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Mass Spectrometric Profiling of hepatic GSTM3 - co-immunoprecipitate in Cholesterol-induced Steatohepatic Apoe knockout Mice

ABSTRACT: Glutathione S-transferase Mu 3 (GSTM3) is a cytosolic detoxification isoform of the glutathione S-transferase family, implicated in cellular redox homeostasis and protection against lipid peroxidation–derived reactive products. Emerging evidence suggests that GSTM3 functions beyond xenobiotic metabolism and may contribute to the pathogenesis of stress-induced diseases, including cardiovascular disorders, neurodegenerative diseases, and cancer. However, how the GSTM3-associated interactome links oxidative stress responses to metabolic and inflammatory signaling pathways remains largely unknown. In this study, we performed mass spectrometry–based proteomic profiling of hepatic GSTM3-associated protein complexes using co-immunoprecipitation followed by LC–MS/MS analysis. GSTM3-containing complexes were isolated from the livers of control and cholesterol-induced steatohepatitis Apoe⁻/⁻ mice. The resulting datasets provide an unbiased characterization of the GSTM3 interactome under both basal and disease-associated conditions, enabling the identification of proteins potentially involved in redox regulation, metabolic stress responses, and downstream inflammatory signaling pathways.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Liver

DISEASE(S): Non-alcoholic Steatohepatitis,Disease Free

SUBMITTER: Trina Roy

LAB HEAD: Dr. Arun Bandyopadhyay

PROVIDER: PXD074038 | Pride | 2026-05-20

REPOSITORIES: Pride

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Project description:Papaya (Carica papaya) is a trioecious species, with female, male, and hermaphrodite plants. Because of sex segregation, selecting hermaphroditic plants is vital for orchard establishment due to their higher commercial value. In addition to the costly sexing step, environmental stresses can result in abnormal flower development. However, molecular mechanisms that regulate sex differentiation in papaya are still poorly known. Thus, this study aimed to identify proteins associated with sex development in female and hermaphrodite flowers of papaya through comparative proteomic analysis. Proteins from flower buds at the early and late developmental stages of three papaya genotypes (UENF-CALIMAN 01, JS12, and Sunrise Solo 72/12) were studied via proteomic analysis via the combination of the shotgun method and nanoESI-HDMSE technology. In buds at an early stage of development, 496 proteins exhibited significantly different abundances between sexes for the SS72/12 genotype, 139 for the JS12 genotype, and 165 for the UC-01 genotype. At the final stage of development, there were 181 for SS72/12, 113 for JS12, and 125 for UC-01. The large group of differentially accumulated proteins (DAPs) between the sexes was related to metabolism, as shown by the observation of only the proteins that exhibited the same pattern of accumulation in the three genotypes. Specifically, carbohydrate metabolism proteins were up-regulated in hermaphrodite flower buds early in development, while those linked to monosaccharide and amino acid metabolism increased during late development. Enrichment of sporopollenin and phenylpropanoid biosynthesis pathways characterizes hermaphrodite samples across developmental stages, with predicted protein interactions highlighting the crucial role of phenylpropanoids in sporopollenin biosynthesis for pollen wall formation. Most of the DAPs played key roles in pectin, cellulose, and lignin synthesis and were essential for cell wall formation and male flower structure development, notably in the pollen coat. These findings suggest that hermaphrodite flowers require more energy for development, likely due to complex pollen wall formation. Overall, these insights illuminate the molecular mechanisms of papaya floral development, revealing complex regulatory networks and energetic demands in the formation of male reproductive structures.

Project description:Background: Racehorses undergo profound physiological changes in response to training and competition, yet current tools to assess training adaptation and overload remain limited. Traditional biomarkers often fail to reflect the complex molecular dynamics induced by physical effort. This study aimed to identify new plasma biomarkers of exercise adaptation in racehorses using high-throughput proteomics. Objectives: We hypothesized that systematic training and racing efforts induce distinct proteomic signatures in plasma, enabling the identification of novel candidate biomarkers reflecting training status, oxidative stress, inflammation, and metabolic remodeling. Study Design: This was an in vivo longitudinal study using repeated blood sampling in the same horses across different phases of training and racing. Methods: Forty-nine Arabian and Thoroughbred racehorses underwent standardized high-intensity training. Plasma samples were collected at rest, immediately post-exercise, and after recovery, during three phases: early training (T1), mid-season conditioning (T2), and racing (R). A total of 314 samples were analyzed using TMT-based quantitative proteomics and high-resolution mass spectrometry. Protein expression changes were evaluated with statistical correction for multiple comparisons (FDR < 0.05), and functional pathway enrichment was conducted via STRING and ShinyGO. Results: The proteomic response evolved across phases: T1 revealed a broad activation of inflammatory (S100A8/A9), antioxidant (SOD1, catalase), and metabolic proteins (G6PD, PGK1), while T2 showed refined expression of remodeling and redox regulators (decorin, thymosin β4, glutathione S-transferase). The racing phase induced the strongest response, with >100 upregulated proteins involved in energy metabolism, oxidative stress defense, and cytoskeletal adaptation. Several proteins (e.g., S100A8, thymosin β4, prothymosin α, cofilin-1, lipocalins) consistently changed across all phases, indicating their biomarker potential. Conclusions: This study identified a panel of promising plasma biomarkers reflecting exercise adaptation and overload in racehorses. These novel candidates may enhance monitoring of performance, training status, and early signs of overtraining in equine athletes.

			Action	DRS
	GSTM3_SDRF.sdrf.tsv	Tabular
	H1_30.mgf	Mgf
	H1_30.msf	Msf
	H1_30.mzid	Mzid
	H1_30.raw	Raw

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Mass Spectrometric Profiling of hepatic GSTM3 - co-immunoprecipitate in Cholesterol-induced Steatohepatic Apoe knockout Mice

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