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Electron microscopic evidence for a mucin-like region in chick muscle alpha-dystroglycan.


Brancaccio, A; Schulthess, T; Gesemann, M; Engel, J (1995). Electron microscopic evidence for a mucin-like region in chick muscle alpha-dystroglycan. FEBS Letters, 368(1):139-142.

Abstract

alpha-Dystroglycan has been isolated from chicken cardiac muscle and its molecular weight was estimated to be approximately 135 kDa. The avian protein interacts with murine Engelbreth-Holm-Swarm (EHS) tumor laminin via interaction with the C-terminal LG4 and LG5 domains (fragment E3) of the laminin alpha-chain. This laminin binding is calcium-dependent and can be competed by heparin. Electron microscopy investigation on the shape of alpha-dystroglycan suggests that the core protein consists of two roughly globular domains connected by a segment which most likely corresponds to a mucin-like central region also predicted by sequence analysis on mammalian isoforms. This segment may act as a spacer in the dystrophin-associated glycoproteins complex exposing the N-terminal domain of alpha-dystroglycan to laminin in the extracellular space.

alpha-Dystroglycan has been isolated from chicken cardiac muscle and its molecular weight was estimated to be approximately 135 kDa. The avian protein interacts with murine Engelbreth-Holm-Swarm (EHS) tumor laminin via interaction with the C-terminal LG4 and LG5 domains (fragment E3) of the laminin alpha-chain. This laminin binding is calcium-dependent and can be competed by heparin. Electron microscopy investigation on the shape of alpha-dystroglycan suggests that the core protein consists of two roughly globular domains connected by a segment which most likely corresponds to a mucin-like central region also predicted by sequence analysis on mammalian isoforms. This segment may act as a spacer in the dystrophin-associated glycoproteins complex exposing the N-terminal domain of alpha-dystroglycan to laminin in the extracellular space.

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Additional indexing

Item Type:Journal Article, refereed
Communities & Collections:04 Faculty of Medicine > Brain Research Institute
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
Language:English
Date:1995
Deposited On:11 Feb 2008 12:13
Last Modified:05 Apr 2016 12:12
Publisher:Elsevier
ISSN:0014-5793
Publisher DOI:10.1016/0014-5793(95)00628-M
PubMed ID:7615068
Permanent URL: http://doi.org/10.5167/uzh-132

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