Glycoxidation of histone proteins in autoimmune disorders

Mir, Abdul Rouf; Moinuddin, Mohammed

doi:10.1016/j.cca.2015.07.029

Cited by 20 publications

(10 citation statements)

References 95 publications

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“…Furthermore, Kurien BT and Scofield RH [50] have demonstrated that conjugated dienes, malondialdehyde, and 8-isoprostaglandin F2α are significantly elevated in the serum of SLE patients. In addition, Mir et al [117] reported that glycosylation of N-terminal region of a variable length in histone proteins can induce various DNA syntheses or repressions, including gene activation, gene silencing, DNA replication, and even gene damage in different autoimmune diseases. These results suggest that ROS not only mediate lipid peroxidation to elicit cardiovascular morbidities (left panel of Figure 5), but also modify self-antigens to neoantigens to induce autoantibody productions (right panel of Figure 5) in patients with SLE.…”

Section: Molecular Basis Of Oxidative and Nitrosative Stresses In mentioning

confidence: 99%

Molecular and Cellular Bases of Immunosenescence, Inflammation, and Cardiovascular Complications Mimicking “Inflammaging” in Patients with Systemic Lupus Erythematosus

Tsai

Shen

Liao

et al. 2019

IJMS

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Systemic lupus erythematosus (SLE) is an archetype of systemic autoimmune disease, characterized by the presence of diverse autoantibodies and chronic inflammation. There are multiple factors involved in lupus pathogenesis, including genetic/epigenetic predisposition, sexual hormone imbalance, environmental stimulants, mental/psychological stresses, and undefined events. Recently, many authors noted that “inflammaging”, consisting of immunosenescence and inflammation, is a common feature in aging people and patients with SLE. It is conceivable that chronic oxidative stresses originating from mitochondrial dysfunction, defective bioenergetics, abnormal immunometabolism, and premature telomere erosion may accelerate immune cell senescence in patients with SLE. The mitochondrial dysfunctions in SLE have been extensively investigated in recent years. The molecular basis of normoglycemic metabolic syndrome has been found to be relevant to the production of advanced glycosylated and nitrosative end products. Besides, immunosenescence, autoimmunity, endothelial cell damage, and decreased tissue regeneration could be the results of premature telomere erosion in patients with SLE. Herein, the molecular and cellular bases of inflammaging and cardiovascular complications in SLE patients will be extensively reviewed from the aspects of mitochondrial dysfunctions, abnormal bioenergetics/immunometabolism, and telomere/telomerase disequilibrium.

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Section: Molecular Basis Of Oxidative and Nitrosative Stresses In mentioning

confidence: 99%

Molecular and Cellular Bases of Immunosenescence, Inflammation, and Cardiovascular Complications Mimicking “Inflammaging” in Patients with Systemic Lupus Erythematosus

Tsai

Shen

Liao

et al. 2019

IJMS

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“…Histone H4 (HIST4H4, UniProtKB accession no. H4_PIG) constitutes an autoantigen in a H3/4 heterodimer form in auto immunity20. NF-kappa B is well-known for its function in immune surveillance, whose inhibitor COMM domain containing 7 (COMMD7, UniProtKB accession no.…”

Section: Resultsmentioning

confidence: 99%

A proteomic adaptation of small intestinal mucosa in response to dietary protein limitation

Qin

Qiu

Sun

et al. 2016

Sci Rep

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Dietary protein limitation (PL) is not only beneficial to human health but also applied to minimize nitrogen excretion in livestock production. However, the impact of PL on intestinal physiology is largely unknown. In this study, we identified 5275 quantitative proteins using a porcine model in which pigs suffered PL. A total of 202 proteins |log2 fold-change| > 1 were taken as differentially expressed proteins and subjected to functional and pathway enrichment analysis to reveal proteomic alterations of the jejunal mucosa. Combining with the results of western blotting analysis, we found that protein/carbohydrate digestion, intestinal mucosal tight junction and cell adhesion molecules, and the immune response to foreign antigens were increased in the jejunal mucosa of the pigs upon PL. In contrast, amino acid transport, innate and auto immunity, as well as cell proliferation and apoptosis were reduced. In addition, the expression of functional proteins that involved in DNA replication, transcription and mRNA splicing as well as translation were altered in the jejunal mucosa in response to PL. Furthermore, PL may reduce amino acid transport and cell proliferation through the depression of mTOR pathway. This study provides new insights into the molecular mechanisms underlying the small intestinal response to PL.

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“…It may be hypothesized that histones are prone to carbamylation as well as to glycation [35]. Indeed, it has been shown that histone molecular aging actively participates in the development of autoimmune diseases [36].…”

Section: Discussionmentioning

confidence: 99%

Proteasome-dependent degradation of intracellular carbamylated proteins

Desmons

Okwieka

Doué

et al. 2019

Aging

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Carbamylation, which corresponds to the binding of isocyanic acid to the amino groups of proteins, is a nonenzymatic post-translational modification responsible for alterations of protein structural and functional properties. Tissue accumulation of carbamylation-derived products and their role in pathological processes such as atherosclerosis or chronic renal failure have been previously documented. However, few studies have focused on the carbamylation of intracellular proteins and their subsequent role in cellular aging. This study aimed to determine the extent of intracellular protein carbamylation, its impact on cell functions and the ability of cells to degrade these modified proteins. Fibroblasts were incubated with cyanate or urea and the carbamylation level was evaluated by immunostaining and homocitrulline quantification. The results showed that carbamylated proteins accumulated intracellularly and that all proteins were susceptible. The presence of intracellular carbamylated proteins did not modify cell proliferation or type I collagen synthesis nor did it induce cell senescence, but it significantly decreased cell motility. Fibroblasts were able to degrade carbamylated proteins through the ubiquitin-proteasome system. In conclusion, intracellular proteins are susceptible to carbamylation but their accumulation does not seem to deeply affect cell function, owing largely to their elimination by the ubiquitin-proteasome system.

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Glycoxidation of histone proteins in autoimmune disorders

Cited by 20 publications

References 95 publications

Molecular and Cellular Bases of Immunosenescence, Inflammation, and Cardiovascular Complications Mimicking “Inflammaging” in Patients with Systemic Lupus Erythematosus

Molecular and Cellular Bases of Immunosenescence, Inflammation, and Cardiovascular Complications Mimicking “Inflammaging” in Patients with Systemic Lupus Erythematosus

A proteomic adaptation of small intestinal mucosa in response to dietary protein limitation

Proteasome-dependent degradation of intracellular carbamylated proteins

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