Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Varner, J. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Varner, J. A.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Volume 271, Number 27, Issue of July 5, 1996 pp. 16119-16125
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Isolation of a Sponge-derived Extracellular Matrix Adhesion Protein

(Received for publication, January 29, 1996, and in revised form, April 9, 1996)

Judith A. Varner

From the Department of Medicine 0063, University of California, San Diego, La Jolla, California 92093-0063

The development of stable intercellular adhesions in the animal kingdom permitted the evolution of the metazoans, of which the sponges are primitive examples. Intercellular adhesion in these simple animals is mediated by a high affinity interaction between the sponge cell surface and aggregation factor, a 2 × 107-Da proteoglycan that is one of the major components of the sponge extracellular matrix. This report describes a sponge cell surface and extracellular matrix ligand for the sponge proteoglycan, aggregation factor. The 210-kDa protein binds aggregation factor proteoglycan with high affinity (Kd = 7 × 10-9 M). Importantly, in soluble form, it also inhibits aggregation factor-mediated cell adhesion. This glycoprotein is expressed on the sponge cell surface and within the extracellular matrix. This novel sponge extracellular matrix protein may represent a primitive antecedent of the extracellular matrix adhesion proteins of higher organisms.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
X. Fernandez-Busquets and M. M. Burger
The Main Protein of the Aggregation Factor Responsible for Species-specific Cell Adhesion in the Marine Sponge Microciona prolifera Is Highly Polymorphic
J. Biol. Chem., October 31, 1997; 272(44): 27839 - 27847.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1996 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement