Dataset Information

LC-MS/MS for harmaline-treated mice cerebellar cortex

ABSTRACT: Harmaline-induced tremor mice model has been well-recognized as a mature pharmacological model for ET, but his model has always been used to test drugs, the exact underlying mechanism of this mouse model has never been fully understood. This project is to provide a novel inspection for ET targeted treatment by revealing the protein signals for harmaline-induced mice model.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Brain

SUBMITTER: Yiwen Wu

LAB HEAD: Yiwen Wu

PROVIDER: PXD055985 | Pride | 2026-01-05

REPOSITORIES: Pride

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Publications

Transcriptomics and Proteomics Identify Serotonin Transporter as a Promising Therapeutic Target for Essential Tremor.

Wang Lingbing L Zhou Zhuofan Z Lin Suzhen S Li Yanjing Y Zhang Shaoyi S Xu Tian-Le TL Song Xing-Lei XL Wu Yiwen Y

Molecular & cellular proteomics : MCP 20251104 12

Essential tremor (ET) stands as one of the most prevalent movement disorders originating from cerebellar dysfunction. However, effective treatment remains limited, largely due to a poor understanding of its molecular pathology. The harmaline-induced tremor in mice is a well-established model for ET research, though its mechanisms remain unclear. This study aimed to get insight into the molecular intricacies underlying cerebellar dysfunction in this model. Combining LC-MS/MS and RNA-Seq approach, ...[more]

PMID: 41192557

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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.

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