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(Circulation. 2003;108:92.)
© 2003 American Heart Association, Inc.

Basic Science Reports

Platelet-Activating Factor Acetylhydrolase Is Mainly Associated With Electronegative Low-Density Lipoprotein Subfraction

Sonia Benítez, PhD^*; José Luis Sánchez-Quesada, PhD^*; Vicent Ribas, BSc; Oscar Jorba, BSc; Francisco Blanco-Vaca, MD, PhD; Francesc González-Sastre, MD, PhD; Jordi Ordóñez-Llanos, MD, PhD

From the Servei de Bioquímica and Institut de Recerca (S.B., J.L.S.-Q., V.R., O.J., F.B.-V., F.G.-S., J.O.-L.), Hospital de la Santa Creu i Sant Pau, and Departament de Bioquímica i Biología Molecular (F.G.-S., J.O.-L.), Universitat Autònoma de Barcelona, Barcelona, Spain.

Correspondence to Dr Jordi Ordóñez-Llanos, Servei de Bioquímica, Hospital de la Santa Creu i Sant Pau, C/Antoni María Claret 167, 08025 Barcelona, Spain. E-mail jordonez{at}hsp.santpau.es

Background— Electronegative LDL [LDL(-)], a modified subfraction of LDL present in plasma, induces the release of interleukin-8 and monocyte chemotactic protein-1 from cultured endothelial cells.

Methods and Results— We demonstrate that platelet-activating factor acetylhydrolase (PAF-AH) is mainly associated with LDL(-). LDL(-) had 5-fold higher PAF-AH activity than the nonelectronegative LDL subfraction [LDL(+)] in both normolipemic and familial hypercholesterolemic subjects. Western blot analysis after SDS-PAGE confirmed these results, because a single band of 44 kDa corresponding to PAF-AH appeared in LDL(-) but not in LDL(+). Nondenaturing polyacrylamide gradient gel electrophoresis demonstrated that PAF-AH was bound to LDL(-) regardless of LDL size. In accordance with the above findings, nonesterified fatty acids, a cleavage product of PAF-AH, were increased in LDL(-) compared with LDL(+).

Conclusions— The high PAF-AH activity observed in LDL(-) could be related to the proinflammatory activity of these lipoproteins toward cultured endothelial cells.

Key Words: lipoproteins • inflammation • fatty acids

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