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- W1504409981 endingPage "248" @default.
- W1504409981 startingPage "205" @default.
- W1504409981 abstract "This chapter discusses differential expression and the physiological meaning of the Ca2+-transport ATPase isoforms involved in intracellular Ca2+ accumulation. The chapter describes the diversity of the eukaryotic Ca2+-transport ATPases in intracellular Ca2+–storage sites. Data on vertebrates, as well as on invertebrates and non-animal species is also included in the chapter. Since alternative processing of primary gene transcripts contributes to the isoform diversity and focuses to alternative transcript processing in Ca2+–transport ATPases and to the mechanisms controlling them. The chapter deals with the regulatory proteins of the Ca2+-transport ATPases, through which the different signal-transduction pathways control the ATPase activity. The chapter discusses various factors controlling tissue-dependent expression of Ca2+-transport ATPases in both health and disease. Both in excitable and inexcitable cells, intracellular Ca2+ stores play a central role in cellular Ca2+ signaling, and in the maturation and targeting of secreted and membrane proteins. Multiple isoforms of Ca2+-transport ATPases accumulate Ca2+ in the stores. The first class of these enzymes is represented by the sarcoen doplasmic reticulum Ca2+–ATPases (SERCA) family. This chapter discusses the different P-type Ca2+–transport ATPases in non-vertebrate species. The mechanisms controlling alternative splicing underlying SERCA2a/b isoform diversity and the functional meaning of the diversity are more extensively explored the chapter." @default.
- W1504409981 created "2016-06-24" @default.
- W1504409981 creator A5016643155 @default.
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- W1504409981 creator A5037743096 @default.
- W1504409981 creator A5040620080 @default.
- W1504409981 creator A5074790932 @default.
- W1504409981 date "1997-01-01" @default.
- W1504409981 modified "2023-09-25" @default.
- W1504409981 title "Isoform Diversity and Regulation of Organellar-Type Ca2+-Transport ATPases" @default.
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