Phospholamban: Protein Structure, Mechanism of Action, and Role in Cardiac Function
- 1 October 1998
- journal article
- review article
- Published by American Physiological Society in Physiological Reviews
- Vol. 78 (4) , 921-947
- https://doi.org/10.1152/physrev.1998.78.4.921
Abstract
Simmerman, Heather K. B., and Larry R. Jones. Phospholamban: Protein Structure, Mechanism of Action, and Role in Cardiac Function. Physiol. Rev. 78: 921–947, 1998. — A comprehensive discussion is presented of advances in understanding the structure and function of phospholamban (PLB), the principal regulator of the Ca2+-ATPase of cardiac sarcoplasmic reticulum. Extensive historical studies are reviewed to provide perspective on recent developments. Phospholamban gene structure, expression, and regulation are presented in addition to in vitro and in vivo studies of PLB protein structure and activity. Applications of breakthrough experimental technologies in identifying PLB structure-function relationships and in defining its interaction with the Ca2+-ATPase are also highlighted. The current leading viewpoint of PLB's mechanism of action emerges from a critical examination of alternative hypotheses and the most recent experimental evidence. The potential physiological relevance of PLB function in human heart failure is also covered. The interest in PLB across diverse biochemical disciplines portends its continued intense scrutiny and its potential exploitation as a therapeutic target.Keywords
This publication has 252 references indexed in Scilit:
- Phospholamban: A Protein Coming of AgeBiochemical and Biophysical Research Communications, 1997
- The Secondary Structure of Phospholamban: A Two-Dimensional NMR StudyBiochemical and Biophysical Research Communications, 1995
- Cyclic GMP-Mediated Phospholamban Phosphorylation in Intact CardiomyocytesBiochemical and Biophysical Research Communications, 1995
- Structural Model of the Phospholamban Ion Channel Complex in Phospholipid MembranesJournal of Molecular Biology, 1995
- Role of phospholamban in No/EDRF-induced relaxation in rat aortaLife Sciences, 1992
- Identification of a highly conserved region at the 5′ flank of the phospholamban geneBiochemical and Biophysical Research Communications, 1992
- Secondary structure of detergent-solubilized phospholamban, a phosphorylatable, oligomeric protein of cardiac sarcoplasmic reticulumBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1989
- Characterization of structural unit of phospholamban by amino acid sequencing and electrophoretic analysisBiochemical and Biophysical Research Communications, 1986
- Phospholamban, the regulator of the cardiac sarcoplasmic reticulum calcium pump, does not copurify with the Ca2+-ATPase enzymeBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
- Isolation of phospholamban and a second proteolipid component from canine cardiac sarcoplasmic reticulumBiochemical and Biophysical Research Communications, 1981