Abstract
Calcium-pum** membrane ATPases play the essential function of terminating Ca2+-dependent responses. Two broad classes of Ca2+-pum** ATPases are now known to exist in animal cells, those of internal membranes (100 kDa) and the plasma membrane enzymes (120–140 kDa). These two families of Ca2+-pum** ATPases differ substantially in molecular, enzymatic and regulatory properties commensurate with their differiential localization and physiological roles. Recent studies in a number of laboratories have provided evidence that multiple isoforms of each type of Ca2+ -ATPase are produced in different cell types as products of either differential splicing events or different genes. These sets of isoforms are almost certain to have subtle differences in functional properties related to the requirements of a particular biological setting.
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© 1989 Plenum Press, New York
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Mann, D.M., Brandt, P., Sisken, B., Vanaman, T.C. (1989). Identification of a Synaptic Membrane-Localized Isoform of the Calcium-Pum** ATPase. In: Hidaka, H., Carafoli, E., Means, A.R., Tanaka, T. (eds) Calcium Protein Signaling. Advances in Experimental Medicine and Biology, vol 255. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5679-0_8
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DOI: https://doi.org/10.1007/978-1-4684-5679-0_8
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