syntrophin

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/02/12 11:05:16」(JST)

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The syntrophins are a family of five 60-kiloDalton proteins that are associated with dystrophin, the protein associated with Duchenne muscular dystrophy and Becker muscular dystrophy. The name comes from the Greek word syntrophos, meaning "companion." The five syntrophins are encoded by separate genes and are termed α, β₁, β₂, γ₁, and γ₂. Syntrophin was first identified as a dystrophin-associated protein present in the Torpedo electric organ (originally called "58K protein"). Subsequently, α-syntrophin was shown to be the predominant isoform in skeletal muscle where it is localized on the sarcolemma and enriched at the neuromuscular junction. The β-syntrophins and γ₂-syntrophin are also present in skeletal muscle but also are in most other tissues. The expression of γ₁-syntrophin is mostly confined to brain. The syntrophins are adapter proteins that use their multiple protein interaction domains (two pleckstrin homology domains and a PDZ domain) to localize a variety of signaling proteins (kinases, ion channels, water channels, nitric oxide synthase) to specific intracellular locations. α-Syntrophin binds to nNOS in the dystrophin-associated glycoprotein complex in skeletal muscle cells. There it produces NO upon muscle contraction leading to dilation of the arteries in the local area.^[1]

References

^ http://jcs.biologists.org/content/117/13/2627.full.pdf

External links

syntrophin at the US National Library of Medicine Medical Subject Headings (MeSH)

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English Journal

Lipid abnormalities in alpha/beta2-syntrophin null mice are independent from ABCA1.

Hebel T1, Eisinger K1, Neumeier M1, Rein-Fischboeck L1, Pohl R1, Meier EM1, Boettcher A2, Froehner SC3, Adams ME3, Liebisch G2, Krautbauer S1, Buechler C4.
Biochimica et biophysica acta.Biochim Biophys Acta.2015 May;1851(5):527-36. doi: 10.1016/j.bbalip.2015.01.012. Epub 2015 Jan 24.
The syntrophins alpha (SNTA) and beta 2 (SNTB2) are molecular adaptor proteins shown to stabilize ABCA1, an essential regulator of HDL cholesterol. Furthermore, SNTB2 is involved in glucose stimulated insulin release. Hyperglycemia and dyslipidemia are characteristic features of the metabolic syndro
PMID 25625330

Protein Assemblies of Sodium and Inward Rectifier Potassium Channels Control Cardiac Excitability and Arrhythmogenesis.

Willis BC1, Ponce-Balbuena D1, Jalife J2.
American journal of physiology. Heart and circulatory physiology.Am J Physiol Heart Circ Physiol.2015 Apr 10:ajpheart.00176.2015. doi: 10.1152/ajpheart.00176.2015. [Epub ahead of print]
The understanding of how cardiac ion channels function in the normal and the diseased heart has greatly increased over the last four decades thanks to the advent of patch-clamp technology and, more recently, the emergence of genetics as well as cellular and molecular cardiology. However, our knowled
PMID 25862830

Correction: altered astrocytic swelling in the cortex of α-syntrophin-negative GFAP/EGFP mice.

PLOS ONE Staff.
PloS one.PLoS One.2015 Mar 16;10(3):e0119744. doi: 10.1371/journal.pone.0119744. eCollection 2015.
PMID 25775461

Japanese Journal

Functional Abnormality of Sodium Channel Interacting Proteins in Arrhythmogenesis

C. Makielski Jonathan
Journal of Arrhythmia 27(Supplement), SS3_1, 2011
… encoding syntrophin α1 as a cause of LQTS (LQT12). …
NAID 130002130110

Immunocytochemical Studies of Aquaporin 4, Kir4.1, and .ALPHA.1-syntrophin in the Astrocyte Endfeet of Mouse Brain Capillaries

Masaki Hisatsugu,Wakayama Yoshihiro,Hara Hajime,Jimi Takahiro,Unaki Akihiko,Iijima Shoji,Oniki Hiroaki,Nakano Kiyoko,Kishimoto Koji,Hirayama Yoshiko
ACTA HISTOCHEMICA ET CYTOCHEMICA 43(4), 99-105, 2010
… We examined the ultrastructural localization of Kir4.1, AQP4, α1-syntrophin, and β-spectrin molecules to understand the functional role(s) of Kir4.1 and AQP4. … Double immunogold electron microscopy showed frequent co-localization in the combination of molecules of Kir4.1 and AQP4, Kir4.1 and α1-syntrophin, and AQP4 and α1-syntrophin, but not those of AQP4 and β-spectrin. …
NAID 130000300030

SKELETAL MUSCLE SYNTROPHIN INTERACTORS REVEALED BY YEAST TWO-HYBRID ASSAY

Inoue Masahiko,Wakayama Yoshihiro,Jimi Takahiro,Shibuya Seiji,Hara Hajime,Unaki Akihiko,Kenmochi Kiyokazu
Nagoya Journal of Medical Science 70(3/4), 117-126, 2008-08
NAID 110007020072

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[1] ttp://jcs.biologists.org/content/117/13/2627.full.pdf

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