Titlebook: Regulation of Ca2+-ATPases,V-ATPases and F-ATPases; Sajal Chakraborti,Naranjan S Dhalla Book 2016 Springer International Publishing Switze

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PMCA3: A Mysterious Isoform of Calcium Pumpls to the cells. The most sensitive for changes in cytosolic Ca. concentration is a family of plasma membrane calcium (PMCA) pump encoded by four independent genes (PMCA1–4). Differences in tissue-specific expression of the isoforms and splicing variants in excitable and non-excitable cells are cons

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The Ca2+ ATPase of the Sarco-/Endoplasmic Reticulum (SERCA): Structure and Controleticulum. In muscle cells its ability to remove Ca. from the cytosol induces relaxation. The transport mechanism employed by SERCA1a from rabbit skeletal muscle has been dissected at the molecular level by several crystal structures that represent nearly all the different conformational states of th

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Functional and Structural Insights into Sarcolipin, a Regulator of the Sarco-Endoplasmic Reticulum Cess. A number of enzymological studies have underlined its regulatory role in connection with the SERCA1a activity. Indeed, SLN folds as a unique transmembrane helix and binds to SERCA1a in a groove close to transmembrane helices M2, M6, and M9, as proposed initially by cross-linking experiments and

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Regulation of Cardiac Sarco(endo)plasmic Reticulum Calcium-ATPases (SERCA2a) in Response to Exercise SERCA2a is primarily responsible for transporting Ca. out of the cytosol into the sarcoplasmic reticulum. Consequently, SERCA2a is key in determining relaxation time and inotropy of subsequent contractions. There are ten different SERCA isoforms in the body, where SERCA2a is the isoform expressed i

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