Mechanism of adhesion and spreading-promoting activities and morphological holding of fish hepatocytes by plasma fibronectin from fishes.

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1.The plasm fibronectins (pFE) of tilapia, black bass and Japanese catfish which showed a specific behavior in the interaction between pFN and hepatocyte were purified and characterized. Two type of pFN (CpFN-I and-II) found in carp existed in the plasma of the three fishes. These peptide maps showed clearly a species difference.2.Tilapia hepatocytes which had not the ability of binding to CpFN-I adhered to the pronase digested-CpFN-I,suggesting that the cell binding domain to fish pFNa seemed to have a site to determine a species specificity.3.Topological arrangement of functional domains of CpFN-I and-II,and also developing of the simple methods for identification and purification of cell binding doman of CpFN-I were examined to make possible to study in detail the structure and function of the cell binding domain of the fish pFNs.(1), The topological arrangement of functional domains of CpFN-I was very similar to that of bovine pFN.CpFN-II,however, differed from CpFN-I in heparin binding domain.(2), It was useful for the simple method for identification of cell binding domain of CpFN-I that the hepatocytes of Japanese eel were cultured on the membrane transferred thermolytic fragments of CpFN-I by Western blot technique and then the cells adhering to the fragments were visualized by tmmunoenzymatic technique using anti cytoskeletal protein antibody as a probe. This simple method demonstrated structural difference in the cell binding fragment among type I pFNs of the three species.(3), Three kinds of the cell binding thermolytic fragments of CpFN-I were separated by sequential chromatographies on a gel filtration and a reverse phase columns.4.Western blot analysis using anti integrin antibody as probe showed that hepatocytes of Japanese eel and rainbow trout differed in distribution of FN-receptor.