Involvement of Sarco/endoplasmic Reticulum Ca2+ ATPases in Cell Function and the Cellular Consequences of Their Inhibition

Involvement of Sarco/endoplasmic Reticulum Ca2+ ATPases in Cell Function and the Cellular... J. Membrane Biol. 172, 91–99 (1999) The Journal of Membrane Biology © Springer-Verlag New York Inc. 1999 Topical Review 2+ Involvement of Sarco/endoplasmic Reticulum Ca ATPases in Cell Function and the Cellular Consequences of Their Inhibition A. Hussain, G. Inesi Department of Biochemistry, Division of Oncology of the Department of Medicine, Greenebaum Cancer Center, University of Maryland, School of Medicine, and the Veterans Affairs Medical Center, Baltimore, MD 21201, USA Received: 14 June 1999/Revised: 5 August 1999 Introduction affecting function of luminal chaperones like Bip [31]), membrane trafficking between the endoplasmic reticu- lum and golgi complex [42], nucleo-cytoplasmic trans- Calcium serves as an important signaling molecule that port [75], and regulation of the store-operated calcium modulates diverse cellular processes. Elevation of cyto- 2+ 2+ currents I [73]. CRAC solic Ca (Ca ) follows the activation of many cell 2+ The sarco/endoplasmic reticulum Ca transport surface receptors as well as depolarization of neuronal 2+ ATPase (SERCA) plays a fundamental role in regulating and muscle tissues [4]. Such Ca transients can regulate 2+ 2+ cytosolic Ca signals, as well as Ca within the endo- gene transcription in a variety of cells including, among plasmic reticulum (ER), the sarcoplasmic reticulum (SR) others, http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Membrane Biology Springer Journals

Involvement of Sarco/endoplasmic Reticulum Ca2+ ATPases in Cell Function and the Cellular Consequences of Their Inhibition

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Publisher
Springer-Verlag
Copyright
Copyright © Inc. by 1999 Springer-Verlag New York
Subject
Life Sciences; Biochemistry, general; Human Physiology
ISSN
0022-2631
eISSN
1432-1424
D.O.I.
10.1007/s002329900587
Publisher site
See Article on Publisher Site

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