Journal article
ε-Sarcoglycan Replaces α-Sarcoglycan in Smooth Muscle to Form a Unique Dystrophin-Glycoprotein Complex
The Journal of biological chemistry, Vol.274(39), pp.27989-27996
09/24/1999
DOI: 10.1074/jbc.274.39.27989
PMID: 10488149
Abstract
The sarcoglycan complex has been well characterized in striated muscle, and defects in its components are associated with muscular dystrophy and cardiomyopathy. Here, we have characterized the smooth muscle sarcoglycan complex. By examination of embryonic muscle lineages and biochemical fractionation studies, we demonstrated that ε-sarcoglycan is an integral component of the smooth muscle sarcoglycan complex along with β- and δ-sarcoglycan. Analysis of genetically defined animal models for muscular dystrophy supported this conclusion. The δ-sarcoglycan-deficient cardiomyopathic hamster and mice deficient in both dystrophin and utrophin showed loss of the smooth muscle sarcoglycan complex, whereas the complex was unaffected in α-sarcoglycan null mice in agreement with the finding that α-sarcoglycan is not expressed in smooth muscle cells. In the cardiomyopathic hamster, the smooth muscle sarcoglycan complex, containing ε-sarcoglycan, was fully restored following intramuscular injection of recombinant δ-sarcoglycan adenovirus. Together, these results demonstrate a tissue-dependent variation in the sarcoglycan complex and show that ε-sarcoglycan replaces α-sarcoglycan as an integral component of the smooth muscle dystrophin-glycoprotein complex. Our results also suggest a molecular basis for possible differential smooth muscle dysfunction in sarcoglycan-deficient patients.
Details
- Title: Subtitle
- ε-Sarcoglycan Replaces α-Sarcoglycan in Smooth Muscle to Form a Unique Dystrophin-Glycoprotein Complex
- Creators
- Volker Straub - Howard Hughes Medical Institute, Department of Physiology and Biophysics, Department of Neurology, University of Iowa College of Medicine, Iowa City, Iowa 52242Audrey J Ettinger - Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, Missouri 63110Madeleine Durbeej - Howard Hughes Medical Institute, Department of Physiology and Biophysics, Department of Neurology, University of Iowa College of Medicine, Iowa City, Iowa 52242David P Venzke - Howard Hughes Medical Institute, Department of Physiology and Biophysics, Department of Neurology, University of Iowa College of Medicine, Iowa City, Iowa 52242Susan Cutshall - Howard Hughes Medical Institute, Department of Physiology and Biophysics, Department of Neurology, University of Iowa College of Medicine, Iowa City, Iowa 52242Joshua R Sanes - Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, Missouri 63110Kevin P Campbell - Howard Hughes Medical Institute, Department of Physiology and Biophysics, Department of Neurology, University of Iowa College of Medicine, Iowa City, Iowa 52242
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.274(39), pp.27989-27996
- DOI
- 10.1074/jbc.274.39.27989
- PMID
- 10488149
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Publisher
- Elsevier Inc
- Grant note
- Muscular Dystrophy Association Str 498/1-1 / Deutsche Forschungsgemeinschaft Swedish Foundation for International Cooperation in Research and Higher Education (STINT) National Institutes of Health
- Language
- English
- Date published
- 09/24/1999
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute
- Record Identifier
- 9984068278802771
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