PXD029480-1

PXD029480 is an original dataset announced via ProteomeXchange.

Title	Site-specific protein modification by 3-n-butylphthalide in primary hepatocytes: covalent protein adducts diminished by glutathione and N-acetylcysteine
Description	The toxicity of NBP and its four major metabolites were compared in both PHHs and PRHs, and 3-OH-NBP was found to be the most toxic metabolite. 3-OH-NBP induced remarkable cell death and oxidative stresses in hepatocytes, which correlated well with the levels of glutathione and N-acetylcysteine adducts (3-GSH-NBP and 3-NAC-NBP) in cell supernatants. Additionally, 3-OH-NBP covalently conjugated with intracellular Cys, Lys and Ser, with preferable binding to Cys sites at Myh9 Cys1380, Prdx4 Cys53, Vdac2 Cys48 and Vdac3 Cys36. Furthermore, we found that CYP3A4 induction by rifampicin augmented NBP-induced cell toxicity and supplementing with GSH or NAC alleviated the oxidative stresses and reactive metabolites caused by 3-OH-NBP.
HostingRepository	PRIDE
AnnounceDate	2022-10-22
AnnouncementXML	Submission_2022-10-21_17:31:15.189.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	HeHuang
SpeciesList	scientific name: Rattus norvegicus (Rat); NCBI TaxID: 10116;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive HF-X

Revision	Datetime	Status	ChangeLog Entry
0	2021-11-01 08:53:24	ID requested
⏵ 1	2022-10-21 17:31:15	announced

Dataset with its publication pending

submitter keyword: 3-n-butylphthalide

Hepatotoxicity

oxidative stresses

covalent protein modification

Drug-drug interaction

HeHuang
contact affiliation	Shanghai Institute of Materia Medica
contact email	hhuang@simm.ac.cn
lab head
HeHuang
contact affiliation	Shanghai Institute of Materia Medica
contact email	hhuang.nu@gmail.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD029480
     1. Label: PRIDE project
     2. Name: Site-specific protein modification by 3-n-butylphthalide in primary hepatocytes: covalent protein adducts diminished by glutathione and N-acetylcysteine