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

This Article Full Text Full Text (PDF) All Versions of this Article: M500239-JLR200v1 46/12/2673    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services 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 Edelstein, C. Articles by Scanu, A. M. Search for Related Content PubMed PubMed Citation Articles by Edelstein, C. Articles by Scanu, A. M. Social Bookmarking                      What's this?

Journal of Lipid Research, Vol. 46, 2673-2680, December 2005
Copyright © 2005 by American Society for Biochemistry and Molecular Biology

Elements in the C terminus of apolipoprotein [a] responsible for the binding to the tenth type III module of human fibronectin

Celina Edelstein^*, Mohammed Yousef and Angelo M. Scanu^1,*,

^* Department of Medicine, University of Chicago, Chicago, IL 60637
Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637

Published, JLR Papers in Press, September 8, 2005. DOI 10.1194/jlr.M500239-JLR200

¹ To whom correspondence should be addressed. e-mail: ascanu{at}medicine.bsd.uchicago.edu

In previous studies, we showed that the C-terminal domain, F2, but not the N-terminal domain, F1, is responsible for the binding of apolipoprotein [a] (apo[a]) to human fibronectin (Fn). To pursue those observations, we prepared, by both elastase digestion and recombinant technology, subsets of F2 of a different length containing either kringle (K) V or the protease domain (PD). We also studied rhesus monkey apo[a], which is known to contain PD but not KV. In the case of Fn, we used both an intact product and its tenth type III module (¹⁰FN-III) expressed in Escherichia coli. The binding studies carried out on microtiter plates showed that the affinity of F2 for immobilized ¹⁰FN-III was 6-fold higher than that for Fn (dissociation constants = 1.75 ± 0.31 nM and 10.25 ± 1.62 nM, respectively). The binding was also exhibited by rhesus apo[a] and by an F2 subset containing the PD linked to an upstream microdomain comprising KIV-8 to KIV-10 and KV, inactive by itself. Competition experiments on microtiter plates showed that both Fn and ¹⁰FN-III, when in solution, are incompetent to bind F2.

Together, our results indicate that F2 binds to immobilized ¹⁰FN-III more efficiently than whole Fn and that the binding can be sustained by truncated forms of F2 that contain the catalytically inactive PD linked to an upstream four K microdomain.

Abbreviations: apo[a], apolipoprotein [a]; EACA, -aminocaproic acid; Fn, fibronectin; ¹⁰FN-III, tenth type III module of fibronectin; K, kringle; K_d, dissociation constant; Lp[a], lipoprotein [a]; PD, protease domain of apolipoprotein [a]

Supplementary key words lipoprotein [a] • kringle V • protease domain • RGD motif

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

This article has been cited by other articles:

				I. Tabas, K. J. Williams, and J. Boren Subendothelial Lipoprotein Retention as the Initiating Process in Atherosclerosis: Update and Therapeutic Implications Circulation, October 16, 2007; 116(16): 1832 - 1844. [Abstract] [Full Text] [PDF]