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Purification of flounder ( Paralichthys olivaceus ) fibronectin and its localization during re‐epithelialization at a fin wound
Author(s) -
Kurokawa T.,
Suzuki T.,
Funakoshi S.
Publication year - 1993
Publication title -
journal of fish biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.672
H-Index - 115
eISSN - 1095-8649
pISSN - 0022-1112
DOI - 10.1111/j.1095-8649.1993.tb00577.x
Subject(s) - flounder , paralichthys , olive flounder , biology , fibronectin , antiserum , fibroblast , baby hamster kidney cell , wound healing , microbiology and biotechnology , cell , cell culture , biochemistry , antibody , fishery , immunology , fish <actinopterygii> , genetics
Plasma fibronectin (FN) of flounder Paralichthys olivacem was purified and characterized. Flounder FN was purified by a combination of affinity chromatography using Sepharose coupled with flounder gelatin and gel filtration on Superose 6. Flounder FN was found to be a disulphide‐linked heterodimer of 220 and 230 kDa polypeptides. It had cell‐spreading activity for baby hamster kidney (BHK) cells, which was inhibited by the synthetic peptide, Gly‐Arg‐Gly‐Asp‐Ser‐Pro. In flounder explants, anti‐flounder FN antiserum distinguished fibroblast‐like cells from epithelial cells; indirect immunofluorescence showed that the fibroblast‐like cells exhibited a fibrous staining to the antiserum, but that epithelial cells did not. These results suggest that flounder FN is a homologue of mammalian FN. The localization of FN during re‐epithelialization at the site of a severed fin was investigated. When the top of the fin was cut, epidermal cells covered the surface of the wound within 1 h. FN is detected at the wound site during epidermal cell migration, suggesting that it serves as a cell‐adhesion factor for prompt re‐epithelialization at wound sites.