HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Fellin, F. M. Articles by Martinez, J. Search for Related Content PubMed PubMed Citation Articles by Fellin, F. M. Articles by Martinez, J. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 263, Issue 4, 1791-1797, Feb, 1988

Binding and cross-linking of rabbit fibronectin by rabbit hepatocytes in suspension

FM Fellin, C Barsigian, E Rich and J Martinez
Cardeza Foundation for Hematologic Research, Department of Medicine, Jefferson Medical College of Thomas Jefferson University, Philadelphia, Pennsylvania 19107.

Fibronectin purified from rabbit plasma was radioiodinated, and its interaction with rabbit hepatocytes in suspension was studied. Iodinated fibronectin interacted in a time-dependent fashion reaching plateau at 3 h. The interaction was greater in the presence of calcium than in the presence of magnesium or EDTA. Saturation occurred at about 140 nM fibronectin with about 1,400,000 molecules bound per cell. The interaction could be inhibited by unlabeled fibronectin or fibrinogen but not by the tetrapeptide Arg-Gly-Asp-Ser or by albumin, transferrin, or fetuin. About 50% of the bound iodinated fibronectin was incorporated, in a calcium-dependent fashion, into cross-linked high molecular weight complexes at the cell surface through a mechanism consistent with a cellular transglutaminase-mediated reaction. Iodinated fibronectin which could be displaced from the cell was monomeric in nature, while the cell-associated material remained in high molecular weight complexes. The role of the interaction is currently under investigation, but it is possible that the binding may promote cellular adhesion or facilitate intercellular interaction.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				E. A. Zemskov, I. Mikhailenko, D. K. Strickland, and A. M. Belkin Cell-surface transglutaminase undergoes internalization and lysosomal degradation: an essential role for LRP1 J. Cell Sci., September 15, 2007; 120(18): 3188 - 3199. [Abstract] [Full Text] [PDF]

				A. Janiak, E. A. Zemskov, and A. M. Belkin Cell Surface Transglutaminase Promotes RhoA Activation via Integrin Clustering and Suppression of the Src-p190RhoGAP Signaling Pathway Mol. Biol. Cell, April 1, 2006; 17(4): 1606 - 1619. [Abstract] [Full Text] [PDF]

				J. Hang, E. A. Zemskov, L. Lorand, and A. M. Belkin Identification of a Novel Recognition Sequence for Fibronectin within the NH2-terminal {beta}-Sandwich Domain of Tissue Transglutaminase J. Biol. Chem., June 24, 2005; 280(25): 23675 - 23683. [Abstract] [Full Text] [PDF]

				A. M. Belkin, G. Tsurupa, E. Zemskov, Y. Veklich, J. W. Weisel, and L. Medved Transglutaminase-mediated oligomerization of the fibrin(ogen) {alpha}C domains promotes integrin-dependent cell adhesion and signaling Blood, May 1, 2005; 105(9): 3561 - 3568. [Abstract] [Full Text] [PDF]

				H.-C. Cheng, M. Abdel-Ghany, R. C. Elble, and B. U. Pauli Lung Endothelial Dipeptidyl Peptidase IV Promotes Adhesion and Metastasis of Rat Breast Cancer Cells via Tumor Cell Surface-associated Fibronectin J. Biol. Chem., September 11, 1998; 273(37): 24207 - 24215. [Abstract] [Full Text] [PDF]

				S.D. Bradway and M.J. Levine Do Proline-rich Proteins Modulate a Transglutaminase Catalyzed Mechanism of Candidal Adhesion? Critical Reviews in Oral Biology & Medicine, January 1, 1993; 4(3): 293 - 299. [Abstract] [Full Text] [PDF]