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 Asaga, H.
Right arrow Articles by Yoshizato, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Asaga, H.
Right arrow Articles by Yoshizato, K.

Journal of Cell Science, Vol 101, Issue 3 625-633, Copyright © 1992 by Company of Biologists

JOURNAL ARTICLES

Recognition of collagen by fibroblasts through cell surface glycoproteins reactive with Phaseolus vulgaris agglutinin

H Asaga and K Yoshizato
Molecular Cell Science Laboratory, Faculty of Science, Hiroshima University, Japan.

The role of glycochains of cell surface glycoproteins in the cell to collagen interaction was examined by studying the effect of lectins on the fibroblast-mediated collagen gel contraction. Lectins of Phaseolus vulgaris agglutinin (PHA), concanavalin A (ConA), lentil seed agglutinin (LCA), pea agglutinin (PSA), Ricinus communis agglutinin-60 (RCA), and wheat germ agglutinin (WGA) dose-dependently inhibited gel contraction, while lectins of mushroom agglutinin (ABA), peanut agglutinin (PNA), pokeweed mitogen (PWM), and soybean agglutinin (SBA) did not. Of these lectins, PHA seemed to be worthy of further analysis, because PHA, but not other lectins, inhibited spreading of fibroblasts on collagen fibrils but not on plastic or gelatin, suggesting that cell-surface glycoproteins responsive to the lectin are involved in the specific binding of fibroblasts to native collagen fibrils. The inhibitory effect of PHA-E4, an isolectin of PHA, was more intense than that of PHA-L4, another isolectin of PHA. The collagen gel contraction was also inhibited by tunicamycin and monensin in a concentration-dependent and reversible manner. These results strongly suggest that PHA-E4-reactive glycoproteins of the fibroblast surface play an important role in cell to collagen binding during the gel contraction. Five membrane proteins including beta 1 subunits of the integrin family were obtained by affinity chromatography with PHA-E4.


This article has been cited by other articles:


Home page
 IOVSHome page
L. Taliana, M. D. M. Evans, S. D. Dimitrijevich, and J. G. Steele
Vitronectin or Fibronectin Is Required for Corneal Fibroblast-Seeded Collagen Gel Contraction
Invest. Ophthalmol. Vis. Sci., January 1, 2000; 41(1): 103 - 109.
[Abstract] [Full Text]

Home page
 IOVSHome page
H. Wenkel, D. Kent, P. Hiscott, M. Batterbury, C. Groenewald, C. M. Sheridan, L.-G. Yu, and J. Milton
Modulation of Retinal Pigment Epithelial Cell Behavior by Agaricus Bisporus Lectin
Invest. Ophthalmol. Vis. Sci., November 1, 1999; 40(12): 3058 - 3062.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 1992