J. Lipid Res. Did you know there is a large type edition? Click here.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on December 1, 2005

Papers In Press, published online ahead of print September 8, 2005
J. Lipid Res., doi:10.1194/jlr.M500239-JLR200
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
M500239-JLR200v1
46/12/2673    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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 Edelstein, C.
Right arrow Articles by Scanu, A. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Edelstein, C.
Right arrow Articles by Scanu, A. M.
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?

Submitted on June 10, 2005
Revised on August 18, 2005
Accepted on August 31, 2005

Elements in the C-terminal of apolipoprotein(a) responsible for the binding to the tenth type III module of human fibronectin

Celina Edelstein, Mohammed Yousef, and Angelo M. Scanu

Department of Medicine, University of Chicago, Chicago, IL 60637

Corresponding Author: ascanu{at}medicine.bsd.uchicago.edu

In previous studies we showed that the C-terminal domain, F2, but not the N-terminal, F1, is responsible for the binding of apolipoprotein(a), (apo(a)), to human fibronectin (Fn). In order to pursue of 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) known to contain PD but not KV. In the case of Fn, we utilized both an intact product and its tenth type III module, (10FN-III), expressed in E.Coli. The binding studies carried out in microtiter plates showed that the affinity of F2 for immobilized 10FN-III was about 6-fold higher than that for Fn (Kd, 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 -10 and KV, inactive by itself. Competition experiments in 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 kringle-microdomain.


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
 CirculationHome page
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]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Journal of Biological Chemistry 
 Molecular and Cellular Proteomics   ASBMB Today 
Copyright © 2005 by the American Society for Biochemistry and Molecular Biology.