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Artikel ; Online: Stable knockout of lanthionine synthase C-like protein-1 (LanCL1) from HeLa cells indicates a role for LanCL1 in redox regulation of deubiquitinating enzymes.

Downey, Aaron / Olcott, Melissa / Spector, Daniel / Bird, Kayla / Ter Doest, Amanda / Pierce, Zachary / Quach, Evan / Sparks, Sawyer / Super, Christa / Naifeh, Jefferey / Powers, Andrea / White, Matthew / Hensley, Kenneth

Free radical biology & medicine

2020  Band 161, Seite(n) 115–124

Abstract: Lanthionine synthase C-like protein-1 (LanCL1) is a glutathione (GSH)-binding protein of uncertain function, widely expressed in mammalian cells. Recent data suggests that LanCL1 has glutathione S-transferase (GST)-like activity, while other reports ... ...

Abstract Lanthionine synthase C-like protein-1 (LanCL1) is a glutathione (GSH)-binding protein of uncertain function, widely expressed in mammalian cells. Recent data suggests that LanCL1 has glutathione S-transferase (GST)-like activity, while other reports claim that LanCL1 suppresses mitogen-activated kinase (MAPK) phosphorylation. In the present study, recombinant human LanCL1 had less than 10% the specific activity of GST. When CRISPR-Cas9 was used to stably ablate LanCL1 from HeLa cells, the resulting line was sensitized to H
Mesh-Begriff(e) Deubiquitinating Enzymes ; HeLa Cells ; Humans ; Hydro-Lyases ; Hydrogen Peroxide ; Multienzyme Complexes ; Oxidation-Reduction ; Receptors, G-Protein-Coupled/metabolism ; Ubiquitin Thiolesterase
Chemische Substanzen LANCL1 protein, human ; Multienzyme Complexes ; Receptors, G-Protein-Coupled ; USP10 protein, human ; USP9X protein, human ; Hydrogen Peroxide (BBX060AN9V) ; Deubiquitinating Enzymes (EC 3.4.19.12) ; Ubiquitin Thiolesterase (EC 3.4.19.12) ; Hydro-Lyases (EC 4.2.1.-) ; lanthionine synthase (EC 4.2.1.-)
Sprache Englisch
Erscheinungsdatum 2020-10-10
Erscheinungsland United States
Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID 807032-5
ISSN 1873-4596 ; 0891-5849
ISSN (online) 1873-4596
ISSN 0891-5849
DOI 10.1016/j.freeradbiomed.2020.10.006
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Zs.A 2109: Hefte anzeigen Standort:
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