Dystrophin constitutes 5% of membrane cytoskeleton in skeletal muscle
- PMID: 2044761
- DOI: 10.1016/0014-5793(91)80595-t
Dystrophin constitutes 5% of membrane cytoskeleton in skeletal muscle
Abstract
Dystrophin, which is absent in skeletal muscle of Duchenne muscular dystrophy patients, has not been considered to play a major structural role in the cell membrane of skeletal muscle because of its low abundance (approximately 0.002% of total muscle protein). Here, we have determined the relative abundance of dystrophin in a membrane cytoskeleton preparation and found that dystrophin constitutes approximately 5% of the total membrane cytoskeleton fraction of skeletal muscle sarcolemma. In addition, dystrophin can be removed from sarcolemma by alkaline treatment. Thus, our results have demonstrated that dystrophin is a major component of the subsarcolemmal cytoskeleton in skeletal muscle and suggest that dystrophin could play a major structural role in the cell membrane of skeletal muscle.
Similar articles
-
Dystrophin colocalizes with beta-spectrin in distinct subsarcolemmal domains in mammalian skeletal muscle.J Cell Biol. 1992 Jun;117(5):997-1005. doi: 10.1083/jcb.117.5.997. J Cell Biol. 1992. PMID: 1577872 Free PMC article.
-
Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy.Cell. 1995 Sep 8;82(5):743-52. doi: 10.1016/0092-8674(95)90471-9. Cell. 1995. PMID: 7545544
-
Association of dystrophin-related protein with dystrophin-associated proteins in mdx mouse muscle.Nature. 1992 Dec 10;360(6404):588-91. doi: 10.1038/360588a0. Nature. 1992. PMID: 1461282
-
Dystrophin-associated glycoproteins: their possible roles in the pathogenesis of Duchenne muscular dystrophy.Mol Cell Biol Hum Dis Ser. 1993;3:139-66. doi: 10.1007/978-94-011-1528-5_6. Mol Cell Biol Hum Dis Ser. 1993. PMID: 8111538 Review.
-
The dystrophin glycoprotein complex: signaling strength and integrity for the sarcolemma.Circ Res. 2004 Apr 30;94(8):1023-31. doi: 10.1161/01.RES.0000126574.61061.25. Circ Res. 2004. PMID: 15117830 Review.
Cited by
-
Mass spectrometric identification of dystrophin, the protein product of the Duchenne muscular dystrophy gene, in distinct muscle surface membranes.Int J Mol Med. 2017 Oct;40(4):1078-1088. doi: 10.3892/ijmm.2017.3082. Epub 2017 Jul 27. Int J Mol Med. 2017. PMID: 28765879 Free PMC article.
-
Proteomic Identification of Markers of Membrane Repair, Regeneration and Fibrosis in the Aged and Dystrophic Diaphragm.Life (Basel). 2022 Oct 22;12(11):1679. doi: 10.3390/life12111679. Life (Basel). 2022. PMID: 36362832 Free PMC article.
-
Understanding dystrophinopathies: an inventory of the structural and functional consequences of the absence of dystrophin in muscles of the mdx mouse.J Muscle Res Cell Motil. 1999 Oct;20(7):605-25. doi: 10.1023/a:1005545325254. J Muscle Res Cell Motil. 1999. PMID: 10672510 Review. No abstract available.
-
Dystrophin is phosphorylated by endogenous protein kinases.Biochem J. 1993 Jul 1;293 ( Pt 1)(Pt 1):243-7. doi: 10.1042/bj2930243. Biochem J. 1993. PMID: 8392335 Free PMC article.
-
The Dystrophin Node as Integrator of Cytoskeletal Organization, Lateral Force Transmission, Fiber Stability and Cellular Signaling in Skeletal Muscle.Proteomes. 2021 Feb 2;9(1):9. doi: 10.3390/proteomes9010009. Proteomes. 2021. PMID: 33540575 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources