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 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 Schmidhauser, C.
Right arrow Articles by Parish, R. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Schmidhauser, C.
Right arrow Articles by Parish, R. W.

Journal of Cell Science, Vol 95, Issue 3 499-506, Copyright © 1990 by Company of Biologists

JOURNAL ARTICLES

A mycoplasmal protein influences tumour cell invasiveness and contact inhibition in vitro

C Schmidhauser, R Dudler, T Schmidt and RW Parish
Institut fur Pflanzenbiologie, Universitat Zurich, Switzerland.

Fab fragments of a monoclonal antibody directed against p37, a protein associated with the surface of FS9 mouse sarcoma cells, were previously found to inhibit the highly invasive behaviour of FS9 cells in vitro. We show that p37 originates from Mycoplasma hyorhinis. Infecting various cell lines with the mycoplasma consistently increased their invasiveness when confronted with chicken heart fibroblasts using Abercrombie's confronted explant technique. Conversely, removing the mycoplasmas or blocking p37 with specific Fab fragments reduced invasiveness. Analysis of individual cell collisions using time-lapse filming showed that the addition of Fab fragments to cells infected with M. hyorhinis greatly increased the level of contact inhibition. The antibody also reduced the invasiveness of transformed cells that did not express the p37 antigen. Hence, a cellular protein or proteins that are structurally related to p37 apparently influence invasive behavior.


This article has been cited by other articles:


Home page
 Molecular Cancer TherapeuticsHome page
M. Gong, L. Meng, B. Jiang, J. Zhang, H. Yang, J. Wu, and C. Shou
p37 from Mycoplasma hyorhinis promotes cancer cell invasiveness and metastasis through activation of MMP-2 and followed by phosphorylation of EGFR
Mol. Cancer Ther., March 1, 2008; 7(3): 530 - 537.
[Abstract] [Full Text] [PDF]

Home page
 Molecular Cancer TherapeuticsHome page
C. M. Ketcham, S. Anai, R. Reutzel, S. Sheng, S. M. Schuster, R. B. Brenes, M. Agbandje-McKenna, R. McKenna, C. J. Rosser, and S. K. Boehlein
p37 induces tumor invasiveness
Mol. Cancer Ther., July 1, 2005; 4(7): 1031 - 1038.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
B. Henrich, M. Hopfe, A. Kitzerow, and U. Hadding
The Adherence-Associated Lipoprotein P100, Encoded by an opp Operon Structure, Functions as the Oligopeptide-Binding Domain OppA of a Putative Oligopeptide Transport System in Mycoplasma hominis
J. Bacteriol., August 15, 1999; 181(16): 4873 - 4878.
[Abstract] [Full Text]


© The Company of Biologists Ltd 1990