Presence of Ceramidase Activity in Electronegative LDL
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Presence of Ceramidase Activity in Electronegative LDL. / Puig, Núria; Rives, Jose; Estruch, Montserrat; Aguilera-Simon, Ana; Rotllan, Noemi; Camacho, Mercedes; Colomé, Núria; Canals, Francesc; Sánchez-Quesada, José Luis; Benitez, Sonia.
I: International Journal of Molecular Sciences, Bind 24, 165, 2023.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Presence of Ceramidase Activity in Electronegative LDL
AU - Puig, Núria
AU - Rives, Jose
AU - Estruch, Montserrat
AU - Aguilera-Simon, Ana
AU - Rotllan, Noemi
AU - Camacho, Mercedes
AU - Colomé, Núria
AU - Canals, Francesc
AU - Sánchez-Quesada, José Luis
AU - Benitez, Sonia
N1 - Publisher Copyright: © 2022 by the authors.
PY - 2023
Y1 - 2023
N2 - 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(−).
AB - 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(−).
KW - ceramidase
KW - ceramide
KW - electronegative LDL
KW - sphingomyelinase
KW - sphingosine
U2 - 10.3390/ijms24010165
DO - 10.3390/ijms24010165
M3 - Journal article
C2 - 36613609
AN - SCOPUS:85145979312
VL - 24
JO - International Journal of Molecular Sciences (Online)
JF - International Journal of Molecular Sciences (Online)
SN - 1661-6596
M1 - 165
ER -
ID: 335963029