PXD036168 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Presence of ceramidase activity in electronegative LDL |
Description | Electronegative LDL (LDL(-)) is a minor modified fraction of human plasma LDL with several atherogenic properties. Among them, LDL(-) has increased content of bioactive lipid mediators, such as lysophosphatidylcholine (LPC), non-esterified fatty acids (NEFA), ceramide (Cer), and sphingosine (Sph), which are related to the presence in LDL(-) of some phospholipolytic activities, including platelet-activating factor acetylhydrolase (PAF-AH), phospholipase C (PLC) and sphingomyelinase (SMase). However, the activity of these enzymes does not explain the increased content of Sph, which should derive from Cer degradation. In the present study we analyzed the putative presence of a ceramidase (CDase) activity that could explain the increased content of Sph. Thin layer chromatography (TLC) and lipidomic analysis showed that Cer, Sph and NEFA spon-taneously increased in LDL(-) incubated alone at 37ºC, in contrast with native LDL(+). An inhibitor of neutral CDase prevented the formation of Sph and, in contrast, increased the content of Cer in LDL(-). In addition, a fluorescently-labelled Cer (NBD-Cer) was efficiently degraded by LDL(-) to form Sph and NEFA. These observations point to the existence of a CDase activity associated to LDL(-). However, neither proteomic analysis nor western blot detected the presence of a known CDase enzyme. Further studies are warranted to define the origin of the CDase activity detected in LDL(-). |
HostingRepository | PRIDE |
AnnounceDate | 2023-11-14 |
AnnouncementXML | Submission_2023-11-14_07:53:35.655.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Francesc Canals |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | Bruker Daltonics instrument model |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2022-08-19 01:29:48 | ID requested | |
1 | 2023-01-09 07:37:34 | announced | |
⏵ 2 | 2023-11-14 07:53:36 | announced | 2023-11-14: Updated project metadata. |
Publication List
Puig N, Rives J, Estruch M, Aguilera-Simon A, Rotllan N, Camacho M, Colom, é N, Canals F, S, á, nchez-Quesada JL, Benitez S, Presence of Ceramidase Activity in Electronegative LDL. Int J Mol Sci, 24(1):(2022) [pubmed] |
Keyword List
submitter keyword: electronegative LDL |
ceramide |
sphingosine |
ceramidase |
sphingomyelinase |
Contact List
José Luis Sánchez-Quesada |
contact affiliation | Cardiovascular Biochemistry Group, Research Institute of the Hospital de la Santa Creu i Sant Pau (IIB Sant Pau), Barcelona, Spain |
contact email | jsanchezq@santpau.cat |
lab head | |
Francesc Canals |
contact affiliation | Vall Hebron Institute of Oncology |
contact email | fcanals@vhio.net |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD036168
- Label: PRIDE project
- Name: Presence of ceramidase activity in electronegative LDL