Oxidized Pork Induces Disorders of Glucose Metabolism in Mice

Ge, Yueting; Li, Bowen; Yang, Yuhui; Feng, Chuanxing; Tang, Xue; Shi, Yonghui; Li, Guowei; Sun, Jin

doi:10.1002/mnfr.202000859

Cited by 16 publications

(15 citation statements)

References 54 publications

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“…Thereafter, we examined the effects of MR on pancreatic β-cell fate and function in HFD-induced obese mice. In vitro , we discovered that MR reduced β-TC6 apoptosis caused by PA. Bcl-2 is an anti-apoptotic protein, and Bax and Caspase-3 are pro-apoptotic factors . In this study, MR inhibited the low expression of Bcl-2 and the high expression of Bax and caspase-3 in mice pancreas induced by HFD and β-TC6 cells induced by PA.…”

Section: Discussionmentioning

confidence: 99%

Dietary Methionine Restriction Improves Gastrocnemius Muscle Glucose Metabolism through Improved Insulin Secretion and H19/IRS-1/Akt Pathway in Middle-Aged Mice

Feng

Jiang

et al. 2023

J. Agric. Food Chem.

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Methionine restriction (MR) improves glucose metabolism. In skeletal muscle, H19 is a key regulator of insulin sensitivity and glucose metabolism. Therefore, this study aims to reveal the underlying mechanism of H19 upon MR on glucose metabolism in skeletal muscle. Middle-aged mice were fed MR diet for 25 weeks. Mouse islets β cell line β-TC6 cells and mouse myoblast cell line C2C12 cells were used to establish the apoptosis or insulin resistance model. Our findings showed that MR increased B-cell lymphoma-2 (Bcl-2) expression, deceased Bcl-2 associated X protein (Bax), cleaved cysteinyl aspartate-specific proteinase-3 (Caspase-3) expression in pancreas, and promoted insulin secretion of β-TC6 cells. Meanwhile, MR increased H19 expression, insulin Receptor Substrate-1/insulin Receptor Substrate-2 (IRS-1/IRS-2) value, protein Kinase B (Akt) phosphorylation, glycogen synthase kinase-3β (GSK3β) phosphorylation, and hexokinase 2 (HK2) expression in gastrocnemius muscle and promoted glucose uptake in C2C12 cells. But these results were reversed after H19 knockdown in C2C12 cells. In conclusion, MR alleviates pancreatic apoptosis and promotes insulin secretion. And MR enhances gastrocnemius muscle insulin-dependent glucose uptake and utilization via the H19/IRS-1/Akt pathway, thereby ameliorating blood glucose disorders and insulin resistance in high-fat-diet (HFD) middle-aged mice.

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Section: Discussionmentioning

confidence: 99%

Dietary Methionine Restriction Improves Gastrocnemius Muscle Glucose Metabolism through Improved Insulin Secretion and H19/IRS-1/Akt Pathway in Middle-Aged Mice

Feng

Jiang

et al. 2023

J. Agric. Food Chem.

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“…Furthermore, there is a strong link between protein oxidation and age-related diseases, such as diabetes, atherosclerosis, and neurodegenerative diseases (Davies & Dean, 1997). For example, Ge et al (2021) showed that the intake of oxidized pork induces disorders of glucose metabolism in mice by impairing pancreatic insulin secretion.…”

Section: Nutrition and Healthmentioning

confidence: 99%

Freezing of meat and aquatic food: Underlying mechanisms and implications on protein oxidation

Bao

Ertbjerg

Estévez

et al. 2021

Comp Rev Food Sci Food Safe

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Over the recent decades,protein oxidation in muscle foods has gained increasing research interests as it is known that protein oxidation can affect eating quality and nutritional value of meat and aquatic products. Protein oxidation occurs during freezing/thawing and frozen storage of muscle foods, leading to irreversible physicochemical changes and impaired quality traits. Controlling oxidative damage to muscle foods during such technological processes requires a deeper understanding of the mechanisms of freezing-induced protein oxidation. This review focus on key physicochemical factors in freezing/thawing and frozen storage of muscle foods, such as formation of ice crystals, freeze concentrating and macromolecular crowding effect, instability of proteins at the icewater interface, freezer burn, lipid oxidation, and so on. Possible relationships between these physicochemical factors and protein oxidation are thoroughly discussed. In addition, the occurrence of protein oxidation, the impact on eating quality and nutrition, and controlling methods are also briefly reviewed. This review will shed light on the complicated mechanism of protein oxidation in frozen muscle foods.

