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Differentiation of sarcoplasmic reticulum during cardiac myogenesis

Journal Article · · Am. J. Physiol.; (United States)
OSTI ID:6351950

The composition and function of fetal and mature sheep cardiac sarcoplasmic reticulum membranes were investigated. Phospholamban, a major phosphoprotein in the mature sarcoplasmic reticulum membranes, was present in early stages of cardiac myogenesis. This fetal form of phospholamban was phosphorylated by cAMP-dependent protein kinase but not in the presence of Ca/sup 2 +/ and calmodulin. /sup 35/Ca/sup 2 +/ uptake and Ca/sup 2 +/-dependent ATPase activity were low in fetal sarcoplasmic reticulum compared with the adult controls, although the apparent affinities for Ca/sup 2 +/ were similar. Sarcoplasmic reticulum vesicles isolated at all developmental stages had very low levels of plasma membrane and mitochondrial contamination. Sarcoplasmic reticulum /sup 45/Ca/sup 2 +/ uptake and Ca/sup 2 +/-dependent. ATPase activities were not affected by micromolar concentrations of vanadate, and the accumulated /sup 45/Ca/sup 2 +/ could not be released by the addition of NaCl. The amount of both the 110- and 55-kDa protein bands, identified with pecific antibodies as Ca/sup 2 +/-ATPase and calsequestrin, respectively, was low in early stages of cardiac myogenesis. Age-related differences in the Ca/sup 2 +/ transport properties of cardiac sarcoplasmic reticulum and in the amount of the Ca/sup 2 +/-ATPase and calsequestrin may explain alterations in the regulation of intracellular Ca/sup 2 +/ concentrations in the fetal heart. This may contribute to the developmental changes in myocardial function.

Research Organization:
Univ. of Toronto, Ontario
OSTI ID:
6351950
Journal Information:
Am. J. Physiol.; (United States), Journal Name: Am. J. Physiol.; (United States) Vol. 252:1; ISSN AJPHA
Country of Publication:
United States
Language:
English

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