マトリックス工学 : 新規細胞外マトリックス分子の創出と細胞の機能制御

概要

論文の詳細を見る
Extracellular matrix(ECM)provides a microenvironment in which a variety of extracellular signals for regulating cell behavior are assembled into an intricate meshwork. Here we describe a novel methodology for manipulating the composition and organization of ECM through immobilization of various bioactive proteins as chimera with the matrix assembly domain of fibronectin. We previously showed that a truncated form of fibronectin comprising N-terminal 70 kDa region and C-terminal 37 kDa region, refferred to as "minifibronectin", retained the ability to assemble into ECM. Taking advantage of the matrix assembly activity of minifibronectin, we demonstrated that an immunogloblin-binding protein, protein A, was immobilized into ECM in an active form upon chimerization with minifibronectin(i. e., insertion of protein A between the N-terminal 70 kDa and the C-terminal 37 kDa regions). We further extended this finding to other bioactive proteins such as TIMP-1, aequorin(a photoprotein of jelly fish), and transforming growth factor α(TGFα), successfully targeting these proteins into ECM with retention of their biological activities. The method we developed offers a new key technology to design multifunctional super-ECM for manipulating cell growth and differentiation both in vitro and in vivo. We propose to call this new technology "matrix engineering".
日本結合組織学会の論文
1998-03-25