-
Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix.
Howard Hughes Medical Institute, University of Iowa College of Medicine, Iowa City 52242.
The primary sequence of two components of the dystrophin-glycoprotein complex has been established by complementary, DNA cloning. The transmembrane 43K and extracellular 156K dystrophin-associated glycoproteins (DAGs) are encoded by a single messenger RNA and the extracellular 156K DAG binds laminin. Thus, the 156K DAG is a new laminin-binding glycoprotein which may provide a linkage between the sarcolemma and extracellular matrix. These results support the hypothesis that the dramatic reduction in the 156K DAG in Duchenne muscular dystrophy leads to a loss of a linkage between the sarcolemma and extracellular matrix and that this may render muscle fibres more susceptible to necrosis.
PMID: 1741056 [PubMed - indexed for MEDLINE]
-
Cited by 99 PubMed Central articles
-
Ligation of alpha-dystroglycan on podocytes induces intracellular signaling: a new mechanism for podocyte effacement?
Vogtländer NP, Visch HJ, Bakker MA, Berden JH, van der Vlag J.
PLoS One. 2009 Jun 19; 4(6):e5979. Epub 2009 Jun 19.
[PLoS One. 2009]
-
Loss of alpha-dystroglycan laminin binding in epithelium-derived cancers is caused by silencing of LARGE.
de Bernabé DB, Inamori K, Yoshida-Moriguchi T, Weydert CJ, Harper HA, Willer T, Henry MD, Campbell KP.
J Biol Chem. 2009 Apr 24; 284(17):11279-84. Epub 2009 Feb 24.
[J Biol Chem. 2009]
-
Dystroglycan, Tks5 and Src mediated assembly of podosomes in myoblasts.
Thompson O, Kleino I, Crimaldi L, Gimona M, Saksela K, Winder SJ.
PLoS One. 2008; 3(11):e3638. Epub 2008 Nov 4.
[PLoS One. 2008]
- » See all...