Journal article
Characterization of δ-Sarcoglycan, a Novel Component of the Oligomeric Sarcoglycan Complex Involved in Limb-Girdle Muscular Dystrophy
The Journal of biological chemistry, Vol.271(50), pp.32321-32329
12/13/1996
DOI: 10.1074/jbc.271.50.32321
PMID: 8943294
Abstract
The sarcoglycan complex is known to be involved in limb-girdle muscular dystrophy (LGMD) and is composed of at least three proteins: α-, β-, and γ-sarcoglycan. δ-Sarcoglycan has now been identified as a second 35-kDa sarcolemmal transmembrane glycoprotein that shares high homology with γ-sarcoglycan and is expressed mainly in skeletal and cardiac muscle. Biochemical analysis has demonstrated that γ- and δ-sarcoglycan are separate entities within the sarcoglycan complex and that all four sarcoglycans exist in the complex on a stoichiometrically equal basis. Immunohistochemical analysis of skeletal muscle biopsies from patients with LGMD2C, LGMD2D, and LGMD2E demonstrated a reduction of the entire sarcoglycan complex in these muscular dystrophies. Furthermore, we have mapped the human δ-sarcoglycan gene to chromosome 5q33-q34 in a region overlapping the recently linked autosomal recessive LGMD2F locus.
Details
- Title: Subtitle
- Characterization of δ-Sarcoglycan, a Novel Component of the Oligomeric Sarcoglycan Complex Involved in Limb-Girdle Muscular Dystrophy
- Creators
- Daniel Jung - Howard Hughes Medical Institute and Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242Franck Duclos - Howard Hughes Medical Institute and Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242Barbara Apostol - Department of Biological Chemistry, University of California, Irvine, Irvine, California 92717Volker Straub - Howard Hughes Medical Institute and Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242Jane C Lee - Howard Hughes Medical Institute and Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242Valérie Allamand - Howard Hughes Medical Institute and Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242David P Venzke - Howard Hughes Medical Institute and Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242Yoshihide Sunada - Howard Hughes Medical Institute and Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242Carolyn R Moomaw - Howard Hughes Medical Institute, Biopolymer Facility, University of Texas Southwestern Medical Center, Dallas, Texas 75235Cynthia J Leveille - Howard Hughes Medical Institute and Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242Clive A Slaughter - Howard Hughes Medical Institute, Biopolymer Facility, University of Texas Southwestern Medical Center, Dallas, Texas 75235Thomas O Crawford - Department of Neurology, The Johns Hopkins University, Baltimore, Maryland 21287-8811John D McPherson - Department of Genetics/Genome Sequencing Center, Washington University School of Medicine, St. Louis, Missouri 63108Kevin P Campbell - Howard Hughes Medical Institute and Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.271(50), pp.32321-32329
- DOI
- 10.1074/jbc.271.50.32321
- PMID
- 8943294
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Publisher
- Elsevier Inc
- Language
- English
- Date published
- 12/13/1996
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute; Obstetrics and Gynecology
- Record Identifier
- 9984068265802771
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