Sulfur-containing histidine compounds inhibit γ-glutamyl transpeptidase activity in human cancer cells.
Autophagy
/ drug effects
Cell Line, Tumor
Cell Proliferation
/ drug effects
Gene Expression Regulation, Neoplastic
/ drug effects
Glutathione
/ genetics
Histidine
/ genetics
Humans
Leukemia, Lymphocytic, Chronic, B-Cell
/ drug therapy
Liver Neoplasms
/ drug therapy
Methylhistidines
/ pharmacology
Oxidation-Reduction
Proteolysis
Substrate Specificity
Sulfur Compounds
/ pharmacology
gamma-Glutamyltransferase
/ antagonists & inhibitors
GGT-positive cells
apoptosis
autophagy
enzyme inhibitor
enzyme kinetics
ergothioneine
glutamyl transpeptidase
marine drugs
ovothiol
thiol
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
04 10 2019
04 10 2019
Historique:
received:
10
05
2019
revised:
04
07
2019
pubmed:
4
8
2019
medline:
7
5
2020
entrez:
4
8
2019
Statut:
ppublish
Résumé
γ-Glutamyl transpeptidase (GGT) is an enzyme located on the surface of cellular membranes and involved in GSH metabolism and maintenance of redox homeostasis. High GGT expression on tumor cells is associated with increased cell proliferation and resistance against chemotherapy. GGT inhibitors evaluated so far in clinical trials are too toxic for human use. In this study, using enzyme kinetics analyses, we demonstrate that ovothiols, 5(
Identifiants
pubmed: 31375562
pii: S0021-9258(20)35013-4
doi: 10.1074/jbc.RA119.009304
pmc: PMC6779435
doi:
Substances chimiques
Methylhistidines
0
Sulfur Compounds
0
ovothiol C
105496-34-2
Histidine
4QD397987E
gamma-Glutamyltransferase
EC 2.3.2.2
gamma-glutamyltransferase, human
EC 2.3.2.2
Glutathione
GAN16C9B8O
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
14603-14614Informations de copyright
© 2019 Brancaccio et al.
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