Interaction of plasma membrane Ca(2+)-ATPase isoform 4 with calcineurin A: implications for catecholamine secretion by PC12 cells

Biochem Biophys Res Commun. 2011 Jul 29;411(2):235-40. doi: 10.1016/j.bbrc.2011.06.098. Epub 2011 Jun 26.

Abstract

PMCA1-4 isoforms have been recently recognised as regulators of various signalling pathways in mammalian cells. PMCAs were found to interact with calcineurin A in an isoform specific manner. In this study we focus on the interaction of calcineurin A with PMCA4 and its effect on catecholamine secretion in PC12 cells with reduced PMCA2 or PMCA3 content. Reduction of synthesis of PMCA2 or PMCA3 led to upregulation of PMCA4 manifested by preferential interaction of PMCA4 with calcineurin A. On the other hand, we observed a significant reduction of dopamine secretion, which did not correspond with an increased [Ca(2+)](c). This result indicates that the interaction of PMCA4 with calcineurin A plays a regulatory role in the signalling during catecholamine secretion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calcineurin / metabolism*
  • Catecholamines / metabolism*
  • Isoenzymes / genetics
  • Isoenzymes / metabolism
  • PC12 Cells
  • Plasma Membrane Calcium-Transporting ATPases / genetics
  • Plasma Membrane Calcium-Transporting ATPases / metabolism*
  • Rats
  • Up-Regulation

Substances

  • Catecholamines
  • Isoenzymes
  • Calcineurin
  • Plasma Membrane Calcium-Transporting ATPases