Ca 2+ ATPase Phospholamban, Sarcolipin Brody Disease Cardiomyopathy Ca2+ Release Channel MH/CCD Ca2+ Binding Proteins Publications						Calcium Binding Proteins The lumen of the sarcoplasmic reticulum contains a series of soluble, acidic proteins of undefined function. Calsequestrin, the most prominent of these, is a high capacity, low affinity calcium binding protein. It forms a matrix attached to the lumenal surface of the junctional terminal cisternae through a nucleation point provided by triadin, a basic, transmembrane protein that interacts with both calsequestrin and the calcium release channel.  All of the evidence points to the calsequestrin matrix as a site of calcium storage which concentrates calcium at the site from which it is released. Calreticulin is also a high capacity calcium binding protein which contains a single high affinity calcium binding site. Although it has been implicated in many cellular functions, it is most likely that it has chaperone activity. Sarcalumenin is an acidic, lumenal glycoprotein which is alternatively spliced from the same gene that encodes a 53,000 Da lumenal glycoproprotein. These glycoproteins are localized in the longitudinal sarcoplasmic reticulum where they may play an interactive role with the calcium pump. We have cloned DNAs encoding each of these proteins and have an abiding interest in understanding their roles in sarcoplasmic reticulum function.
Ca 2+ ATPase Phospholamban, Sarcolipin Brody Disease Cardiomyopathy Ca2+ Release Channel MH/CCD Ca2+ Binding Proteins Top of Page						Calcium Binding Protein Publications Fujii, J., Willard, H.F. and MacLennan, D.H. (1990) Characterization and localization to human chromosome 1 of human fast-twitch skeletal muscle calsequestrin gene. Somatic Cell & Molecular Genetics 16(2):185-9 Leberer, E., Timms, B.G., Campbell, K.P. and MacLennan, D.H. (1990) Purification, calcium binding properties, and ultrastructural localization of the 53,000- and 160,000 (sarcalumenin)-dalton glycoproteins of the sarcoplasmic reticulum. Journal of Biological Chemistry 265(17):10118-24 Fliegel, L., Burns, K., MacLennan, D.H., Reithmeier, R.A. and Michalak, M. (1989) Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum. Journal of Biological Chemistry 264(36):21522-8 Leberer, E., Charuk, J.H., Green, N.M. and MacLennan, D.H. (1989) Molecular cloning and expression of cDNA encoding a lumenal calcium binding glycoprotein from sarcoplasmic reticulum. Proceedings of the National Academy of Sciences of the United States of America 86(16):6047-51 Leberer, E., Charuk, J.H., Clarke, D.M., Green, N.M., Zubrzycka-Gaarn, E. and MacLennan, D.H. (1989) Molecular cloning and expression of cDNA encoding the 53,000-dalton glycoprotein of rabbit skeletal muscle sarcoplasmic reticulum. Journal of Biological Chemistry 264(6):3484-93 Fliegel, L., Leberer, E., Green, N.M. and MacLennan, D.H. (1989) The fast-twitch muscle calsequestrin isoform predominates in rabbit slow-twitch soleus muscle. FEBS Letters 242(2):297-300 Tuana, B.S. and MacLennan, D.H. (1988) Isolation of the calmodulin-dependent protein kinase system from rabbit skeletal muscle sarcoplasmic reticulum. FEBS Letters 235(1-2):219-23 Zarain-Herzberg, A., Fliegel, L. and MacLennan, D.H. (1988) Structure of the rabbit fast-twitch skeletal muscle calsequestrin gene. Journal of Biological Chemistry 263(10):4807-12 Reithmeier, R.A.F., Ohnishi, M., Carpenter, M.R., Slupsky, J.R., Gounden, K., Fliegel, L., Khanna, V.K. and MacLennan, D.H. (1987) Calsequestrin, in Calcium Binding Proteins in Health and Disease (Norman, A.W., Vanaman, T.C. and Means, A.R.) Academic Press New York Fliegel, L., Ohnishi, M., Carpenter, M.R., Khanna, V.K., Reithmeier, R.A. and MacLennan, D.H. (1987) Amino acid sequence of rabbit fast-twitch skeletal muscle calsequestrin deduced from cDNA and peptide sequencing. Proceedings of the National Academy of Sciences of the United States of America 84(5):1167-71 Campbell, K.P., MacLennan, D.H., Jorgensen, A.O. and Mintzer, M.C. (1983) Purification and characterization of calsequestrin from canine cardiac sarcoplasmic reticulum and identification of the 53,000 dalton glycoprotein. Journal of Biological Chemistry 258(2):1197-204 Campbell, K.P. and MacLennan, D.H. (1982) A calmodulin-dependent protein kinase system from skeletal muscle sarcoplasmic reticulum. Phosphorylation of a 60,000-dalton protein. Journal of Biological Chemistry 257(3):1238-46 Campbell, K.P. and MacLennan, D.H. (1981) Purification and characterization of the 53,000-dalton glycoprotein from the sarcoplasmic reticulum. Journal of Biological Chemistry 256(9):4626-32 Michalak, M., Campbell, K.P. and MacLennan, D.H. (1980) Localization of the high affinity calcium binding protein and an intrinsic glycoprotein in sarcoplasmic reticulum membranes. Journal of Biological Chemistry 255(4):1317-26 Ostwald, T.J., MacLennan, D.H. and Dorrington, K.J. (1974) Effects of cation binding on the conformation of calsequestrin and the high affinity calcium-binding protein of sarcoplasmic reticulum. Journal of Biological Chemistry 249(18):5867-71 Ostwald, T.J. and MacLennan, D.H. (1974) Isolation of a high affinity calcium-binding protein from sarcoplasmic reticulum. Journal of Biological Chemistry 249(3):974-9 MacLennan, D.H. (1974) The Ayerst Award Lecture: Resolution of the calcium transport system of sarcoplasmic reticulum. Can. J. Biochem. 53251-61 MacLennan, D.H., Yip, C.C., Iles, G.H. and Seeman, P. (1972) Isolation of sarcoplasmic reticulum proteins. Cold Spring Harbor Symp. Quant. Biol. 37469-78 MacLennan, D.H. and Wong, P.T. (1971) Isolation of a calcium-sequestering protein from sarcoplasmic reticulum. Proceedings of the National Academy of Sciences of the United States of America 68(6):1231-5
Ca2+ Binding Proteins Top of Page Publications Revised 1998Apr09