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- W2048071350 endingPage "190" @default.
- W2048071350 startingPage "183" @default.
- W2048071350 abstract "Significant progress has been achieved in elucidating the role of the plasma membrane Ca2(+)-ATPase in cellular Ca2+ homeostasis and physiology since the enzyme was first purified and physiology since the enzyme was first purified and cloned a number of years ago. The simple notion that the PM Ca2(+)-ATPase controls resting levels of [Ca2+]CYT has been challenged by the complexity arising from the finding of four major isoforms and splice variants of the Ca2+ pump, and the finding that these are differentially localized in various organs and subcellular regions. Furthermore, the isoforms exhibit differential sensitivities to Ca2+, calmodulin, ATP, and kinase-mediated phosphorylation. The latter pathways of regulation can give rise to activation or inhibition of the Ca2+ pump activity, depending on the kinase and the particular Ca2+ pump isoform. Significant progress is being made in elucidating subtle and more profound roles of the PM Ca2(+)-ATPase in the control of cellular function. Further understanding of these roles awaits new studies in both transfected cells and intact organelles, a process that will be greatly aided by the development of new and selective Ca2+ pump inhibitors." @default.
- W2048071350 created "2016-06-24" @default.
- W2048071350 creator A5052949569 @default.
- W2048071350 creator A5083099452 @default.
- W2048071350 creator A5087976195 @default.
- W2048071350 date "1998-11-01" @default.
- W2048071350 modified "2023-10-18" @default.
- W2048071350 title "The plasma membrane calcium pump, its role and regulation: new complexities and possibilities" @default.
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- W2048071350 doi "https://doi.org/10.1016/s1056-8719(99)00004-0" @default.
- W2048071350 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10465152" @default.