title: Specific protein-protein interactions of calsequestrin with junctional sarcoplasmic reticulum of skeletal muscle.
abstract: Minor protein components of triads and of sarcoplasmic reticulum (SR) terminal cisternae (TC), i.e. 47 and 37 kDa peptides and 31-30 kDa and 26-25 kDa peptide doublets, were identified from their ability to bind 125I calsequestrin (CS) in the presence of EGTA. The CS-binding peptides are specifically associated with the junctional membrane of TC, since they could not be detected in junctional transverse tubules and in longitudinal SR fragments. The 31-30 kDa peptide doublet, exclusively, did not bind CS in the presence of Ca2+. Thus, different types of protein-protein interactions appear to be involved in selective binding of CS to junctional TC.
authors.affiliation: Centro di Studio per la Biologia e la Fisiopatologia Muscolare, Universita' di Padova, Italy.
authors.forename: E
authors.initials: E
authors.lastname: Damiani
authors.forename: A
authors.initials: A
authors.lastname: Margreth
mesh_terms: D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002155:Calsequestrin / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D002645:Chickens; D004492:Edetic Acid / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007457:Iodine Radioisotopes; D008297:Male; D009132:Muscles / Q000378:metabolism*; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000378:metabolism*; D013045:Species Specificity; D013552:Swine
chemical_list: D002155:Calsequestrin; D007457:Iodine Radioisotopes; D004492:Edetic Acid; D002118:Calcium