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Association of sorcin with the cardiac ryanodine receptor.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 1995 Nov 03; Vol. 270 (44), pp. 26411-8. - Publication Year :
- 1995
-
Abstract
- 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.
- Subjects :
- Animals
Caffeine pharmacology
Calcium metabolism
Calcium Channels analysis
Calcium Channels isolation & purification
Calcium-Binding Proteins analysis
Calcium-Binding Proteins isolation & purification
Calmodulin-Binding Proteins metabolism
Cell Line
Cells, Cultured
Cricetinae
Cricetulus
Immunohistochemistry
Kinetics
Lung
Male
Methionine metabolism
Mice
Mice, Inbred BALB C
Microscopy, Immunoelectron
Muscle Proteins analysis
Muscle Proteins isolation & purification
Phosphoproteins metabolism
Protein Binding
Rats
Rats, Sprague-Dawley
Recombinant Proteins analysis
Recombinant Proteins isolation & purification
Recombinant Proteins metabolism
Ryanodine Receptor Calcium Release Channel
Sarcoplasmic Reticulum ultrastructure
Transfection
Calcium Channels metabolism
Calcium-Binding Proteins metabolism
Muscle Proteins metabolism
Myocardium cytology
Myocardium metabolism
Sarcoplasmic Reticulum metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 270
- Issue :
- 44
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 7592856
- Full Text :
- https://doi.org/10.1074/jbc.270.44.26411