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Title-nitrosoglutathione reductase as a therapeutic target for diabetic vascular complications in rodent models.
Journal, issue, pagesSci Transl Med, Vol. 17, Issue 818, Page eadn9216, Year 2025
Publish dateOct 1, 2025
AuthorsShuang Zhao / Tianyu Song / Xin Tang / Chenglin Fan / Yuhao Yang / Zhiren Zhang / Ying Xia / Yan Zhang / Jiawei Cao / Ziyu Wang / Zhiguang Shi / Xinlong Tang / Dongjin Wang / Guoyong Yin / Shaohua Zhang / Yuanqing Gao / Hongshan Chen / Liansheng Wang / Feng Chen / Hong Wang / Bo Yu / Yu Cao / Kangyun Sun / Xin Liu / Xiujie Wang / Chenghui Yan / Yaling Han / Yi Han / Liping Xie / Yong Ji /
PubMed AbstractEndothelial dysfunction is one of the earliest processes in diabetes and a major contributor to diabetic vascular complications, which often exhibit limited response to glucose-lowering therapies. We ...Endothelial dysfunction is one of the earliest processes in diabetes and a major contributor to diabetic vascular complications, which often exhibit limited response to glucose-lowering therapies. We identified up-regulated -nitrosoglutathione reductase (GSNOR) as a critical factor associated with diabetic vascular complications by unbiased proteomics. Elevated GSNOR expression was observed in the endothelium of patients with type 2 diabetes and in streptozotocin (STZ)-induced type 1 diabetes mice as well as in type 2 diabetes mouse models. Genetic ablation of endothelial promoted angiogenesis, maintained vascular permeability, and improved vasodilation in type 1 diabetes mice induced by STZ. GSNOR deficiency protected against high glucose-induced endothelial dysfunction in vitro, as evidenced by rescued tube formation, enhanced spheroid sprouting, maintained barrier integrity, and reduced permeability. Mechanistically, GSNOR orchestrated endothelial dysfunction independently of its enzymatic activity by binding the transcription factor ETS-related gene (ERG) and triggered its nuclear export through chromosome region maintenance 1. We synthesized NYY-001, an oral agent, that selectively blocks the GSNOR-ERG interaction. The direct targeting of NYY-001 to GSNOR was determined by resolving the crystal structure of their complex using cryo-electron microscopy. NYY-001 treatment enhanced postischemic neovascularization and restored vascular permeability in the peripheral vasculature in STZ-induced type 1 diabetes and type 2 diabetes mouse models. These findings reveal a mechanistic role for the GSNOR-ERG complex in diabetic vascular complications and highlight NYY-001 as a promising therapeutic candidate.
External linksSci Transl Med / PubMed:41032622
MethodsEM (single particle)
Resolution3.05 Å
Structure data

34282

8gv3

EMDB-34282, PDB-8gv3:
The cryo-EM structure of GSNOR with NYY001
Method: EM (single particle) / Resolution: 3.05 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-WKZ:
(4P)-4-{2-[4-(1H-imidazol-1-yl)phenyl]-5-[3-oxo-3-(2-oxo-1,3-thiazolidin-3-yl)propyl]-1H-pyrrol-1-yl}-3-methylbenzamide

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / Alcohol dehydrogenase class-3

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