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1.
J Agric Food Chem ; 71(23): 9097-9109, 2023 Jun 14.
Article in English | MEDLINE | ID: mdl-37265263

ABSTRACT

Cortisol is inevitably secreted by pigs due to the physical and psychological stressors produced by mixed group transportation and preslaughter handling. Accumulated cortisol in animal tissues enters the human body through the food chain and entails potential risks to human health. An integrated lipidome and proteome analysis was conducted to investigate the effect of the spatiotemporal variation of residual cortisol on nutrient acquisition in pork. A total of 55 crucial lipid molecules associated with cortisol residue were identified based on debiased sparse partial correlation analysis. Label-free proteomics was applied to screen 58 differentially abundant proteins (including phospholipase A2, lysophosphatidylcholine acyltransferase, and CTP:phosphocholine cytidylyltransferase), indicating that cortisol residue perturbed the glycerophospholipid biosynthetic process and glycerophospholipid metabolic process. Cortisol induced downregulations of cPLA2 encoding genes and decreased phospholipase A2 activity, resulting in the bioaccumulation of phosphatidylethanolamine (from 36.86 to 43.18 mg kg-1). Cortisol increased the activity of CTP:phosphocholine cytidylyltransferase by improving the availability of fatty acids and aggregating the inactive L-form (lipid-independent form) to the active H-form (lipid-associated form). The metabolic pathways perturbed by cortisol resulted in phosphatidylcholine degradation (from 93.73 to 58.28 mg kg-1) and lysophosphatidylcholine accumulation (from 3.39 to 5.16 mg kg-1). These findings indicated that cortisol residue deteriorated meat quality and obstructed nutrient acquisition in animal-origin foods.


Subject(s)
Hydrocortisone , Nucleotidyltransferases , Humans , Swine , Animals , Nucleotidyltransferases/metabolism , Phosphorylcholine , Choline-Phosphate Cytidylyltransferase , Phospholipases A2 , Fatty Acids , Nutrients , Phosphatidylcholines/metabolism
2.
Mol Nutr Food Res ; 66(23): e2200487, 2022 12.
Article in English | MEDLINE | ID: mdl-36261391

ABSTRACT

SCOPE: As the tremendous increases in consumption of animal-derived food, endogenous hydrocortisone migrating along the food chain to organism arouses extensive attention. This study aims to investigate the cumulative impacts of dietary hydrocortisone intake and mechanistic understanding on metabolism of lipid nutrients. METHODS AND RESULTS: A total of 120 porcine muscles samples with different concentrations of hydrocortisone are collected at three time points. An operational food chain simulation framework is constructed and 175 lipid molecules are identified by UHPLC-Q-Orbitrap HRMS. Compared to the control group, 66 lipid molecules are significantly different, including 17 triglycerides and 31 glycerophospholipids. Integrated analyses of lipidomics and proteomics indicate that hydrocortisone promotes adipose triglyceride lipase and hormone sensitive lipase activity to precondition for triglycerides hydrolysis. Quantitative lipidomics analysis shows the presence of hydrocortisone decreases the concentration of docosahexaenoic acid (3.66 ± 0.15-3.09 ± 0.12 mg kg-1 ) and eicosapentanoic acid (0.54 ± 0.09-0.48 ± 0.06 mg kg-1 ). A noteworthy increase of most saturated triglycerides concentration with the prolonging of time is observed. CONCLUSIONS: Hydrocortisone originating from animal-derived food induces glycerophospholipids degradation and triglycerides hydrolysis through promoting adipose triglyceride lipase, hormone sensitive lipase, and phosphoglycerate kinase activity and further intervenes lipid nutrients utilization.


Subject(s)
Adipose Tissue , Hydrocortisone , Animals , Swine , Hydrocortisone/metabolism , Adipose Tissue/metabolism , Triglycerides/metabolism , Nutrients , Glycerophospholipids/metabolism , Eating , Lipid Metabolism
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