PRIMARY STRUCTURE OF DYSTROPHIN-ASSOCIATED GLYCOPROTEINS LINKING DYSTROPHIN TO THE EXTRACELLULAR-MATRIX

被引:1202
|
作者
IBRAGHIMOVBESKROVNAYA, O
ERVASTI, JM
LEVEILLE, CJ
SLAUGHTER, CA
SERNETT, SW
CAMPBELL, KP
机构
[1] UNIV IOWA,COLL MED,HOWARD HUGHES MED INST,IOWA CITY,IA 52242
[2] UNIV IOWA,COLL MED,DEPT PHYSIOL & BIOPHYS,IOWA CITY,IA 52242
[3] UNIV TEXAS,SW MED CTR,BIOPOLYMER FACIL HOWARD HUGHES MED INST,DALLAS,TX 75235
关键词
D O I
10.1038/355696a0
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 glyco proteins (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.
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页码:696 / 702
页数:7
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