J. Lipid Res. Neurobiology of Lipids (ISSN1683-5506)
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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
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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.


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