Original Article

Enhancement of Endothelial Cell Migration and In Vitro Tube Formation by TAP20, A Novel ß5 Integrin–Modulating, PKC-Dependent Protein

Correspondence to: Shaoqing Tang, Albert Einstein College of Medicine, Forchheimer Building G-42, 1300 Morris Park Ave., Bronx, NY 10461. Tel:(718) 430-2365 Fax:(718) 430-8989 E-mail:tang{at}aecom.yu.edu.

Migration, proliferation, and tube formation of endothelial cells are regulated by a protein kinase C isoenzyme PKC. A full-length cDNA encoding a novel 20-kD protein, whose expression was PKC-dependent, was identified in endothelial cells, cloned, characterized, and designated as theta-associated protein (TAP) 20. Overexpression of TAP20 decreased cell adhesion and enhanced migration on vitronectin and tube formation in three-dimensional culture. An antiintegrin vß5 antibody prevented these TAP20 effects. Overexpression of TAP20 also decreased focal adhesion formation in vß3-deficient cells. The interaction between TAP20 and ß5 integrin cytoplasmic domain was demonstrated by protein coprecipitation and immunoblotting. Thus, the discovery of TAP20, which interacts with integrin ß5 and modulates cell adhesion, migration, and tube formation, further defines a possible pathway to angiogenesis dependent on PKC.

Key Words: TAP20, integrin, PKC, endothelial cells, migration

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