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Dystrophin as a focal adhesion protein. Collocalization with talin and the Mr 48,000 sarcolemmal protein in cultured Xenopus muscle.

作者信息

Kramarcy N R, Sealock R

机构信息

Department of Physiology, University of North Carolina, Chapel Hill 27599.

出版信息

FEBS Lett. 1990 Nov 12;274(1-2):171-4. doi: 10.1016/0014-5793(90)81356-s.

DOI:10.1016/0014-5793(90)81356-s
PMID:2123804
Abstract

Monoclonal antibodies against dystrophin and the postsynaptic 58 kDa protein from Torpedo electric organ were used to localize homologs of these proteins in cultured skeletal muscle (Xenopus laevis). The Xenopus homolog is an Mr 48,000 protein and, like dystrophin, is a sarcolemmal protein. Both proteins localized precisely to talin-positive sites, hence with each other, on the substrate-apposed sarcolemma. Therefore, the first sites of appearance of dystrophin on cultured muscle cells are focal adhesions, i.e. specific sites of cytoskeleton/extracellular matrix interaction. These data also add to evidence that dystrophin and the 58 kDa act together.

摘要

相似文献

1
Dystrophin as a focal adhesion protein. Collocalization with talin and the Mr 48,000 sarcolemmal protein in cultured Xenopus muscle.
FEBS Lett. 1990 Nov 12;274(1-2):171-4. doi: 10.1016/0014-5793(90)81356-s.
2
Association of the Mr 58,000 postsynaptic protein of electric tissue with Torpedo dystrophin and the Mr 87,000 postsynaptic protein.电组织中58,000道尔顿突触后蛋白与电鳐肌营养不良蛋白及87,000道尔顿突触后蛋白的关联
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3
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4
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3
Retinal signal transmission in Duchenne muscular dystrophy: evidence for dysfunction in the photoreceptor/depolarizing bipolar cell pathway.
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J Clin Invest. 1994 Jun;93(6):2425-30. doi: 10.1172/JCI117250.
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The submembrane machinery for nicotinic acetylcholine receptor clustering.烟碱型乙酰胆碱受体聚集的膜下机制。
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