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JBC, Vol. 254, Issue 2, 530-539, Jan, 1979
L. R. Jones, H. R. Besch Jr, J. W. Fleming, M. M. McConnaughey and A. M. Watanabe
Sarcolemmal and sarcoplasmic reticulum membrane vesicle fractions were
isolated from cardiac microsomes. Separation of sarcolemmal and
sarcoplasmic reticulum membrane markers was documented by a combination of
correlative assay and centrifugation techniques. To facilitate the
separation, the crude microsomes were incubated in the presence of ATP,
Ca2+, and oxalate to increase the density of the sarcoplasmic reticulum
vesicles. After sucrose gradient centrifugation, the densest subfraction
(sarcoplasmic reticulum) contained the highest (K+,Ca2+)-ATPase activity
and virtually no (Na2+,K+)-ATPase activity, even when latent
(Na+,K+)-ATPase activity was unmasked. In addition, the sarcoplasmic
reticulum fraction contained no significant sialic acid, beta receptor
binding activity, or adenylate cyclase activity. Sarcolemmal membrane
fractions were of low buoyant density. Preparations most enriched in
sarcolemmal vesicles contained the highest level of all the other
parameters and only about 10% of the (K+,Ca2+)-ATPase activity of the
sarcoplasmic reticulum fraction. The results suggest that (Na+,K+)-ATPase,
sialic acid, beta-adrenergic receptors, and adenylate cyclase can be
entirely accounted for by the sarcolemmal content of cardiac microsomes.
Gel electrophoresis of the sarcolemmal and sarcoplasmic reticulum membrane
fractions showed distinct bands. Membrane proteins exclusive to each of the
fractions were also demonstrated by phosphorylation. Cyclic AMP stimulated
phosphorylation by [gamma-32P]ATP of two proteins of apparent Mr = 20,000
and 7,000 that were concentrated in sarcoplasmic reticulum, but the
stimulation was markedly dependent on the presence of added soluble cyclic
AMP-dependent protein kinase. Cyclic AMP also stimulated phosphorylation of
membrane proteins in sarcolemma, but this phosphorylation was mediated by
an endogenous protein kinase activity. The apparent molecular weights of
these phosphorylated proteins were 165,000, 90,000, 56,000, 24,000, and
11,000. The results suggest that sarcolemma may contain an integral enzyme
complex, not present in sarcoplasmic reticulum, that contains
beta-adrenergic receptors, adenylate cyclase, cyclic AMP-dependent protein
kinase, and several substrates of the protein kinase.
Separation of vesicles of cardiac sarcolemma from vesicles of cardiac sarcoplasmic reticulum. Comparative biochemical analysis of component activities
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