WordNet

complicated in structure; consisting of interconnected parts; "a complex set of variations based on a simple folk melody"; "a complex mass of diverse laws and customs"
a compound described in terms of the central atom to which other atoms are bound or coordinated (同)coordination_compound
a conceptual whole made up of complicated and related parts; "the complex of shopping malls, houses, and roads created a new town" (同)composite
(psychoanalysis) a combination of emotions and impulses that have been rejected from awareness but still influence a persons behavior

PrepTutorEJDIC

『いくつかの部分から成る』,複合の,合成の / 『複雑な』,入りくんだ,こみいった(complicated) / 複合体,合成物 / コンプレックス,複合(抑圧されて心に残った複雑なしこり)

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/01/12 03:28:34」(JST)

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Costamere structure in mouse quadriceps.

The costamere is a structural-functional component of striated muscle cells^[1] which connects the sarcomere of the muscle to the cell membrane.^[2]

Costameres are sub-sarcolemmal protein assemblies circumferentially aligned in register with the Z-disk of peripheral myofibrils. 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.^[3]

The dystrophin-associated glycoprotein (DAG) complex 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.^[4] Desmin protein may also bind to the DAG complex, and regions of it are known to be involved in signaling.

References

^ Costameres at the US National Library of Medicine Medical Subject Headings (MeSH)
^ 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
^ 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. PMID 21312057.

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English Journal

Neuronal Dystroglycan Is Necessary for Formation and Maintenance of Functional CCK-Positive Basket Cell Terminals on Pyramidal Cells.

Früh S1, Romanos J1, Panzanelli P2, Bürgisser D3, Tyagarajan SK1, Campbell KP4, Santello M1, Fritschy JM5.
The Journal of neuroscience : the official journal of the Society for Neuroscience.J Neurosci.2016 Oct 5;36(40):10296-10313.
Distinct types of GABAergic interneurons target different subcellular domains of pyramidal cells, thereby shaping pyramidal cell activity patterns. Whether the presynaptic heterogeneity of GABAergic innervation is mirrored by specific postsynaptic factors is largely unexplored. Here we show that dys
PMID 27707967

Mechanistic aspects of the formation of α-dystroglycan and therapeutic research for the treatment of α-dystroglycanopathy: A review.

Taniguchi-Ikeda M1, Morioka I2, Iijima K2, Toda T3.
Molecular aspects of medicine.Mol Aspects Med.2016 Oct;51:115-24. doi: 10.1016/j.mam.2016.07.003. Epub 2016 Jul 12.
α-Dystroglycanopathy, an autosomal recessive disease, is associated with the development of a variety of diseases, including muscular dystrophy. In humans, α-dystroglycanopathy includes various types of congenital muscular dystrophy such as Fukuyama type congenital muscular dystrophy (FCMD), muscl
PMID 27421908

The role of LAMP1 binding and pH sensing by the spike complex of Lassa virus.

Cohen-Dvashi H1, Israeli H1, Shani O1, Katz A1, Diskin R2.
Journal of virology.J Virol.2016 Sep 7. pii: JVI.01624-16. [Epub ahead of print]
To effectively infect cells, Lassa virus needs to switch in endosomal compartment from its primary receptor α-dystroglycan to a protein termed LAMP1. A unique histidine triad on the surface of the receptor-binding domain from the glycoprotein spike complex of Lassa virus is important for LAMP1 bind
PMID 27605678