JCB logo
amgmicro.com
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 518K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Tang, S.
Right arrow Articles by Ware, J. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tang, S.
Right arrow Articles by Ware, J. A.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

© The Rockefeller University Press, 0021-9525/1999//1073 $5.00
The Journal of Cell Biology, Volume 147, Number 5, , 1999 1073-1084

Original Article

Enhancement of Endothelial Cell Migration and in Vitro Tube Formation by Tap20, a Novel β5 Integrin–Modulating, Pkc{theta}-Dependent Protein



Shaoqing Tanga, Yunling Gaoa, and J. Anthony Warea

a Cardiovascular Division, Department of Medicine, Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York 10461
Albert Einstein College of Medicine, Forchheimer Building G-42, 1300 Morris Park Ave., Bronx, NY 10461.(718) 430-8989(718) 430-2365

tang{at}aecom.yu.edu

Migration, proliferation, and tube formation of endothelial cells are regulated by a protein kinase C isoenzyme PKC{theta}. A full-length cDNA encoding a novel 20-kD protein, whose expression was PKC{theta}-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 {alpha}vβ5 antibody prevented these TAP20 effects. Overexpression of TAP20 also decreased focal adhesion formation in {alpha}vβ3-deficient cells. The interaction between TAP20 and β5 integrin cytoplasmic domain was demonstrated by protein coprecipitation and immunoblotting. Thus, the discovery of TAP20, which interacts with integrin β5 and modulates cell adhesion, migration, and tube formation, further defines a possible pathway to angiogenesis dependent on PKC{theta}.

Key Words: TAP20 • integrin • PKC{theta} • endothelial cells • migration

© 1999 The Rockefeller University Press

Abbreviations used in this paper: EC, endothelial cell(s); ECM, extracellular matrix; EGFP, enhanced GFP; FAK, focal adhesion kinase; FN, fibronectin; HUVEC, human umbilical vein EC(s); GFP, green fluorescent protein; GST, glutathione S-transferase; LN, laminin; PKC, protein kinase C; RCE, rat capillary endothelial cell(s); TAP, theta-associated protein; VEGF, vascular endothelial growth factor; VN, vitronectin; wt, wild-type.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?




  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents