Premium
Plasma Membrane Calcium ATPase and Its Relationship to Nitric Oxide Signaling in the Heart
Author(s) -
CARTWRIGHT ELIZABETH J.,
OCEANDY DELVAC,
NEYSES LUDWIG
Publication year - 2007
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1387.007
Subject(s) - plasma membrane ca2+ atpase , calmodulin , nitric oxide , calcium , nitric oxide synthase , sodium calcium exchanger , microbiology and biotechnology , chemistry , signal transduction , cytosol , calcium pump , calcium signaling , contractility , calcium atpase , atpase , biochemistry , biophysics , biology , enzyme , endocrinology , organic chemistry
The plasma membrane calcium/calmodulin‐dependent ATPase (PMCA) is a ubiquitously expressed calcium‐extruding enzymatic pump. In the majority of cells the main function of PMCA is as the only system to extrude calcium from the cytosol, however, in the excitable cells of the heart it has only a minor role in the bulk removal of calcium compared to the sodium–calcium exchanger. There is increasing evidence to suggest that PMCA has an additional role as a potential modulator of a number of signal transduction pathways. Of key interest in the heart is the functional interaction between the calcium/calmodulin‐dependent enzyme neuronal nitric oxide synthase (nNOS) and isoform 4 of PMCA. Nitric oxide production from nNOS is known to be important in the regulation of excitation–contraction (EC) coupling and subsequently contractility. This article will focus on recent evidence suggesting that PMCA4 has a regulatory role in the nitric oxide signaling pathway in the heart.