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Ca 2+ ‐Transport ATPases and Their Regulation in Muscle and Brain
Author(s) -
WUYTACK F.,
RAEYMAEKERS L.,
SMEDT H.,
EGGERMONT J. A.,
MISSIAEN L.,
BOSCH L.,
JAEGERE S.,
VERBOOMEN H.,
PLESSERS L.,
CASTEELS R.
Publication year - 1992
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 - 10.1111/j.1749-6632.1992.tb43786.x
Subject(s) - serca , gene isoform , microbiology and biotechnology , plasma membrane ca2+ atpase , calmodulin , endoplasmic reticulum , biology , atpase , complementary dna , biochemistry , chemistry , gene , enzyme
Eukaryotic cells express one or more isoforms of a sarco(endo)plasmic reticulum (SERCA) and of a plasma membrane (PMCA) Ca2+ pump. Both the SERCA and PMCA gene transcripts are subject to alternative processing in a differentiation stage-dependent and tissue-dependent manner. The Ca2+ pump isoforms thus generated may present different functional properties. This is exemplified by the SERCA2a and SERCA2b isoforms which differ in their Ca2+ sensitivity. Analysis of the cDNA structures for PMCA1 predicts protein isoforms with variant calmodulin- and phospholipid-binding domains. A comparative study of the tissue-specific mechanisms governing SERCA-PMCA transcript processing and a more detailed study of the functional implication of the PMCA pumps isoform diversity will be challenging subjects for future studies.