WordNet

an extensible membrane enclosing the contractile substance of a muscle fiber
of or relating to sarcolemma (同)sarcolemnous
of or relating to the sarcolemma

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/02/25 20:02:12」(JST)

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The sarcolemma is the cell membrane of a muscle cell (skeletal, cardiac, and smooth muscle).^[1] It consists of a true cell membrane, called the plasma membrane, and an outer coat made up of a thin layer of polysaccharide material that contains numerous thin collagen fibrils. At each end of the muscle fiber, this surface layer of the sarcolemma fuses with a tendon fiber, and the tendon fibers in turn collect into bundles to form the muscle tendons that then insert into bones. The membrane is configured to receive and conduct stimuli.

Alterations in the sarcolemma membrane stability and repair system can lead to muscular dystrophy. The mechanism of one type of muscular dystrophy, for example, is lack of functional dystrophin. This means that the sarcolemma is not attached to the cytoskeleton. Therefore during muscle contraction, the sarcolemma is not synchronized with the interior of the cell. The looseness of the sarcolemma permits membrane calcium channels to open. The rise in internal calcium ions causes activation of the proteolytic enzyme calpain, which digests proteins including contractile proteins, rendering the muscle much weaker.

The sarcolemma invaginates into the cytoplasm of the muscle cell, forming membranous tubules called transverse tubules (T-tubules). Terminal cisternae is the enlargement of smooth endoplasmic reticulum found in muscle cells on either side of the transverse tubules. The triad of transverse tubules surrounded by two smooth ER cisternae transmit altered membrane permeability down the tubules. The nuclei lie just adjacent to the sarcolemma, at the periphery of the fiber.

This membrane is extensible and encloses the contractile substance of a muscle fiber.

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References

^ MeSH Sarcolemma

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English Journal

β1D chain increases α7β1 integrin and laminin and protects against sarcolemmal damage in mdx mice.

Liu J, Milner DJ, Boppart MD, Ross RS, Kaufman SJ.SourcePresent address: Department of Cell and Tissue Biology, University of California at San Francisco, School of Dentistry, San Francisco, CA, USA.
Human molecular genetics.Hum Mol Genet.2012 Apr 1;21(7):1592-603. Epub 2011 Dec 16.
The dystrophin-glycoprotein complex connects myofibers with extracellular matrix laminin. In Duchenne muscular dystrophy, this linkage system is absent and the integrity of muscle fibers is compromised. One potential therapy for addressing muscular dystrophy is to augment the amount of α7β1 integr
PMID 22180459

In Vivo imaging of molecular interactions at damaged sarcolemma.

Roostalu U, Strähle U.SourceInstitute of Toxicology and Genetics, Karlsruhe Institute of Technology and University of Heidelberg, Hermann-von-Helmholtz-Platz 1, 76344 Eggenstein-Leopoldshafen, Germany.
Developmental cell.Dev Cell.2012 Mar 13;22(3):515-29.
Muscle cells have a remarkable capability to repair plasma membrane lesions. Mutations in dysferlin (dysf) are known to elicit a progressive myopathy in humans, probably due to impaired sarcolemmal repair. We show here that loss of Dysf and annexin A6 (Anxa6) function lead to myopathy in zebrafish.
PMID 22421042

Japanese Journal

Satellite cell heterogeneity and hierarchy in skeletal muscle

Ono Yusuke
The Journal of Physical Fitness and Sports Medicine 3(2), 229-234, 2014
… Satellite cells are skeletal muscle tissue stem cells located between the basal lamina and sarcolemma of myofibres and play crucial roles in adult muscle repair and regeneration as well as postnatal muscle growth. …
NAID 130004626101

Becker Muscular Dystrophy-Like Myopathy Regarded as So-Called "Fatty Muscular Dystrophy" in a Pig: A Case Report and Its Diagnostic Method

HORIUCHI Noriyuki,AIHARA Naoyuki,MIZUTANI Hiroshi,KOUSAKA Shinichi,NAGAFUCHI Tsuneyuki,OCHIAI Mariko,OCHIAI Kazuhiko,KOBAYASHI Yoshiyasu,FURUOKA Hidefumi,ASAI Tetsuo,OISHI Koji
Journal of Veterinary Medical Science 76(2), 243-248, 2014
… We describe a case of human Becker muscular dystrophy (BMD)-like myopathy that was characterized by the declined stainability of dystrophin at sarcolemma in a pig and the immunostaining for dystrophin on the formalin-fixed, paraffin-embedded (FFPE) tissue. … The immunostaining for dystrophin was conducted and confirmed to be applicable on FFPE porcine muscular tissues and revealed diminished stainability of dystrophin at the sarcolemma in the present case. …
NAID 130003382368

Subcellular Localization of Dystrophin Isoforms in Cardiomyocytes and Phenotypic Analysis of Dystrophin-deficient Mice Reveal Cardiac Myopathy is Predominantly Caused by a Deficiency in Full-length Dystrophin

MASUBUCHI Nami,SHIDOH Yuichi,KONDO Shunzo [他],Takatoh Jun,Hanaoka Kazunori
Experimental Animals 62(3), 211-217, 2013
… By immunohistochemical staining and density-gradient centrifugation, we found that Dp427 was located in the cardiac sarcolemma and also at the T-tubules, whereas Dp71 was specifically located at the T-tubules. …
NAID 130003362959