title: Abnormal expression of proteoglycans in Ullrich's disease with collagen VI deficiency.
abstract: Patients with Ullrich's disease have generalized muscle weakness, multiple contractures of the proximal joints, and hyperextensibility of the distal joints. Recently we found a marked reduction of fibronectin receptors in the skin and cultured fibroblasts of two patients with Ullrich's disease with collagen VI deficiency, and speculated that an abnormality of cell adhesion may be involved in the pathogenesis of the disease. In this study, we investigated the expression of proteoglycans and adhesion molecules in Ullrich's disease and other muscle diseases. We found a reduction of NG2 proteoglycan in the membrane of skeletal muscle but not in the skin in Ullrich's disease. By contrast, we found the upregulation of tenascin C in the extracellular matrix of skeletal muscle in Ullrich's disease. Our findings suggest that abnormal expression of proteoglycans and adhesion molecules may be involved in the pathogenesis of the dystrophic muscle changes in Ullrich's disease.
authors.affiliation: Department of Neurology and Geriatrics, Faculty of Medicine, Kagoshima University, 8-35-1 Sakuragaoka, Kagoshima 890-8520, Japan.
authors.forename: Keiko
authors.initials: K
authors.lastname: Higashi
authors.forename: Itsuro
authors.initials: I
authors.lastname: Higuchi
authors.forename: Takahito
authors.initials: T
authors.lastname: Niiyama
authors.forename: Yuichi
authors.initials: Y
authors.lastname: Uchida
authors.forename: Tadafumi
authors.initials: T
authors.lastname: Shiraishi
authors.forename: Akihiro
authors.initials: A
authors.lastname: Hashiguchi
authors.forename: Akiko
authors.initials: A
authors.lastname: Saito
authors.forename: Takashi
authors.initials: T
authors.lastname: Horikiri
authors.forename: Masahito
authors.initials: M
authors.lastname: Suehara
authors.forename: Kimiyoshi
authors.initials: K
authors.lastname: Arimura
authors.forename: Mitsuhiro
authors.initials: M
authors.lastname: Osame
mesh_terms: D000328:Adult; D000941:Antigens / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D002462:Cell Membrane / Q000737:chemistry; D024142:Collagen Type VI / Q000172:deficiency* / Q000235:genetics; D015536:Down-Regulation; D005109:Extracellular Matrix / Q000737:chemistry / Q000378:metabolism; D016368:Frameshift Mutation; D006801:Humans; D008297:Male; D018482:Muscle, Skeletal / Q000737:chemistry / Q000378:metabolism / Q000473:pathology; D009136:Muscular Dystrophies / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D011509:Proteoglycans / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D012867:Skin / Q000737:chemistry / Q000378:metabolism; D013577:Syndrome; D019063:Tenascin / Q000032:analysis / Q000378:metabolism*; D015854:Up-Regulation; D000099216:Chondroitin Sulfate Proteoglycan 4
chemical_list: D000941:Antigens; D024142:Collagen Type VI; D011509:Proteoglycans; D019063:Tenascin; D000099216:Chondroitin Sulfate Proteoglycan 4