| Costamere | |
|---|---|
 Costamere structure in mouse quadriceps | |
| Details | |
| Part of | Striated muscle |
| Identifiers | |
| Latin | costamerum |
| MeSH | D054974 |
| TH | H2.00.05.2.01013 |
| Anatomical terminology | |
The costamere is a structural-functional component of striated muscle cells[1] which connects the sarcomere of the muscle to the cell membrane (i.e. the sarcolemma).[2]
Costameres are sub-sarcolemmal protein assemblies circumferentially aligned in register with the Z-disk of peripheral myofibrils.[3][4][5] They physically couple force-generating sarcomeres with the sarcolemma in striated muscle cells and are thus considered one of several "Achilles' heels" of skeletal muscle, a critical component of striated muscle morphology which, when compromised, is thought to directly contribute to the development of several distinct myopathies.[6]
The dystrophin-associated protein complex, also referred to as the dystrophin-associated glycoprotein complex (DGC or DAGC),[2] contains various integral and peripheral membrane proteins such as dystroglycans and sarcoglycans, which are thought to be responsible for linking the internal cytoskeletal system of individual myofibers to structural proteins within the extracellular matrix (such as collagen and laminin). Therefore, it is one of the features of the sarcolemma which helps to couple the sarcomere to the extracellular connective tissue as some experiments have shown.[7] Desmin protein may also bind to the DAG complex, and regions of it are known to be involved in signaling.
- ^ Costameres at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- ^ a b Srivastava, D.; Yu, S (2006). "Stretching to meet needs: integrin-linked kinase and the cardiac pump". Genes Dev. 20 (17): 2327–2331. doi:10.1101/gad.1472506. PMID 16951248.20: 2327-2331
- ^ Pardo, Jose V; Siliciano, Janet D'Angelo; Craig, Susan W (February 1983). "A vinculin-containing cortical lattice in skeletal muscle: Transverse lattice elements ("costameres") mark sites of attachment between myofibrils and sarcolemma" (PDF). Proceedings of the National Academy of Sciences. 80 (4): 1008–1012. Bibcode:1983PNAS...80.1008P. doi:10.1073/pnas.80.4.1008. PMC 393517. PMID 6405378.
- ^ Pardo, Jose V; Siliciano, Janet D'Angelo; Craig, Susan W (1 October 1983). "Vinculin is a component of an extensive network of myofibril-sarcolemma attachment regions in cardiac muscle fibers". Journal of Cell Biology. 97 (4): 1081–1088. doi:10.1083/jcb.97.4.1081. PMC 2112590. PMID 6413511.
- ^ Craig, Susan W; Pardo, Jose V (1983). "Gamma actin, spectrin, and intermediate filament proteins colocalize with vinculin at costameres, myofibril-to-sarcolemma attachment sites". Cell Motility. 3 (5): 449–462. doi:10.1002/cm.970030513. PMID 6420066.
- ^ James M. Ervasti (2003). "Costameres: the Achilles' Heel of Herculean Muscle". J. Biol. Chem. 278 (13591–13594): 13591–4. doi:10.1074/jbc.R200021200. PMID 12556452.
- ^ García-Pelagio Karla; Bloch Robert; Ortega A; Gonzáles-Serratos Hugo (2011). "Biomechanics of the sarcolemma and costameres in single skeletal muscle fibers from normal and dystrophin- null mice". J Muscle Res Cell Motil. 31 (5–6): 323–336. doi:10.1007/s10974-011-9238-9. PMC 4326082. PMID 21312057.