Sarcoplasmic reticulum Ca2+ ATPase

The structure and mechanism of the sarcoplasmic reticulum Ca2+-ATPase a bioinorganic perspective. E. M. Stephens andC. M. Grisham, Adv. Inorg. Biochem., 1982, 4, 263-288 (151). 

Mahaney, J. E., Thomas, D. D. and Froehlich, J. P. The time-dependent distribution of phosphorylated intermediates in native sarcoplasmic reticulum Ca2+-ATPase from skeletal muscle is not compatible with a linear kinetic model. Biochemistry 43 4400-4416, 2004. 

Odermatt, A., Taschner, P. E., Khanna, V. K. etal. Mutations in the gene-encoding SERCA1, the fast-twitch skeletal muscle sarcoplasmic reticulum Ca2+ ATPase, are associated with Brody disease. Nat. Genet.lA. 191-194,1996. 

A spin label was attached by photoaffinity to the nucleotide binding site of sarcoplasmic reticulum Ca2+-ATPase.56 Dipolar interaction corresponding to an interspin distance of about 15 A was observed, which demonstrated that the minimal functional unit is a dimer with the nucleotide-binding sites of the two monomers in close proximity. 

Teshima, Y., Takahashi, N., Saikawa, T., Hara, M., Yasunaga, S., Hidaka, S., and Sakata, T. (2000). Diminished Expression of Sarcoplasmic Reticulum Ca2+-ATPase and Ryanodine Sensitive Ca2+ Channel mRNA in Streptozotocin-Induced Diabetic Rat Heart. J Mol Cell Cardiol 32(4) 655-64. 

Moller, J.V., Nissen, P., Sorensen, T.L., le Maire, M., 2005, Transport mechanism of the sarcoplasmic reticulum Ca2+-ATPase pump. Curr Opin Struct Biol 15, 387—393. 

Clarke, D.M., Loo, T.W., Inesi, G., and MacLennan, D.H., 1989, Location of high affinity Ca2+-binding sites within die predicted transmembrane domain of the sarcoplasmic reticulum Ca2+-ATPase. Nature... 

Dode, L., Andersen, J.P., Raeymaekers, L., Missiaen, L., Vilsen, B., and Wuytack, F., 2005, Functional comparison between secretory pathway Ca2+/Mn2+-ATPase (SPCA) 1 and sarcoplasmic reticulum Ca2+-ATPase (SERCA) 1 isoforms by steady-state and transient kinetic analyses. J. Biol. Chem. 280, 39124-39134... 

Flavonoids can affect the function of plasma membrane transport Na+- and K+-ATPase, mitochondrial ATPase, and Ca2+-ATPase. The Mg2+-ectoATPase of human leukocytes is inhibited by quercetin, which acts as a competitor of ATP binding to the enzyme. The sarcoplasmic reticulum Ca2+-ATPase of muscle is effectively inhibited by several flavonoids that were also active inhibitors of antigen-induced mast cell histamine release. 

The present paper will outline some of our recent EPR and NMR studies using Mn2+ as a paramagnetic probe of sheep kidney (Na+ + K+)-ATPase and Gd2+ as a paramagnetic probe of sarcoplasmic reticulum Ca2+-ATPase. Estimates of the relevant electron spin relaxation times and some features of the interaction between substrates and activators with the enzyme-metal complexes will be inferred from the EPR spectra and the accompanying nuclear relaxation data. 

Andersen, J.P. Vilsen, B. (1992a). Structural basis for the E]/E P-E2/E2P conformation changes in the sarcoplasmic reticulum Ca2+-ATPase studied by site-specific mutagenesis. Acta Physiol. Scand. 146,151-159. 

De Foresta, B Champeil, P., Le Maire, M. (1990). Different classes of tryptophan residues involved in the conformational changes characteristic of the sarcoplasmic reticulum Ca2+-ATPase cycle. Eur. J. Biochem. 194,383-388. 

De Meis, L. (1991). Fast effux of Ca2+ mediated by the sarcoplasmic reticulum Ca2+-ATPase. J. Biol. Chem. 266, 5736-5742. 

McIntosh, D.B., Ross, D.C., Champeil, P., Guillain, F. (1991). Crosslinking the active site of sarcoplasmic reticulum Ca2+-ATPase completely blocks Ca2+ release to the vesicle lumen. Proc. Natl. Acad. Sci. USA 88,6437-6441. 

Orlowski, S. Champeil, P. (1991b). The two calcium ions initially bound to nonphosphorylated sarcoplasmic reticulum Ca2+-ATPase can no longer be kinetically distinguished when they dissociate from phosphorylated ATPase toward the lumen. Biochemistry 30,11331-11342. 

Suzuki, H., Obara, M., Kubo, K., Kanazawa, T. (1989). Changes in the steady-state fluorescence anisotropy of N-iodoacetyl-N -(5-sulfo-l-naphthyl)ethylenediamine attached to the specific thiol of sarcoplasmic reticulum Ca2+-ATPase throughout the catalytic cycle. J. Biol. Chem. 264, 920-927. 

Vilsen, B. Andersen, J.P. (1987). Characterization of CrATP-induced calcium occlusion in membrane-bound and soluble monomeric sarcoplasmic reticulum Ca2+-ATPase. Biochim. Biophys. Acta 898,313-322. 

Ohizumi, Y., Sasaki, S., Shibusawa, K., Ishikawa, K. and Ikemoto, F. (1996) Stimulation of sarcoplasmic reticulum Ca2+-ATPase by gingerol analogues. Biological and Pharmaceutical Bulletin 19(10), 1 3 77-1 3 79. 

Palm, T., Coan, C., and Trommer, W.E. (2001). Nucleotide-binding sites in the functional unit of sarcoplasmic reticulum Ca2+-ATPase as studied by photoaffinity spin-labeled 2-N3-SL-ATP, Biol. Chem. 382, 417-423... 

At low pH, one-electron oxidation predominates, yielding thiyl radicals R—S. At physiological values of pH, both pathways coexist however, two-electron oxidation predominates (G5, Ql, SI 2). The peroxynitrite inactivation of the sarcoplasmic reticulum Ca2+-ATPase (at a low concentration of ONOCT) mainly accounts for the thiol group oxidation, and can be reversed by thiol reducing agents (V8). 

V9. Viner, R. I., Krainev, A. G., Williams, T. D., Schoneich, C., and Bigelow, D. J., Identification of oxidation-sensitive peptides within die cytoplasmic domain of die sarcoplasmic reticulum Ca2+-ATPase. Biochemistry 36, 7706—7716 (1997). 

Active transport is often carried out at the expense of ATP hydrolysis. P-type ATPases pump ions against a concentration gradient and become transiently phosphorylated on an aspartic acid residue in the process of transport. P-type ATPases, which include the sarcoplasmic reticulum Ca2+ ATPase and the Na+-K+ ATPase, are integral membrane proteins with conserved structures and catalytic mechanisms. 

K. C. Chang, V. M. Figuercdo, J. H. M. Schreur, K. Kariya, M. W. Weiner, P. C. Simpson, S. A. Camacho, Thyroid hormone improves function and Ca2+ handling in pressure overload hypertrophy. Association with increased sarcoplasmic reticulum Ca2+-ATPase and alpha-myosin heavy chain in rat hearts, J Clin Invest 100, 1742-1749 (1997). 

Orlowski S, Champeil P. 1993. Strontium binding to sarcoplasmic reticulum Ca2+-ATPase ... 

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