Dynamics of Ca2+ and guanosine 5'-[gamma-thio]triphosphate action on insulin secretion from alpha-toxin-permeabilized HIT-T15 cells

Biochem J. 1994 Jul 15;301 ( Pt 2)(Pt 2):523-9. doi: 10.1042/bj3010523.

Abstract

The time course of Ca2+ and GTP-analogue effects on insulin secretion was investigated in HIT-T15 cells permeabilized with Staphylococcus alpha-toxin. These cells responded to Ca2+ in the range 0.1-10 microM and could be used in a dynamic perifusion system because of the minimal run-down of the secretory response. High Ca2+ (10 microM) elicited a monophasic ATP-dependent stimulation of insulin secretion that reached a peak within 5 min (approximately 20-fold increase) and rapidly decreased during the subsequent 15 min to a plateau remaining above basal rates (0.1 microM Ca2+). The decrease in Ca(2+)-induced insulin secretion with time could not be attributed to decreased capacity to respond to Ca2+ after prolonged perfusion at low Ca2+ (run-down), nor to depletion of a particular secretory-granule pool. It was rather due to desensitization of the secretory machinery to Ca2+ that was not reversed by selective inhibition of the Ca2+/calmodulin-dependent kinase II with KN-62. However, an intermediate Ca2+ concentration (2 microM) increased insulin secretion to stable level without causing any desensitization. Imposed oscillations of Ca2+ (0.1-10 microM) produced phasic oscillations of insulin secretion, but did not prevent desensitization to Ca2+. Poorly hydrolysable GTP analogues increased insulin secretion at low Ca2+, whereas they strongly inhibited Ca(2+)-induced insulin secretion. By contrast, GTP did not affect basal secretion, and slightly increased Ca(2+)-evoked secretion. These results indicate the following. (1) Oscillations of insulin secretion are tightly coupled to cytosolic Ca2+ oscillations. (2) Oscillations of Ca2+ do not prevent high-Ca(2+)-induced desensitization to Ca2+; this result does not support the idea of a greater efficiency of oscillations compared with sustained Ca2+ rises in triggering exocytosis. (3) Activation of G-proteins modulates exocytosis in a bimodal manner.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine* / analogs & derivatives*
  • Adenosine Triphosphate / pharmacology
  • Calcium / pharmacology*
  • Calcium-Calmodulin-Dependent Protein Kinases / antagonists & inhibitors
  • Cell Line
  • Cell Membrane Permeability*
  • Guanosine 5'-O-(3-Thiotriphosphate) / pharmacology*
  • Guanosine Triphosphate / pharmacology
  • Guanylyl Imidodiphosphate / pharmacology
  • Insulin / metabolism*
  • Insulin Secretion
  • Isoquinolines / pharmacology
  • Kinetics
  • Piperazines / pharmacology
  • Staphylococcus aureus
  • Type C Phospholipases / pharmacology*

Substances

  • Insulin
  • Isoquinolines
  • Piperazines
  • Guanylyl Imidodiphosphate
  • Guanosine 5'-O-(3-Thiotriphosphate)
  • KN 62
  • 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine
  • Guanosine Triphosphate
  • Adenosine Triphosphate
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Type C Phospholipases
  • Calcium