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“…To similar conclusions came Ge et al ( 2020 ) who found that the alteration of the gut microbiota in mice by the intake of oxidized pork contributed to the onset of oxidative stress and inflammation processes in this murine model. The same authors reported that dietary oxidized pork induced impaired lipid metabolism by decreasing insulin levels and suppressing of the insulin receptor substrate-1 (IRS-1)/phosphoinositide 3-kinase (PI3K)/protein kinase B (Akt) signaling pathway and its downstream signaling molecules (Ge et al 2021 ). Li et al ( 2019 ) observed impaired spatial learning and memory in rats fed with carbonylated proteins from a severely processed milk product.…”

Section: Concise Update On the Biological Consequences Of Protein Car...mentioning

confidence: 99%

Protein carbonylation in food and nutrition: a concise update

2021

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Protein oxidation is a topic of indisputable scientific interest given the impact of oxidized proteins on food quality and safety. Carbonylation is regarded as one of the most notable post-translational modifications in proteins and yet, this reaction and its consequences are poorly understood. From a mechanistic perspective, primary protein carbonyls (i.e. α-aminoadipic and γ-glutamic semialdehydes) have been linked to radical-mediated oxidative stress, but recent studies emphasize the role alternative carbonylation pathways linked to the Maillard reaction. Secondary protein carbonyls are introduced in proteins via covalent linkage of lipid carbonyls (i.e. protein-bound malondialdehyde). The high reactivity of protein carbonyls in foods and other biological systems indicates the intricate chemistry of these species and urges further research to provide insight into these molecular mechanisms and pathways. In particular, protein carbonyls are involved in the formation of aberrant and dysfunctional protein aggregates, undergo further oxidation to yield carboxylic acids of biological relevance and establish interactions with other biomolecules such as oxidizing lipids and phytochemicals. From a methodological perspective, the routine dinitrophenylhydrazine (DNPH) method is criticized not only for the lack of accuracy and consistency but also authors typically perform a poor interpretation of DNPH results, which leads to misleading conclusions. From a practical perspective, the biological relevance of protein carbonyls in the field of food science and nutrition is still a topic of debate. Though the implication of carbonylation on impaired protein functionality and poor protein digestibility is generally recognized, the underlying mechanism of such connections requires further clarification. From a medical perspective, protein carbonyls are highlighted as markers of protein oxidation, oxidative stress and disease. Yet, the specific role of specific protein carbonyls in the onset of particular biological impairments needs further investigations. Recent studies indicates that regardless of the origin (in vivo or dietary) protein carbonyls may act as signalling molecules which activate not only the endogenous antioxidant defences but also implicate the immune system. The present paper concisely reviews the most recent advances in this topic to identify, when applicable, potential fields of interest for future studies.

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Oxidized Pork Induces Disorders of Glucose Metabolism in Mice

Cited by 16 publications

References 54 publications

Dietary Methionine Restriction Improves Gastrocnemius Muscle Glucose Metabolism through Improved Insulin Secretion and H19/IRS-1/Akt Pathway in Middle-Aged Mice

Dietary Methionine Restriction Improves Gastrocnemius Muscle Glucose Metabolism through Improved Insulin Secretion and H19/IRS-1/Akt Pathway in Middle-Aged Mice

Freezing of meat and aquatic food: Underlying mechanisms and implications on protein oxidation

Protein carbonylation in food and nutrition: a concise update

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