Premium
Effect of retinyl acetate on the assembly of the fibronectin extracellular matrix and the processing of the fibronectin receptor β subunit of confluent C3H/10T1/2 mouse embryo fibroblasts
Author(s) -
Suzuki Satoshi S.,
Piette Lawrence H.
Publication year - 1993
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240510210
Subject(s) - fibronectin , extracellular matrix , retinyl acetate , extracellular , microbiology and biotechnology , cell culture , fibroblast , receptor , chemistry , biology , biochemistry , retinoic acid , genetics
Abstract The mouse embryo fibroblast cell line, C3H/10T1/2, synthesized and deposited a large amount of fibronectin especially in the pericellular matrix. Confluent cultures of these cells cultured in the presence of 0.3 μg/ml of retinyl acetate released cell surface fibronectin and the extracellular matrix fibronectin fibrils were disorganized. The immunoblot analysis demonstrated that the number of the fibronectin receptor was decreased in the prolonged culturing of retinyl acetate‐treated cells. Immunoprecipitation of 35 S‐methionine pulse‐chase labeled cell extracts by antifibronectin receptor antibody indicated that about one‐half of the pre‐β subunit was processed and converted to the mature form in control cells, and only about one‐fourth of the pre‐β subunit was processed in the retinyl acetate‐treated confluent cells. 1‐deoxymannojirimycin (MNJ), which is an inhibitor of oligosaccharide processing, induced disorganization of the extracellular matrix fibronectin assembly similar to that observed with retinyl acetate. The results of this study suggest that a mechanism of action of retinyl acetate is inhibition of the glycosylation during processing of the fibronectin receptor, a step necessary for fibronectin binding and for assembly of the extracellular matrix. © 1993 Wiley‐Liss, Inc.