spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

This Article
Right arrow Full Text (PDF)
Right arrow References
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by De Corte, V.
Right arrow Articles by Vandekerckhove, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by De Corte, V.
Right arrow Articles by Vandekerckhove, J.

Journal of Cell Science, Vol 107, Issue 3 405-416, Copyright © 1994 by Company of Biologists

JOURNAL ARTICLES

A 50 kDa protein present in conditioned medium of COLO-16 cells stimulates cell spreading and motility, and activates tyrosine phosphorylation of Neu/HER-2, in human SK-BR-3 mammary cancer cells

V De Corte, C De Potter, D Vandenberghe, N Van Laerebeke, M Azam, H Roels, M Mareel and J Vandekerckhove
Laboratory of Physiological Chemistry, University of Ghent, Belgium.

A factor present in conditioned medium of COLO-16 human cancer cells causes fast spreading, fast plasma membrane ruffling, cell shape change, net translocation, stimulation of chemotaxis and growth arrest in human SK-BR-3 mammary cancer cells. Based on the spreading effect, the factor was purified to homogeneity and migrated as a 50 kDa protein in SDS-polyacrylamide gel electrophoresis. Addition of the purified 50 kDa factor to the target cells in culture results in tyrosine phosphorylation of the p185erbB2 receptor concomitant with a fast redistribution and clustering of the receptor. The 50 kDa factor is also specifically retained by affinity chromatography on the immobilized extracellular domain of p185erbB2. Antibodies directed against this domain also inhibit the induction of motility. These data suggest that the 50 kDa factor is a putative ligand of p185erbB2 in SK-BR-3 cells. Biochemical and immunological evidence further indicate that this factor differs from p185erbB2 ligands described so far. Its activity could play a role in the pathogenesis of breast cancer.


This article has been cited by other articles:


Home page
 Clin. Cancer Res.Home page
J. G. Christensen, R. E. Schreck, E. Chan, X. Wang, C. Yang, L. Liu, J. Cui, L. Sun, J. Wei, J. M. Cherrington, et al.
High Levels of HER-2 Expression Alter the Ability of Epidermal Growth Factor Receptor (EGFR) Family Tyrosine Kinase Inhibitors to Inhibit EGFR Phosphorylation in Vivo
Clin. Cancer Res., December 1, 2001; 7(12): 4230 - 4238.
[Abstract] [Full Text] [PDF]

Home page
 JNCI J Natl Cancer InstHome page
V. R. J. Schelfhout, E. D. Coene, B. Delaey, S. Thys, D. L. Page, and C. R. De Potter
Pathogenesis of Paget's Disease: Epidermal Heregulin-{alpha}, Motility Factor, and the HER Receptor Family
J Natl Cancer Inst, April 19, 2000; 92(8): 622 - 628.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 1994