A role of calcyclin, a Ca(2+)-binding protein, on the Ca(2+)-dependent insulin release from the pancreatic beta cell

Abstract

Exocytosis is an important example of cell activation. Ca2+ and calcium-binding proteins are considered to modulate signal transduction in exocytosis. We examined the role of calcyclin, calcium-binding protein, in the stimulus-secretion coupling in pancreatic beta cells. The presence of calcyclin in these cells was demonstrated immunologically. We permeabilized rat pancreatic islets with streptolysin-O and examined the effects of calcyclin on insulin release. The Ca(2+)-stimulated insulin release was enhanced by calcyclin, in a dose-dependent manner, whereas this calcium-binding protein had no effect on insulin release from islets in low Ca2+ buffer or from the islets not subjected to the streptolysin-O treatment. Calgizzarin, another member of the S-100 protein family, had no apparent effect on the Ca(2+)-stimulated secretion under parallel conditions. An anticalcyclin antibody suppressed the increase in insulin release induced by calcyclin. We propose that calcyclin may be involved in signal transduction of the Ca(2+)-induced release of insulin.