PXD001582

PXD001582 is an original dataset announced via ProteomeXchange.

Title	Study of reversible oxidation of thiol proteins after hexyl aminolevulinate mediated photodynamic therapy
Description	This 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.
HostingRepository	PRIDE
AnnounceDate	2016-01-12
AnnouncementXML	Submission_2016-01-12_06:13:18.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Animesh Sharma
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	N-ethylmaleimide derivatized cysteine
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2014-12-08 02:30:38	ID requested
⏵ 1	2016-01-12 06:13:19	announced

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]

curator keyword: Biomedical, Biological

submitter keyword: photodynamic therapy, reversible protein oxidation, reactive oxygen species, apoptosis, proteomic, redox signalling

Geir Slupphaug
contact affiliation	Department of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology, Trondheim, Norway.
contact email	geir.slupphaug@ntnu.no
lab head
Animesh Sharma
contact affiliation	Engineer at NTNU, Norway
contact email	sharma.animesh@gmail.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD001582
     1. Label: PRIDE project
     2. Name: Study of reversible oxidation of thiol proteins after hexyl aminolevulinate mediated photodynamic therapy