Dataset Information

Syntaxin 4 (STX4) protects islet -cells from cytokine-induced senescence

ABSTRACT: Syntaxin 4 (STX4) is a plasma membrane SNARE protein known to facilitate insulin granule exocytosis in pancreatic β-cells. Recent studies have uncovered that STX4 also exerts protective effects against inflammatory and metabolic stress by stabilizing mitochondrial function and suppressing NF-κB activation. In this project, we investigated the role of β-cell STX4 in modulating the secretome and paracrine signaling under pro-inflammatory conditions associated with β-cell senescence and type 1 diabetes.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Pancreatic Islet Cell

DISEASE(S): Type 1 Diabetes Mellitus

SUBMITTER: Nathaniel Hansen

LAB HEAD: Dr Patrick Pirrotte

PROVIDER: PXD069706 | Pride | 2026-02-25

REPOSITORIES: Pride

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			Action	DRS
	090_0014_01B_R_Sample10_09AUG24_CELL_MOU_ECL_0003_01AA_120MIN_KAD_RS_01.pdResult	Other
	090_0014_01B_R_Sample10_09AUG24_CELL_MOU_ECL_0003_01AA_120MIN_KAD_RS_01.raw	Raw
	090_0014_01B_R_Sample20_09AUG24_CELL_MOU_ECL_0003_01AA_120MIN_KAD_RS_01.pdResult	Other
	090_0014_01B_R_Sample20_09AUG24_CELL_MOU_ECL_0003_01AA_120MIN_KAD_RS_01.raw	Raw
	090_0014_01B_R_Sample22_09AUG24_CELL_MOU_ECL_0003_01AA_120MIN_KAD_RS_01.pdResult	Other

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Project description:Objective: ADP-ribosylation is a post-translational modification that plays an important role in cellular processes. Our previous work implemented multiple gas-phase separation strategies (e.g., FAIMS) and in-source CID on the quadrupole-Orbitrap (Exploris 480) to increase the yield and acceptor site confidence scores of HCD-dependent ADP-ribosyl (ADPr) peptide identifications. We evaluated whether FAIMS coupled on the quadrupole-ion trap-Orbitrap (Fusion Lumos) also improves EThcD-dependent ADP-ribosyl peptide sequencing. Methods: ADP-ribosyl peptides derived from the human macrophage-like cell line THP-1 were analyzed on the Fusion Lumos fronted with a FAIMS Pro device. FAIMS plus/minus gas-phase segmentation (GPS) of the MS1 scan was applied to HCD and EThcD acquisitions. ADP-ribosyl peptide spectra were annotated using the SEQUEST-HT algorithm and RiboMaP, an annotation tool specific for ADP-ribosylated peptide spectra. Results: HCD-dependent ADP-ribosyl peptide identifications were enriched at higher compensation voltages as compared to EThcD. The net number of unique ADP-ribosyl and non-ADP-ribosyl (contaminant) peptides across compensation voltages increased by 3.2- and 3.8-fold more respectively for HCD, and 2.0- and 3.6-fold respectively for EThcD, compared to no FAIMS. We also confirmed that while multiple injections of peptides employing distinct compensation voltages maximized the number of EThcD-dependent ADP-ribosyl peptide identifications, their associated XCorr and p-series scores decreased. The most frequent ADP-ribosyl acceptor site was lysine, followed by serine, and that the proportion of ADP-ribosylated serine sites increased when THP-1 cells were activated with IFN-γ. Conclusions: Although FAIMS increases EThcD-dependent sequencing depth of ADP-ribosyl peptides, the gains are less than when using HCD. The ability to filter out doubly charged non-ADP-ribosylated peptides at increasingly higher negative compensation voltages benefits HCD, but not EThcD since this dissociation method works optimally with highly charged peptides, non-ADP-ribosyl and ADP-ribosyl alike.

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Syntaxin 4 (STX4) protects islet -cells from cytokine-induced senescence

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