Presence of Ceramidase Activity in Electronegative LDL

Electronegative low-density lipoprotein (LDL(-)) is a minor modified fraction of human plasma LDL with several atherogenic properties. Among them is increased bioactive lipid mediator content, such as lysophosphatidylcholine (LPC), non-esterified fatty acids (NEFA), ceramide (Cer), and sphingosine (...

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Detalhes bibliográficos
Autores: Puig Calvó, Núria|||0000-0001-8235-4934, Rives Jimenez, Jose|||0009-0001-5725-9270, Estruch, Montserrat|||0000-0002-7162-4158, Aguilera-Simón, Ana|||0000-0003-1428-8212, Rotllan, Noemi|||0000-0002-0587-8045, Camacho, Mercedes|||0000-0001-5970-3294, Colomé, Núria, Canals, Francesc|||0000-0002-0650-1135, Sánchez Quesada, José Luis|||0000-0003-0224-591X, Benitez, Sonia|||0000-0003-3565-0743
Formato: artículo
Fecha de publicación:2022
País:España
Recursos:Universitat Autònoma de Barcelona
Repositorio:Dipòsit Digital de Documents de la UAB
Idioma:inglés
OAI Identifier:oai:ddd.uab.cat:280926
Acesso em linha:https://ddd.uab.cat/record/280926
https://dx.doi.org/urn:doi:10.3390/ijms24010165
Access Level:acceso abierto
Palavra-chave:Ceramidase
Ceramide
Electronegative LDL
Sphingomyelinase
Sphingosine
Descrição
Resumo:Electronegative low-density lipoprotein (LDL(-)) is a minor modified fraction of human plasma LDL with several atherogenic properties. Among them is increased bioactive lipid mediator content, such as lysophosphatidylcholine (LPC), non-esterified fatty acids (NEFA), ceramide (Cer), and sphingosine (Sph), which are related to the presence of some phospholipolytic activities, including platelet-activating factor acetylhydrolase (PAF-AH), phospholipase C (PLC), and sphingomyelinase (SMase), in LDL(-). However, these enzymes' activities do not explain the increased Sph content, which typically derives from Cer degradation. In the present study, we analyzed the putative presence of ceramidase (CDase) activity, which could explain the increased Sph content. Thin layer chromatography (TLC) and lipidomic analysis showed that Cer, Sph, and NEFA spontaneously increased in LDL(-) incubated alone at 37 °C, in contrast with native LDL(+). An inhibitor of neutral CDase prevented the formation of Sph and, in turn, increased Cer content in LDL(-). In addition, LDL(-) efficiently degraded fluorescently labeled Cer (NBD-Cer) to form Sph and NEFA. These observations defend the existence of the CDase-like activity's association with LDL(-). However, neither the proteomic analysis nor the Western blot detected the presence of an enzyme with known CDase activity. Further studies are thus warranted to define the origin of the CDase-like activity detected in LDL(-).

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