Can Electronegative LDL Act as a Multienzymatic Complex?
Benitez, Sonia (Institut d'Investigació Biomèdica Sant Pau)
Puig Grifol, Núria (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Rives Jimenez, Jose (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Solé, Arnau (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Sánchez Quesada, José Luis (Instituto de Salud Carlos III)

Data:	2023
Resum:	Electronegative LDL (LDL(-)) is a minor form of LDL present in blood for which proportions are increased in pathologies with increased cardiovascular risk. In vitro studies have shown that LDL(-) presents pro-atherogenic properties, including a high susceptibility to aggregation, the ability to induce inflammation and apoptosis, and increased binding to arterial proteoglycans; however, it also shows some anti-atherogenic properties, which suggest a role in controlling the atherosclerotic process. One of the distinctive features of LDL(-) is that it has enzymatic activities with the ability to degrade different lipids. For example, LDL(-) transports platelet-activating factor acetylhydrolase (PAF-AH), which degrades oxidized phospholipids. In addition, two other enzymatic activities are exhibited by LDL(-). The first is type C phospholipase activity, which degrades both lysophosphatidylcholine (LysoPLC-like activity) and sphingomyelin (SMase-like activity). The second is ceramidase activity (CDase-like). Based on the complementarity of the products and substrates of these different activities, this review speculates on the possibility that LDL(-) may act as a sort of multienzymatic complex in which these enzymatic activities exert a concerted action. We hypothesize that LysoPLC/SMase and CDase activities could be generated by conformational changes in apoB-100 and that both activities occur in proximity to PAF-AH, making it feasible to discern a coordinated action among them.
Ajuts:	Ministerio de Economía y Competitividad PI13/00364 Ministerio de Economía y Competitividad PI16/00471 Instituto de Salud Carlos III PI019/00421 Instituto de Salud Carlos III PI20/00334 Instituto de Salud Carlos III FI20/00252 Instituto de Salud Carlos III CB07/08/0016 Instituto de Salud Carlos III RD21/0006/0006 Agència de Gestió d'Ajuts Universitaris i de Recerca 2017/SGR-1149
Drets:	Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original.
Llengua:	Anglès
Document:	Article ; recerca ; Versió publicada
Matèria:	Low-density lipoprotein ; Modified LDL ; Electronegative LDL ; Platelet-activating factor acetylhydrolase ; Phospholipase C ; Sphingomyelinase ; Ceramidase ; LDL aggregation ; Inflammation
Publicat a:	International journal of molecular sciences, Vol. 24, Num. 8 (April 2023) , art. 7074, ISSN 1422-0067

DOI: 10.3390/ijms24087074
PMID: 37108253

15 p, 764.0 KB

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