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Titolo:
HUMAN DYSTROGLYCAN - SKELETAL-MUSCLE CDNA, GENOMIC STRUCTURE, ORIGIN OF TISSUE-SPECIFIC ISOFORMS AND CHROMOSOMAL LOCALIZATION
Autore:
IBRAGHIMOVBESKROVNAYA O; MILATOVICH A; OZCELIK T; YANG B; KOEPNICK K; FRANCKE U; CAMPBELL KP;
Indirizzi:
UNIV IOWA,COLL MED,HOWARD HUGHES MED INST,400 EMRB IOWA CITY IA 52242 UNIV IOWA,COLL MED,HOWARD HUGHES MED INST,400 EMRB IOWA CITY IA 52242 UNIV IOWA,COLL MED,DEPT PHYSIOL & BIOPHYS IOWA CITY IA 52242 STANFORD UNIV,MED CTR,SCH MED,HOWARD HUGHES MED INST STANFORD CA 94305 STANFORD UNIV,MED CTR,SCH MED,DEPT GENET & PEDIAT STANFORD CA 94305
Titolo Testata:
Human molecular genetics
fascicolo: 10, volume: 2, anno: 1993,
pagine: 1651 - 1657
SICI:
0964-6906(1993)2:10<1651:HD-SCG>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
EPIDERMOLYSIS BULLOSA SIMPLEX; DUCHENNE MUSCULAR-DYSTROPHY; PROTEOGLYCAN CORE PROTEIN; RENAL-CELL CARCINOMA; GLYCOPROTEIN; MEMBRANE; RECEPTOR; HETEROZYGOSITY; ORGANIZATION; DEFICIENCY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
O. Ibraghimovbeskrovnaya et al., "HUMAN DYSTROGLYCAN - SKELETAL-MUSCLE CDNA, GENOMIC STRUCTURE, ORIGIN OF TISSUE-SPECIFIC ISOFORMS AND CHROMOSOMAL LOCALIZATION", Human molecular genetics, 2(10), 1993, pp. 1651-1657

Abstract

Dystroglycan is a novel laminin binding component of the dystrophin-glycoprotein complex which provides a linkage between the subsarcolemmal cytoskeleton and the extracellular matrix. Here we report the cDNA and genomic structure of human dystroglycan. The human dystroglycan is encoded by a single gene (DAG1) mapped to chromosome 3 band p21. The coding sequence is organized into two exons, separated by a large intron. The predicted amino acid sequence of human and rabbit dystroglycan are 93% identical with predicted glycosylation sites being conserved. Human dystroglycan is expressed in a variety of fetal and adult tissues. Our data suggest that muscle and non-muscle isoforms of dystroglycan differ by carbohydrate moieties but not protein sequence. Therefore,we hypothesize that variable glycosylation of the conserved protein core might modulate laminin binding. The relationship of dystroglycan to human diseases is discussed.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/07/20 alle ore 22:23:43