ISI Web of Knowledge Take the next step  
Web of Science®
 
Previous Record (inactive) Record 1  of  1 Next Record (inactive)
Record from Web of Science®
STIMULATION OF SULFATED GLYCOSAMINOGLYCAN AND DECORIN PRODUCTION IN ADULT DERMAL FIBROBLASTS BY RECOMBINANT HUMAN INTERLEUKIN-4
Author(s): WEGROWSKI Y, PALTOT V, GILLERY P, KALIS B, RANDOUX A, MAQUART FX
Source: BIOCHEMICAL JOURNAL    Volume: 307    Pages: 673-678    Part: Part 3    Published: MAY 1 1995  
Times Cited: 40     References: 46     
Abstract: Interleukin-4 (IL-4) is a pleiotropic cytokine expressed by inflammatory cells. Previous work from our laboratory has shown that it stimulates collagen synthesis in fibroblasts. Here we report the effects of recombinant human IL-4 on glycosaminoglycan (GAG) and proteoglycan synthesis in normal dermal fibroblasts from adult donors. IL-4 (10 and 100 units/ml) induced a dose-dependent increase of [H-3]glucosamine and [S-35]sulphate incorporation into total GAGs. The analysis of the different GAG fractions indicated the enhanced synthesis of dermatan/chondroitin sulphates. IL-4 had no effect on hyaluronan synthesis. The increase of sulphated GAG synthesis was correlated with an increase of proteoglycans in the culture medium. Decorin was identified as the major chondroitin/dermatan sulphate-containing proteoglycan in the culture medium of fibroblasts. Its synthesis was strongly stimulated by IL-4. Both the core-protein synthesis and mRNA expression were enhanced, indicating that the cytokine acted, at least in part, at the pre-translational level. These results indicate that IL-4 is able to modulate not only collagen, but also proteoglycan, production by human fibroblasts. Their implications in physiopathological processes such as wound healing or fibrosis is suggested.
Document Type: Article
Language: English
Addresses:
1. FAC MED REIMS, BIOCHIM LAB, CNRS, ER 084, F-51095 REIMS, FRANCE
2. FAC MED REIMS, RECH BIOMED DERMATOL LAB, F-51095 REIMS, FRANCE
Publisher: PORTLAND PRESS, 59 PORTLAND PLACE, LONDON W1N 3AJ, ENGLAND
Subject Category: Biochemistry & Molecular Biology
IDS Number: QW667
ISSN: 0264-6021
Previous Record (inactive) Record 1  of  1 Next Record (inactive)
Record from Web of Science®
  
Thomson Reuters Logo