Skip Navigation

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 Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Maeda, T.
Right arrow Articles by Sekiguchi, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Maeda, T.
Right arrow Articles by Sekiguchi, K.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1994, Vol. 115, No. 2 182-189
© 1994 Japanese Biochemical Society


research-article

Cell-Adhesive Activity and Receptor-Binding Specificity of the Laminin-Derived YIGSR Sequence Grafted onto Staphylococcal Protein A1

Toshinaga Maeda*, Koiti Titani** and Kiyotoshi Sekiguchi*,2

*Research Institute, Osaka Medical Center for Maternal and Child Health Izumi, Osaka 590-02
**Institute for Comprehensive Medical Science, Fujia Health University School of Medicine Toyoake, Aichi 470-11

2To whom correspondence should be addressed

Laminin contains multiple oligopeptide motifs to promote cell adhesion and migration. One of these motifs is YIGSR within the B1 chain. We reconstituted the cell-adhesive activity of YIGSR motif by grafting it onto a truncated form of the Staphylococcal protein A (designated tSPA) via cassette mutagenesis. When coated on a polystyrene surface, the YIGSR-grafted tSPA (YIGSR-tSPA) promoted attachment and spreading of mouse melanoma and human rhabdomyosarcoma cells, but not of hamster fibroblasts. The cell-adhesive activity of YIGSR-tSPA was abolished by amino acid substitution or scrambling of the inserted YIGSR sequence. Divalent cations Mn2+ and Mg2+, but not Ca2+, promoted the cell adhesion to YIGSR-tSPA. Interestingly, the YIGSR-tSPA-mediated cell adhesion was barely inhibited by the linear peptide CDPGYIGSR-NH2, but was strongly inhibited by the cyclic peptide CDPGYIGSRC and another peptide PEILDVPST, which is a specific inhibitor for integrin {alpha}1. Among various anti-integrin antibodies, anti-{alpha}, and anti-ß1, antibodies specifically inhibited the cell adhesion to YIGSR-tSPA. In support of these observations, adhesion of rhabdomyosarcoma cells to intact laminin was also partially inhibited by synthetic PEILDVPST peptide and anti-{alpha}, antibody. These results, taken together, indicate that the YIGSR motif exerts its cell-adhesive activity through interaction with integrin {alpha}1.

1This investigation was supported by a Special Coordination Fund from the Science and Technology Agency of Japan and by Grants-in-Aid from the Ryoichi Naito Foundation for Medical Research, Terumo Life Science Foundation, and Fujita Health University


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
J. Appl. Physiol.Home page
M. A. Peake, L. M. Cooling, J. L. Magnay, P. B. M. Thomas, and A. J. El Haj
Cellular Responses to Mechanical Stress: Selected Contribution: Regulatory pathways involved in mechanical induction of c-fos gene expression in bone cells
J Appl Physiol, December 1, 2000; 89(6): 2498 - 2507.
[Abstract] [Full Text] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.