Dataset Information

Protein S-nitrosylation in lung endothelial cells from mouse

ABSTRACT: Long.term consequences of loss of arginase-1 (Arg1) in red blood cells were analysed by redox-proteomics. We enriched S-Nitrosylated proteins to study nitrosylated proteins in red-bood cells using a BIAM-switch assay.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Lung

SUBMITTER: Ilka Wittig

LAB HEAD: Prof. Dr. med. Katrin Schäfer

PROVIDER: PXD075167 | Pride | 2026-06-08

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	Data_analysis.xlsx	Xlsx
	EndothelialCells.zip	Other
	P23_030_Rajini_Erythrocytes_Sample01_B.raw	Raw
	P23_030_Rajini_Erythrocytes_Sample01_C.raw	Raw
	P23_030_Rajini_Erythrocytes_Sample01_D.raw	Raw

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Publications

Loss of erythrocyte arginase-1 impairs vasorelaxation due to endothelial GSNOR overexpression and denitrosylation of G protein subunits.

Gogiraju Rajinikanth R Sun Beichen B Bochenek Magdalena L ML Wittig Ilka I Rezende Flávia F Lopez Melina M Wirth Angela A Zhao Wenjia W Böhm Elsa W EW Guliani Payal P Moiko Kateryna K Molitor Michael M Wenzel Philip P Freichel Marc M Lurz Philipp P Brandes Ralf P RP Schäfer Katrin K

Redox biology 20260504

<h4>Introduction</h4>Overexpression of arginase-1 (ARG1) in red blood cells (RBCs) is associated with endothelial dysfunction, and short-term ARG1 inhibition or l-arginine supplementation restored endothelial function. However, the long-term consequences of ARG1 loss in RBCs and its effects on endothelial cells (ECs) are largely unknown. Here, we determined how deletion of ARG1 in RBCs affects blood pressure and vasorelaxation and the role of endothelial NO signaling via the soluble guanylyl cyc ...[more]

PMID: 42085863

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Project description:Trypomastigotes from Trypanosoma cruzi adhere to the extracellular matrix (ECM) in order to invade mammalian host cells. Incubation of trypomastigotes with ECM leads to a decrease of nitric oxide synthase (NOS) activity and associated post-translational modifications (PTMs). Herein, resin-assisted enrichment of thiols combined with mass spectrometry were employed to map site-specific S-nitrosylated (SNO) proteins from T. cruzi trypomastigotes incubated (MTy) or not (Ty) with ECM. We confirmed the reduction of S-nitrosylation upon incubation with ECM, associated to a rewiring of the subcellular distribution and intracellular signaling pathways of the SNO proteins between MTy and Ty conditions. Forty (~10.7%) and 248 (~66.4%) SNO-peptides were uniquely identified in MTy and Ty, respectively, in addition to 85 peptides (~22.7%) quantified in both conditions. S-nitrosylated proteins were enriched in a wide range of cellular components, including surface membranes and vesicles, and are involved in ribosome, transport, carbohydrate and lipid metabolisms. Of note, we described for the first time nytrosylation of histones H2B and H3 on Cys64 and Cys126, respectively, which is was more abundant in MTy. Additionally, sequence alignment shows that H3 (Cys126) histone is also present in T.b.brucei, but not in L. major, while H2B (Cys64) is absent in both parasites and other higher eukaryotes. Protein-protein interaction networks analyzed by STRING revealed ribosomal proteins, proteins involved in carbon and fatty acid metabolism to be among the enriched protein complexes. Among the SNO ribosomal proteins, 90% were identified and quantified uniquely or upregulated in the Ty fraction. Enzymes involved in oxidoreductase, kinases and phosphatases were identified as nitrosylated and phosphorylated in the same conditions suggesting a crosstalk between these modifications linked to regulation of energy metabolism of T. cruzi in the presence of ECM. Although enzymatic activity of NOS was described in T. cruzi, its identification is elusive. In silico mapping of putative nitric oxide synthase (NOS) gene(s) based on domain architecture identified four putative T. cruzi proteins expressing a putative C-terminal NOS domain: two putative P450 reductases, a putative FMN/FAD containing oxidoreductase and a putative oxidoreductase-protein. Our results provide the first site-specific characterization of S-nitrosylated proteins in T. cruzi linked to the roles of NO in reprogramming parasite cells to invade mammalian hosts.