Increased deposition of chondroitin/dermatan sulfate glycosaminoglycan and upregulation of 1,3-glucuronosyltransferase I in pulmonary fibrosis

monary fibrosis (PF) is characterized by increased deposition of proteoglycans (PGs), in particular core proteins. Glycosaminoglycans (GAGs) are key players in tissue repair and fibrosis, and we investi-gated whether PF is associated with changes in the expression and structure of GAGs as well as in the expression of 1,3-glucuronosyl-transferase I (GlcAT-I), a rate-limiting enzyme in GAG synthesis. Lung biopsies from idiopathic pulmonary fibrosis (IPF) patients and lung tissue from a rat model of bleomycin (BLM)-induced PF were immunostained for chondroitin sulfated-GAGs and GlcAT-I expres-sion. Alterations in disaccharide composition and sulfation of chon-droitin/dermatan sulfate (CS/DS) were evaluated by fluorophore-assisted carbohydrate electrophoresis (FACE) in BLM rats. Lung fibroblasts isolated from control (saline-instilled) or BLM rat lungs were assessed for GAG structure and GlcAT-I expression. Disaccha-ride analysis showed that 4- and 6-sulfated disaccharides were in