 and inhibitor-1 are expressed in pancreatic β-cells

Lena Lilja, Björn Meister, Per Olof Berggren, Christina Bark

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

Insulin secretion from pancreatic β-cells has to be tightly regulated to ensure accurate glucose homeostasis. The capacity of β-cells to respond to extracellular stimulation is determined by several signaling pathways. One important feature of these pathways is phosphorylation and subsequent dephosphorylation of a wide range of cellular substrates. Protein phosphatase 1 (PP1) is a major eukaryotic serine/threonine protein phosphatase that controls a multitude of physiological processes. We have investigated the expression and cellular distribution of two endogenous inhibitors of PP1 activity in β-cells. RT-PCR, Western blotting, and immunohistochemistry showed that DARPP-32 and inhibitor-1 are present in insulin-secreting endocrine β-cells. Subcellular fractionation of mouse islets revealed that both PP1 inhibitors predominantly localized to cytosol-enriched fractions. Inhibitor-1 was also present in fractions containing plasma membrane-associated proteins. These data indicate a potential role for DARPP-32 and inhibitor-1 in the regulation of PP1 activity in pancreatic β-cell stimulus-secretion coupling.

Original languageEnglish (US)
Pages (from-to)673-677
Number of pages5
JournalBiochemical and biophysical research communications
Volume329
Issue number2
DOIs
StatePublished - Apr 8 2005

Keywords

  • Dephosphorylation
  • Exocytosis
  • Immunohistochemistry
  • Insulin
  • Phosphatase
  • PP1 inhibitor
  • RT-PCR
  • Secretion
  • Subcellular fractionation

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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