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J. Lipid Res.
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Originally published In Press as doi:10.1194/jlr.M800318-JLR200 on October 24, 2008

Papers In Press, published online ahead of print March 1, 2009
J. Lipid Res., doi:10.1194/jlr.M800318-JLR200
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Journal of Lipid Research, Vol. 50, 446-455, March 2009
Copyright © 2009 by American Society for Biochemistry and Molecular Biology

High binding affinity of electronegative LDL to human aortic proteoglycans depends on its aggregation levelboxs

Cristina Bancells*,{dagger}, Sònia Benítez*, Matti Jauhiainen§, Jordi Ordóñez-Llanos*,{dagger}, Petri T. Kovanen**, Sandra Villegas{dagger}, José Luis Sánchez-Quesada1,* and Katariina Öörni**

* Servei de Bioquímica, Institut de Recerca, Hospital de la Santa Creu i Sant Pau, C/ Antoni Maria Claret 167, 08025 Barcelona, Spain
{dagger} Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193 Bellaterra, Spain
§ National Public Health Institute and FIMM, Institute for Molecular Medicine Finland, Biomedicum, Haartmaninkatu 8, 00290 Helsinki, Finland
** Wihuri Research Institute, Kalliolinnantie 4, 00140 Helsinki, Finland

boxs The online version of this article (available at http://www.jlr.org) contains supplementary data in the form of one table and one figure.

This work was supported by Grants PI030885, PI060500, PI070148, and RD060015 from the Ministerio de Sanidad/Instituto de Salud Carlos III/FIS. S.B. and J.L.S-Q. are recipients of personal grants CP040110 and CP060220 from Fondo de Investigación Sanitaria (FIS). C.B. is the recipient of personal grant AP2004-1468 from the Ministerio de Educación y Ciencia.

Published, JLR Papers in Press, October 24, 2008.

1 To whom correspondence should be addressed. e-mail: jsanchezq{at}santpau.cat

Electronegative LDL [LDL(–)] is an atherogenic subfraction of plasma LDL that has increased apolipoprotein E (apoE) and apoC-III content, high density, and increased susceptibility to aggregation. These characteristics suggest that LDL(–) could bind to proteoglycans (PGs); therefore, our aim was to evaluate its affinity to PGs. Binding of LDL(–) and native LDL [LDL(+)] to human aortic PGs was determined by precipitation of LDL-glycosaminoglycan complexes, LDL incubation in PG-coated microtiter wells, and affinity chromatography on PG column. All methods showed that LDL(–) had higher binding affinity to PGs than did LDL(+). PG capacity to bind LDL(–) was increased approximately 4-fold compared with LDL(+) in precipitation and microtiter assays. Chromatography on PG column showed LDL(–) to consist of two subpopulations, one with higher and one with lower PG binding affinity than LDL(+). Unexpectedly, the lower PG affinity subpopulation had increased apoE and apoC-III content. In contrast, the high PG affinity subpopulation presented phospholipase C (PLC)-like activity and increased aggregation. These results suggest that PLC-like activity could alter LDL lipid composition, thereby promoting particle aggregation and binding to PGs. This propensity of a subpopulation of LDL(–) to bind to PGs could facilitate its retention in the extracellular matrix of arterial intima and contribute to atherosclerosis progression.

Supplementary key words glycosaminoglycans • lipoprotein aggregation • sphingomyelinase • phospholipase C

Abbreviations: apoE, apolipoprotein E; GAG, glycosaminoglycan; GGE, native polyacrylamide gradient gel electrophoresis; LDL(–), electronegative LDL; LDL(+), native LDL; lysoPLC, lysophospholipase C; PAF-AH, platelet-activating factor acetylhydrolase; PG, proteoglycan; PLC, phospholipase C; sPLA2, secretory phospholipase A2


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