反細胞接着分子としてのフィブロネクチン : 反接着活性部位の同定およびその機能発現機構

概要

論文の詳細を見る
We have found that a 30kDa fragment derived from the heparin-binding domain 2(Hep2)of fibronectin(FN)shows anti-adhesive activity. This anti-adhesive activity was localized in a hydrophobic amino acid sequence YTIYVIAL(#1848-1855)that resides in the 14th type III module of FN, indicating that the anti-adhesive site may be usually buried within the FN structure because of its hydrophobic nature. We then investigated the mechanism by which the cryptic anti-adhesive site is exposed in vivo. As a result, matrix metalloproteinase-2(MMP-2 / gelatinase A)was shown to degrade the Hep2 fragment to produce an anti-adhesive peptide containing the YTIYVIAL sequence. Furthermore, the Hep2 fragment became anti-adhesive after the interaction with heparin, in parallel with changing in the secondary structure of the Hep2 fragment similar to the structure change of the fragment induced by urea denaturation. Thus the cryptic anti-adhesive site can be easily exposed through the physiological processes such as proteolytic degradation and interaction with certain ECM components. The anti-adhesive activity buried within the FN molecule may play an important role in various biological events by counteracting cell adhesion to ECM.
日本結合組織学会の論文
1998-09-25