Abstract
The mechanism of antitumor activities in hen egg white ovomucin (OVM) was analyzed by examining the interaction between the 120 kDa fragment (a highly glycosylated fragment in β-subunit from the pronase-treated OVM) and basic fibroblast growth factor receptor (bFGFR). The 120 kDa fragment, which was transblotted onto a polyvinylidene difluoride membrane after SDS-polyacrylamide gel electrophoresis, was found to interact with bFGFR. The interaction was detected by Western blotting method with mouse anti-FGFR IgM. When sarcoma-180 (SR-180) cells were cultured on addition of the 120 kDa fragment, they were observed to be in the necrotic state by transmission electron microscopy, and the 120 kDa fragment was seen to be dispersed on the cell surface by light and transmission electron microscopic observations with the immunocytochemical staining method. The growth of SR-180 cell in the presence of bFGF was reduced with increase in the amount of 120 kDa fragment added. Thus, it was found that the 120 kDa fragment interacted with SR-180 cells through bFGFR and affected them.
