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Chemical inhibition of the target of rapamycin kinase in Chlamydomonas reinhardtii leads to rapid cysteine oxidation and sustained physiological changes.

ABSTRACT: The target of rapamycin (TOR) kinase is a key metabolic regulator with a role in diverse processes, including nutritional sensing, protein translation, and autophagy. In the green alga Chlamydomonas reinhardtii, TOR maintains these responsibilities and is additionally linked to the regulation of increased triacylglycerol accumulation. In this study, we used an ATP-competitive inhibitor (AZD8055) to inactivate TOR kinase in vivo and quantified any accompanying changes in global protein abundance and reversible cysteine oxidation.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Chlamydomonas Reinhardtii

TISSUE(S): Photosynthetic Cell

SUBMITTER: Evan McConnell

LAB HEAD: Leslie M. Hicks

PROVIDER: PXD014819 | Pride | 2019-10-04

REPOSITORIES: Pride

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			Action	DRS
	20190123_EWM_AZD1_R0_1_2h_5-35_5uL.wiff	Wiff
	20190123_EWM_AZD1_R0_1_2h_5-35_5uL.wiff.scan	Wiff
	20190123_EWM_AZD1_R0_2_2h_5-35_5uL.wiff	Wiff
	20190123_EWM_AZD1_R0_2_2h_5-35_5uL.wiff.scan	Wiff
	20190123_EWM_AZD1_R0_3_2h_5-35_5uL.wiff	Wiff

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Project 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.

Dataset Information

Chemical inhibition of the target of rapamycin kinase in Chlamydomonas reinhardtii leads to rapid cysteine oxidation and sustained physiological changes.

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