Regulation of Mg2+ uptake in isolated rat myocytes and hepatocytes by protein kinase C

FEBS Lett. 1992 Jan 20;296(2):135-40. doi: 10.1016/0014-5793(92)80364-m.

Abstract

A large Mg2+ cell uptake against concentration gradients is stimulated in collagenase-dispersed rat myocytes by carbachol and in hepatocytes by carbachol or vasopressin. The signalling pathway(s) responsible for this stimulation of Mg2+ uptake was investigated by using various activators or inhibitors of protein kinase C (PKC) and by correlating Mg2+ uptake with cell PKC activity and cAMP content. In both cell preparations, the direct stimulation of PKC by diacylglycerol analogs or phorbol esters reproduce the same pattern of Mg2+ uptake as that induced by carbachol or vasopressin. These data indicate that the activation of PKC is responsible for a stimulation of Mg2+ uptake by myocytes or hepatocytes, whereas increase in cAMP in these cells stimulates Mg2+ release.

MeSH terms

  • Animals
  • Carbachol / pharmacology
  • Cell Fractionation
  • Cyclic AMP / metabolism
  • Diglycerides / pharmacology
  • Liver / cytology
  • Liver / drug effects
  • Magnesium / metabolism*
  • Male
  • Muscles / cytology
  • Muscles / drug effects
  • Phorbol Esters / pharmacology
  • Protein Kinase C / antagonists & inhibitors
  • Protein Kinase C / metabolism*
  • Rats
  • Rats, Inbred Strains
  • Signal Transduction / drug effects
  • Signal Transduction / physiology*
  • Vasopressins / pharmacology

Substances

  • Diglycerides
  • Phorbol Esters
  • Vasopressins
  • Carbachol
  • Cyclic AMP
  • Protein Kinase C
  • Magnesium