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

J. Biol. Chem., Vol. 276, Issue 21, 18108-18114, May 25, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/21/18108    most recent M009597200v1 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 Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Cluzel, C. Articles by Exposito, J.-Y. Search for Related Content PubMed PubMed Citation Articles by Cluzel, C. Articles by Exposito, J.-Y. Social Bookmarking                      What's this?

Characterization of Fibrosurfin, an Interfibrillar Component of Sea Urchin Catch Connective Tissues^*

Caroline Cluzel, Claire Lethias, Frédéric Humbert, Robert Garrone, and Jean-Yves Exposito^§

From the Institut de Biologie et Chimie des Protéines, CNRS, Unité Mixte de Recherche 5086, Université Claude Bernard, 7 passage du Vercors, 69367 Lyon cedex 07, France

The Sea URchin Fibrillar (SURF) domain is a four-cysteine module present in the amino-propeptide of the sea urchin 2 fibrillar collagen chain. Despite numerous international genome and expressed sequence tag projects, computer searches have so far failed to identify similar domains in other species. Here, we have characterized a new sea urchin protein of 2656 amino acids made up of a series of epidermal growth factor-like and SURF modules. From its striking similarity to the modular organization of fibropellins, we called this new protein fibrosurfin. This protein is acidic with a calculated pI of 4.12. Eleven of the 17 epidermal growth factor-like domains correspond to the consensus sequence of calcium-binding type. By Western blot and immunofluorescence analyses, this protein is not detectable during embryogenesis. In adult tissues, fibrosurfin is co-localized with the amino-propeptide of the 2 fibrillar collagen chain in several collagenous ligaments, i.e., test sutures, spine ligaments, peristomial membrane, and to a lesser extent, tube feet. Finally, immunogold labeling indicates that fibrosurfin is an interfibrillar component of collagenous tissues. Taken together, the data suggest that proteins possessing SURF modules are localized in the vicinity of mineralized tissues and could be responsible for the unique properties of sea urchin mutable collagenous tissues.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EMBL Data Bank with accession number(s) AJ291489.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				A. Aouacheria, C. Cluzel, C. Lethias, M. Gouy, R. Garrone, and J.-Y. Exposito Invertebrate Data Predict an Early Emergence of Vertebrate Fibrillar Collagen Clades and an Anti-incest Model J. Biol. Chem., November 12, 2004; 279(46): 47711 - 47719. [Abstract] [Full Text] [PDF]

				C. Cluzel, C. Lethias, R. Garrone, and J.-Y. Exposito Distinct Maturations of N-propeptide Domains in Fibrillar Procollagen Molecules Involved in the Formation of Heterotypic Fibrils in Adult Sea Urchin Collagenous Tissues J. Biol. Chem., March 12, 2004; 279(11): 9811 - 9817. [Abstract] [Full Text] [PDF]