Recombinant human uteroglobin/CC10 inhibits the adhesion and migration of primary human endothelial cells via specific and saturable binding to fibronectin.

摘要: Uteroglobin (UG) or Clara Cell 10 kDa protein (CC10) is a small, stable, epithelial secretory anti-inflammatory protein. has been shown to inhibit neointimal formation in vivo after balloon angioplasty through an unknown mechanism. An interaction between UG and plasma fibronectin (Fn) demonstrated mice. Since Fn plays key role endothelial cell (EC) migration angiogenesis, we investigated whether recombinant human (rhUG) affects EC via binding. In this report, show saturable binding of rhUG depending on conformation that covalently cross-linked by transglutaminase (TGase). Additionally, our study highlights can also bind exogenously added self-secreted the membrane primary microvascular cells (HMVEC), although these complexes are weakly associated with plasmalemma. Upon solid phase, strongly inhibits HMVEC attachment Fn, but not other ECM proteins. Consequently, dose dependent fashion (I.C.50 = 65 nM) hinders “wound healing” vitro. The small size, stability tolerability suggest slow-release form genetically delivered could be used humans modulate cell/Fn interactions context tumor microenvironment inflammation fibrosis. J. Cell. Physiol. 207: 553–561, 2006. © 2006 Wiley-Liss, Inc.