Ca2+-transporting ATPase

PS Reinach, N Holmbeg, R Chiesa. (1991). Identification of calmodulin-sensitive Ca2+-transporting ATPase in the plasma membrane of bovine corneal epithelial cell. Biochim Biophys Acta 1068 1-8. 

The organization of lipids around the plasma membrane Ca2+-transport ATPase of erythrocytes has been also determined by FRET. Taking advantage of the intrinsic fluorescence of the ATPase due to tryptophan residues and labeling different types of lipids with pyrene, it was demonstrated that the transporter is preferentially surrounded by negatively charged lipids such as phosphoinositides [167],... 

Verbist, J., Gadella, T. W. J., Raeymaekers, L., Wuytack, F., Wirtz, K. W. A. and Casteels, R. (1991). Phosphoinositide-protein Interactions of the plasma-membrane Ca2+-transport ATPase as revealed by fluorescence energy-transfer. Biochim. Biophys. Acta 1063, 1-6. 

Inesi G, Sagara Y 1994 Specific inhibitors of intracellular Ca2+ transport ATPases. J Membr Biol... 

Raeymaekers L, Wuytack F 1996 Calcium Pumps. In Barany M (ed) Biochemistry of smooth muscle contraction. Academic Press, New York, p 241-253 Shull GE 2000 Gene knockout studies of Ca2+-transporting ATPases. Eur J Biochem 267 5284-5290... 

Janik F, Wolf HU. 1992. The Ca2+-transport-ATPase of human erythrocytes as an in vitro toxicity test system—acute effects of some chlorinated compounds. J Appl Toxicol 12 351-358. 

J. M. Vanderkooi, A. Ierokomas, H. Nakamura, and A. Martonosi, Fluorescence energy transfer between Ca2+ transport ATPase molecule in artifical membranes, Biochemistry 16, 1262-1267 (1977). 

Ton, V.K. and Rao, R. Functional expression of heterologous proteins in yeast Insights into Ca2+ signalling and Ca2+-transporting ATPases. Am J Physiol 287 C580-C589, 2004. 

Greeb, J., Shull, G.E., 1989, Molecular cloning of a third isoform of the calmodulin-sensitive plasma membrane Ca2+-transporting ATPase that is expressed predominantly in brain and skeletal muscle. J Biol Chem 264, 18569-18576. 

Abstract Secretory-pathway Ca2+-transport ATPases (SPCA) provide the Golgi apparatus with... 

Figure 1. Phylogenetic tree of P2A and 2 B subfamilies of Ca2+-transporting ATPases. Protein sequences of P-type ATPases of different species were aligned using ClustalW software and a phylogenetic tree was generated using TreeView. Three different branches representing die three main subtypes of Ca2+-ATPases are apparent SERCAs, PMCAs and SPCAs...

Yamamoto, H., Imamura, Y., Tagaya, M., Fukui, T Kawakita, M. (1989). Ca2+-dependent conformational change of the ATP-binding site of Ca2+-transporting ATPase of sarcoplasmic reticulum as revealed by an alteration of the target-site specificity of adenosine triphosphopyridoxal. J. Biochem. 106,1121-1125. 

Shull, G.E. Greeb, J. (1988). Molecular cloning of two isoforms of the plasma membrane Ca2+ transporting ATPase from rat brain. Structural and functional domains exhibit similarity to Na+, K+- and other cation transport ATPases. J. Biol. Chem. 263, 8646-8657. 

Sarcoplasmic reticulum Ca2+-transporting ATPase (SR-ATPase) is a member of the ATPase family that couples ion translocation across cell membranes to hydrolysis. There... 

The level of calcium in the cell is low, about 0.1 //M compared with approximately 1.3 mM outside the cell. The intracellular concentration is kept low by the activity of transport systems which transport calcium out of the cell and sequester it in the mitochondria and endoplasmic reticulum. The plasma membrane thus houses a Ca2+ transporting ATPase, as does the endoplasmic reticulum and nucleus. Calcium may also be stored in the mitochondria, and the intracellular protein calmodulin will bind calcium. Interference with any of these processes may be caused by toxic compounds and can alter calcium homeostasis. This can allow an influx of Ca2+, inhibition of export of Ca2+ out of the cell, or a release of Ca2+ from compartments within the cell. The result of each of these will be a rise of intracellular Ca2+ which can cause a variety of damaging events. 

Our knowledge on the structure of Ca2+-ATPases is mainly based on studies of the Ca + pump of the SR of fast skeletal muscle (a SERCAl gene product). However, the general structural model that emerged from these studies is probably also valid for the other SERCAs as well as for the PM Ca + pump. The predicted structure of the Ca2+-transport ATPase incorpo-... 

Ca2+-transport ATPases [PMCA (Niggli et al., 1982) as well as SERCA (Martonosi et al., 1985)] operate as obligatory Ca2+-H+ exchangers. Since the number of protons exchanged for Ca + has not been firmly es-... 

Barzilai A, Rahamimoff H. Inhibition of Ca2+-transport ATPase from synaptosomal vesicles hy flavonoids. Biochim Biophys Acta 1983 730 245-254. 

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