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FEBS Lett. 1995 Jul 10;368(1):139-42.

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

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1
Department of Biophysical Chemistry, Biozentrum, University of Basel, Switzerland.

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.

PMID:
7615068
[Indexed for MEDLINE]
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