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Insulin and insulin-like growth factor-I inhibit the L-type calcium channel current in rat pinealocytes

C L Chik1, B Li, E Karpinski

  • 1Department of Medicine, University of Alberta, Edmonton, Canada.

Endocrinology
|May 1, 1997
PubMed

Insights

Insulin and insulin-like growth factor-I (IGF-I) inhibit L-type calcium channel currents in rat pinealocytes. This effect involves tyrosine phosphorylation, highlighting a key signaling pathway in ion channel regulation.

Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Tyrosine phosphorylation is increasingly recognized as a regulator of ion channel function.
  • L-type calcium channels play crucial roles in cellular signaling and function, including in pinealocytes.

Purpose of the Study:

  • To investigate the effects of growth factors, specifically insulin and IGF-I, on L-type calcium channel currents in rat pinealocytes.
  • To elucidate the signaling pathways, particularly tyrosine phosphorylation, involved in mediating these effects.

Main Methods:

  • Whole-cell patch clamp technique was employed to measure L-type calcium channel currents.
  • Concentration-response relationships were determined for insulin and IGF-I.
  • Involvement of specific signaling molecules was assessed using inhibitors and antibodies (e.g., lavendustin A, calphostin C, anti-IGF-I receptor antibodies).

Main Results:

  • Both insulin and IGF-I significantly inhibited the L-type calcium channel current in a dose-dependent manner (EC50 values: 60 nM for insulin, 0.14 nM for IGF-I).
  • Heat-inactivated growth factors and other growth factors (NGF, EGF) did not affect the current.
  • The inhibitory effects were blocked by a tyrosine kinase inhibitor (lavendustin A) and attenuated by a protein kinase C inhibitor (calphostin C), but not by a PI3K inhibitor (wortmannin).
  • Anti-IGF-I receptor antibodies blocked IGF-I's inhibitory effect.

Conclusions:

  • Insulin and IGF-I exert an inhibitory effect on L-type calcium channel current in rat pinealocytes.
  • Tyrosine phosphorylation is a critical component of the signaling cascade mediating these inhibitory effects.
  • These findings reveal a novel mechanism of growth factor-mediated regulation of ion channel activity via tyrosine kinase pathways.

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