Decorin and glycosaminoglycan synthesis in skin fibroblasts from patients with systemic sclerosis.
We investigated the expression of decorin and the synthesis of sulphated glycosaminoglycans (GAGs) in cultured fibroblasts from patients with early-stage systemic sclerosis (SSc). Decorin mRNA levels were 1.8-fold higher in SSc fibroblasts than in control fibroblasts. SSc fibroblasts also produced 2.3-fold more decorin core protein and 2.2-fold more sulphated GAGs including dermatan sulphate and chondroitin sulphate. Newly synthesized GAGs, in the presence of p-nitrophenyl beta-xylopyranoside, which elongates dermatan sulphate and chondroitin sulphate as an initiator, were increased tenfold and were mainly composed of dermatan sulphate and chondroitin sulphate. The rate of stimulation by the beta-xyloside was similar in SSc and control fibroblasts. These results suggest that the increased amount of dermatan/chondroitin sulphate in SSc fibroblasts reflects an enhanced expression of decorin core protein. Type I collagen mRNA levels in SSc fibroblasts were also increased together with its synthesis. Therefore, our results indicate that an altered decorin and collagen production may affect the organization of collagen fibres and the fibrotic process observed in patients with SSc.
Kuroda
K
K
Department of Dermatology, School of Medicine, Chiba University, Japan.
Shinkai
H
H
D000328:Adult; D003094:Collagen / Q000032:analysis; D058575:Decorin; D016326:Extracellular Matrix Proteins; D005260:Female; D005347:Fibroblasts / Q000378:metabolism; D006025:Glycosaminoglycans / Q000096:biosynthesis*; D006801:Humans; D008875:Middle Aged; D011509:Proteoglycans / Q000096:biosynthesis*; D012595:Scleroderma, Systemic / Q000378:metabolism*; D012867:Skin / Q000166:cytology / Q000378:metabolism
C546878:DCN protein, human; D058575:Decorin; D016326:Extracellular Matrix Proteins; D006025:Glycosaminoglycans; D011509:Proteoglycans; D003094:Collagen