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(Received for publication, May 17, 1995; and in revised form, August 30, 1995) Sorcin is a 22-kDa calcium-binding protein initially identified
in multidrug-resistant cells; however, its patterns of expression and
function in normal tissues are unknown. Here we demonstrate that sorcin
is widely distributed in rodent tissues, including the heart, where it
was localized by immunoelectron microscopy to the sarcoplasmic
reticulum. A >500-kDa protein band immunoprecipitated from cardiac
myocytes by sorcin antiserum was indistinguishable in size on gels from
the 565-kDa ryanodine receptor/calcium release channel recognized by
ryanodine receptor-specific antibody. Association of sorcin with a
ryanodine receptor complex was confirmed by complementary
co-immunoprecipitations of sorcin with the receptor antibody. Forced
expression of sorcin in ryanodine receptor-negative Chinese hamster
lung fibroblasts resulted in accumulation of the predicted 22-kDa
protein as well as the unexpected appearance of ryanodine receptor
protein. In contrast to the parental host fibroblasts, sorcin
transfectants displayed a rapid and transient rise in intracellular
calcium in response to caffeine, suggesting organization of the
accumulated ryanodine receptor protein into functional calcium release
channels. These data demonstrate an interaction between sorcin and the
ryanodine receptor and suggest a role for sorcin in modulation of
calcium release channel activity, perhaps by stabilizing the channel
protein.
Volume 270,
Number 44,
Issue of November 3, 1995 pp. 26411-26418
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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