Can Electronegative LDL Act as a Multienzymatic Complex?
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 indu...
| Autores: | , , , , |
|---|---|
| Tipo de documento: | artigo |
| Data de publicação: | 2023 |
| País: | España |
| Recursos: | Universitat Autònoma de Barcelona |
| Repositório: | Dipòsit Digital de Documents de la UAB |
| Idioma: | inglês |
| OAI Identifier: | oai:ddd.uab.cat:281649 |
| Acesso em linha: | https://ddd.uab.cat/record/281649 https://dx.doi.org/urn:doi:10.3390/ijms24087074 |
| Access Level: | Acceso aberto |
| Palavra-chave: | Low-density lipoprotein Modified LDL Electronegative LDL Platelet-activating factor acetylhydrolase Phospholipase C Sphingomyelinase Ceramidase LDL aggregation Inflammation |
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Can Electronegative LDL Act as a Multienzymatic Complex?Benitez, Sonia|||0000-0003-3565-0743Puig Grifol, Núria|||0000-0002-4699-3162Rives Jimenez, Jose|||0009-0001-5725-9270Solé, Arnau|||0009-0007-6517-6188Sánchez Quesada, José Luis|||0000-0003-0224-591XLow-density lipoproteinModified LDLElectronegative LDLPlatelet-activating factor acetylhydrolasePhospholipase CSphingomyelinaseCeramidaseLDL aggregationInflammationElectronegative 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. 22023-01-0120232023-01-01Articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://ddd.uab.cat/record/281649https://dx.doi.org/urn:doi:10.3390/ijms24087074reponame:Dipòsit Digital de Documents de la UABinstname:Universitat Autònoma de BarcelonaInglésengMinisterio de Economía y Competitividad https://doi.org/10.13039/501100003329 PI13/00364Ministerio de Economía y Competitividad https://doi.org/10.13039/501100003329 PI16/00471Instituto de Salud Carlos III https://doi.org/10.13039/501100004587 PI019/00421Instituto de Salud Carlos III https://doi.org/10.13039/501100004587 PI20/00334Instituto de Salud Carlos III https://doi.org/10.13039/501100004587 FI20/00252Instituto de Salud Carlos III https://doi.org/10.13039/501100004587 CB07/08/0016Instituto de Salud Carlos III https://doi.org/10.13039/501100004587 RD21/0006/0006Agència de Gestió d'Ajuts Universitaris i de Recerca https://doi.org/10.13039/501100003030 2017/SGR-1149open accesshttp://purl.org/coar/access_right/c_abf2Aquest 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.https://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:ddd.uab.cat:2816492026-06-06T12:50:31Z |
| dc.title.none.fl_str_mv |
Can Electronegative LDL Act as a Multienzymatic Complex? |
| title |
Can Electronegative LDL Act as a Multienzymatic Complex? |
| spellingShingle |
Can Electronegative LDL Act as a Multienzymatic Complex? Benitez, Sonia|||0000-0003-3565-0743 Low-density lipoprotein Modified LDL Electronegative LDL Platelet-activating factor acetylhydrolase Phospholipase C Sphingomyelinase Ceramidase LDL aggregation Inflammation |
| title_short |
Can Electronegative LDL Act as a Multienzymatic Complex? |
| title_full |
Can Electronegative LDL Act as a Multienzymatic Complex? |
| title_fullStr |
Can Electronegative LDL Act as a Multienzymatic Complex? |
| title_full_unstemmed |
Can Electronegative LDL Act as a Multienzymatic Complex? |
| title_sort |
Can Electronegative LDL Act as a Multienzymatic Complex? |
| dc.creator.none.fl_str_mv |
Benitez, Sonia|||0000-0003-3565-0743 Puig Grifol, Núria|||0000-0002-4699-3162 Rives Jimenez, Jose|||0009-0001-5725-9270 Solé, Arnau|||0009-0007-6517-6188 Sánchez Quesada, José Luis|||0000-0003-0224-591X |
| author |
Benitez, Sonia|||0000-0003-3565-0743 |
| author_facet |
Benitez, Sonia|||0000-0003-3565-0743 Puig Grifol, Núria|||0000-0002-4699-3162 Rives Jimenez, Jose|||0009-0001-5725-9270 Solé, Arnau|||0009-0007-6517-6188 Sánchez Quesada, José Luis|||0000-0003-0224-591X |
| author_role |
author |
| author2 |
Puig Grifol, Núria|||0000-0002-4699-3162 Rives Jimenez, Jose|||0009-0001-5725-9270 Solé, Arnau|||0009-0007-6517-6188 Sánchez Quesada, José Luis|||0000-0003-0224-591X |
| author2_role |
author author author author |
| dc.subject.none.fl_str_mv |
Low-density lipoprotein Modified LDL Electronegative LDL Platelet-activating factor acetylhydrolase Phospholipase C Sphingomyelinase Ceramidase LDL aggregation Inflammation |
| topic |
Low-density lipoprotein Modified LDL Electronegative LDL Platelet-activating factor acetylhydrolase Phospholipase C Sphingomyelinase Ceramidase LDL aggregation Inflammation |
| description |
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. |
| publishDate |
2023 |
| dc.date.none.fl_str_mv |
2 2023-01-01 2023 2023-01-01 |
| dc.type.none.fl_str_mv |
Article http://purl.org/coar/resource_type/c_6501 VoR http://purl.org/coar/version/c_970fb48d4fbd8a85 |
| dc.type.openaire.fl_str_mv |
info:eu-repo/semantics/article |
| format |
article |
| dc.identifier.none.fl_str_mv |
https://ddd.uab.cat/record/281649 https://dx.doi.org/urn:doi:10.3390/ijms24087074 |
| url |
https://ddd.uab.cat/record/281649 https://dx.doi.org/urn:doi:10.3390/ijms24087074 |
| dc.language.none.fl_str_mv |
Inglés eng |
| language_invalid_str_mv |
Inglés |
| language |
eng |
| dc.relation.none.fl_str_mv |
Ministerio de Economía y Competitividad https://doi.org/10.13039/501100003329 PI13/00364 Ministerio de Economía y Competitividad https://doi.org/10.13039/501100003329 PI16/00471 Instituto de Salud Carlos III https://doi.org/10.13039/501100004587 PI019/00421 Instituto de Salud Carlos III https://doi.org/10.13039/501100004587 PI20/00334 Instituto de Salud Carlos III https://doi.org/10.13039/501100004587 FI20/00252 Instituto de Salud Carlos III https://doi.org/10.13039/501100004587 CB07/08/0016 Instituto de Salud Carlos III https://doi.org/10.13039/501100004587 RD21/0006/0006 Agència de Gestió d'Ajuts Universitaris i de Recerca https://doi.org/10.13039/501100003030 2017/SGR-1149 |
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open access http://purl.org/coar/access_right/c_abf2 https://creativecommons.org/licenses/by/4.0/ |
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info:eu-repo/semantics/openAccess |
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open access http://purl.org/coar/access_right/c_abf2 https://creativecommons.org/licenses/by/4.0/ |
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openAccess |
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application/pdf |
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