Abstract
The plasma membrane Ca2+ ATPase has been first described in erythrocytes by Schatzmann (1966) and is now known to be present in all cells of higher eucaryotes. The pump belongs to the family of P-type ATPases (Pedersen & Carafoli, 1987a; Pedersen & Carafoli, 1987b), i.e., it forms an aspartyl-phosphate during the reaction cycle. It is a target of calmodulin (Gopinath & Vincenzi, 1977; Jarret & Penniston, 1977), which increases its affinity for Ca2+ by one order of magnitude, to a Kd of about 0.5 µM. The pump, however, can also be activated by a number of alternative treatments: the exposure to acidic phospholipids (Ronner et al., 1977; Niggli et al., 1981a), a controlled proteolytic treatment (Enyedi et al., 1980; Caroni & Carafoli, 1981), phosphorylations by two protein kinases, (protein kinase A (PKA) (Caroni & Carafoli, 1981) and protein kinase C (PKC) (Wright et al., 1993; Furukawa et al., 1989)), and an oligomerization process (Kosk-Kosicka & Bzdega, 1988). By general consensus, calmodulin is considered the natural modulator of the pump, but it is well to remember that the pump in the membrane is surrounded by amounts of acidic phospholipids which are, in principle, sufficient for half-maximal activation (Niggli et al., 1981b). The interaction with calmodulin has been exploited to purify the pump using calmodulin columns (Niggli et al., 1981 b). The purified enzyme is active, and can be reconstituted in liposomes with optimal Ca2+ transport efficiency (Niggli, et al., 1981c): at variance with the Ca2+ pump of sarcoplasmic reticulum, whose Ca2+/ATP molar transport stoichiometry is 2.0, the pump transports only one Ca2+ per ATP hydrolyzed.
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Carafoli, E., Guerini, D. (1997). The Plasma Membrane Calcium Pump. In: Sotelo, J.R., Benech, J.C. (eds) Calcium and Cellular Metabolism. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9555-4_7
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DOI: https://doi.org/10.1007/978-1-4757-9555-4_7
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