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Can Electronegative LDL Act as a Multienzymatic Complex?

Sonia Benitez1,2, Núria Puig1,3, José Rives1,3

  • 1Cardiovascular Biochemistry Group, Research Institute of the Hospital de la Santa Creu i Sant Pau (IIB Sant Pau), 08041 Barcelona, Spain.

International Journal of Molecular Sciences
|April 28, 2023
PubMed
Summary

Electronegative LDL (LDL(-)) has unique enzymatic activities that may act as a multienzyme complex. This complex may play a role in controlling atherosclerosis by degrading lipids and influencing cardiovascular risk.

Keywords:
LDL aggregationceramidaseelectronegative LDLinflammationlow-density lipoproteinmodified LDLphospholipase Cplatelet-activating factor acetylhydrolasesphingomyelinase

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Area of Science:

  • Biochemistry
  • Cardiovascular Research
  • Lipid Metabolism

Background:

  • Electronegative LDL (LDL(-)) is a minor LDL subfraction elevated in conditions associated with increased cardiovascular risk.
  • LDL(-) exhibits pro-atherogenic properties (aggregation, inflammation, apoptosis, proteoglycan binding) but also potential anti-atherogenic roles.
  • A key characteristic of LDL(-) is its intrinsic enzymatic activities, including the degradation of lipids.

Purpose of the Study:

  • To explore the enzymatic activities of LDL(-), specifically platelet-activating factor acetylhydrolase (PAF-AH), type C phospholipase (LysoPLC/SMase-like), and ceramidase (CDase-like).
  • To hypothesize that these activities might function as a coordinated multienzymatic complex.
  • To investigate the potential role of LDL(-) in modulating the atherosclerotic process through its enzymatic functions.

Main Methods:

  • Review of in vitro studies on LDL(-) properties and enzymatic activities.
  • Analysis of substrate and product complementarity for identified enzymatic activities.
  • Speculative modeling of LDL(-) as a multienzymatic complex.

Main Results:

  • LDL(-) possesses PAF-AH activity, degrading oxidized phospholipids.
  • LDL(-) exhibits type C phospholipase (LysoPLC/SMase-like) and ceramidase (CDase-like) activities.
  • The products and substrates suggest a potential concerted action among these enzymes.

Conclusions:

  • LDL(-) may function as a multienzymatic complex with coordinated enzymatic actions.
  • Conformational changes in apoB-100 are hypothesized to generate LysoPLC/SMase and CDase activities.
  • The proximity of these activities to PAF-AH supports the concept of coordinated lipid degradation and potential modulation of atherosclerosis.