作者: Paul C. Billings , J. Charles Whitbeck , Christopher S. Adams , William R. Abrams , Arthur J. Cohen
关键词: Cell biology 、 Transforming growth factor beta 、 Biology 、 Biochemistry 、 Transforming growth factor 、 Protein domain 、 Fibronectin 、 Extracellular matrix 、 Matrix (biology) 、 Type I collagen 、 Binding domain
摘要: Proper growth and development require the orderly synthesis deposition of individual components extracellular matrix (ECM) into well ordered networks. Once formed, ECM maintains tissue structure houses resident cells. One component, βig-h3, is a highly conserved transforming factor-β-inducible protein that has been hypothesized to function as bifunctional linker between To gain insights its physiological function, full-length βig-h3 was produced using baculovirus expression system purified under native conditions. Human fibroblasts attached spread on βig-h3-coated plates developed actin stress fibers. Purified binds fibronectin (FN) type I collagen (Col I) but does not bind gelatin. Using defined fragments FN, we localized recognition region gelatin/collagen binding domain present in N-terminal FN molecule. Our results identify Col two ligands ECM.