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PXD001582-1

PXD001582 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleStudy of reversible oxidation of thiol proteins after hexyl aminolevulinate mediated photodynamic therapy
DescriptionThis proteomic study This proteomic study focuses on the role of reversible thiol oxidation after hexyl aminolevulinate mediated PDT (HAL-PDT). The human epidermoid carcinoma cell line A431 was used as model system and red light as light source, a clinical relevant in vitro model. The light dose dependent cell cytotoxicity was measured by resazurin assay. The most clinical relevant dose, LD100, was used for the proteomic part of the study and cells where harvested 30 min after treatment. The reversibly oxidized thiol proteins were selected by biotinylation and identified by mass spectrometry. This proteomic technique revealed over 1100 thiol proteins which were reversibly oxidized after HAL-PDT. Identified proteins were analysed by bioinformatics (IPA and GO) and a list of reliable identified proteins (282 proteins) where further analysed. Both the cellular location and function was determined for these proteins. In addition, 18 of the proteins where identified as redox regulated, 36 to be a part of the apoptotic pathway and 9 to be both redox regulated and a part of apoptotic pathway. From these results we suggest redox regulated proteins as a trigger mechanism for PDT induced apoptosis.focuses on the role of reversible thiol oxidation after hexyl aminolevulinate mediated PDT (HAL-PDT). The human epidermoid carcinoma cell line A431 was used as model system and red light as light source, a clinical relevant in vitro model. The light dose dependent cell cytotoxicity was measured by resazurin assay. The most clinical relevant dose, LD100, was used for the proteomic part of the study and cells where harvested 30 min after treatment. The reversibly oxidized thiol proteins were selected by biotinylation and identified by mass spectrometry. This proteomic technique revealed over 1100 thiol proteins which were reversibly oxidized after HAL-PDT. Identified proteins were analysed by bioinformatics (IPA and GO) and a list of reliable identified proteins (282 proteins) where further analysed. Both the cellular location and function was determined for these proteins. In addition, 18 of the proteins where identified as redox regulated, 36 to be a part of the apoptotic pathway and 9 to be both redox regulated and a part of apoptotic pathway. From these results we suggest redox regulated proteins as a trigger mechanism for PDT induced apoptosis.
HostingRepositoryPRIDE
AnnounceDate2016-01-12
AnnouncementXMLSubmission_2016-01-12_06:13:18.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterAnimesh Sharma
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListN-ethylmaleimide derivatized cysteine
InstrumentQ Exactive
Dataset History
RevisionDatetimeStatusChangeLog Entry
02014-12-08 02:30:38ID requested
12016-01-12 06:13:19announced
22024-10-22 04:21:58announced2024-10-22: Updated project metadata.
Publication List
Helander L, Sharma A, Krokan HE, Plaetzer K, Krammer B, Tortik N, Gederaas OA, Slupphaug G, Hagen L, Photodynamic treatment with hexyl-aminolevulinate mediates reversible thiol oxidation in core oxidative stress signaling proteins. Mol Biosyst, 12(3):796-805(2016) [pubmed]
Keyword List
curator keyword: Biomedical, Biological
submitter keyword: photodynamic therapy, reversible protein oxidation, reactive oxygen species, apoptosis, proteomic, redox signalling
Contact List
Geir Slupphaug
contact affiliationDepartment of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology, Trondheim, Norway.
contact emailgeir.slupphaug@ntnu.no
lab head
Animesh Sharma
contact affiliationEngineer at NTNU, Norway
contact emailsharma.animesh@gmail.com
dataset submitter
Full Dataset Link List
Dataset FTP location
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