Content of methylhistidines in normal and pathological human skeletal muscles

Mussini, E.; Cornelio, F.; Dworzak, F.; Cotellessa, L.; Morandi, Lucia; Colombo, Laura; Ponte, G. De; Marcucci, F.

doi:10.1002/mus.880060605

Cited by 20 publications

(12 citation statements)

References 32 publications

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“…Little has been detailed regarding PRMT content and activity in mature muscle, which is surprising since protein methylation in skeletal muscle was first described ϳ40 yr ago (33). Protein methylation, primarily 3-methylhistidine of noncollagen proteins (e.g., actin and myosin), is altered in dystrophic skeletal muscle (46,50). Protein arginine methylation has been shown to affect the myogenic program in cell culture (16,27,31), whereas PGC-1␣ and RIP 140 activity are directly influenced by arginine methylation in nonmuscle cells (48,66).…”

Section: Discussionmentioning

confidence: 98%

Chronic AMPK stimulation attenuates adaptive signaling in dystrophic skeletal muscle

Ljubicic

Khogali

Renaud

et al. 2012

American Journal of Physiology-Cell Physiology

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In the present study, we evaluated how a pharmacologically induced phenotype shift in dystrophic skeletal muscle would affect subsequent intracellular signaling in response to a complementary, adaptive physiological stimulus. mdx mice were treated with the AMP-activated protein kinase (AMPK) activator 5-aminoimidazole-4-carboxamide-1-β-D-ribofuranoside (AICAR; 500 mg·kg(-1)·day(-1)) for 30 days, and then one-half of the animals were subjected to a bout of treadmill running to induce acute AMPK and p38 MAPK signaling. The mRNA levels of phenotypic modifiers, including peroxisome proliferator-activated receptor-δ (PPARδ), PPARγ coactivator-1α (PGC-1α), receptor interacting protein 140 (RIP 140), and silent information regulator two ortholog 1 (SIRT1) were assessed in skeletal muscle, as well as the expression of the protein arginine methyltransferase genes PRMT1 and CARM1. We found unique AMPK and p38 phosphorylation and expression signatures between dystrophic and healthy muscle. In dystrophic skeletal muscle, treadmill running induced PPARδ, PGC-1α, and SIRT1 mRNAs, three molecules that promote the slow, oxidative myogenic program. In the mdx animals that received the chronic AICAR treatment, running-elicited AMPK and p38 phosphorylation was attenuated compared with vehicle-treated mice. Similarly, acute stress-evoked expression of PPARδ, PGC-1α, and SIRT1 was also blunted by chronic pharmacological AMPK stimulation. Skeletal muscle PRMT1 and CARM1 protein contents were higher in mdx mice compared with wild-type littermates. The acute running-evoked induction of PRMT1 and CARM1 mRNAs was also attenuated by the AICAR treatment. Our data demonstrate that prior pharmacological conditioning is a salient determinant in how dystrophic muscle adapts to subsequent complementary, acute physiological stress stimuli. These results provide insight into possible therapeutic applications of synthetic agonists in neuromuscular diseases, such as during chronic administration to Duchenne muscular dystrophy patients.

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Section: Discussionmentioning

confidence: 98%

Chronic AMPK stimulation attenuates adaptive signaling in dystrophic skeletal muscle

Ljubicic

Khogali

Renaud

et al. 2012

American Journal of Physiology-Cell Physiology

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“…Thus, muscle protein degradation is the only endogenous source of 3‐MH in human plasma. In healthy adults (20–70 years) the content of 3‐MH in muscle and the 3‐MH‐to‐creatinine excretion (3‐MH/Crea) ratio remain constant . Thus, we suggest that 3‐MH might be a helpful biomarker in the assessment of muscle protein turnover, which is important in the diagnosis of frailty and sarcopenia.…”

Section: Introductionmentioning

confidence: 88%

“…3‐Methylhistidine (3‐MH; N ‐tau‐methylhistidine) seems to be a suitable biomarker to identify elevated muscle degradation or an unfavorable muscle protein turnover as shown in muscle wasting disease and elderly populations . 3‐MH is synthesized only in the muscle by the methylation of one histidine residue in actin and in varying amounts in myosin depending on the type of muscle .…”

Section: Introductionmentioning

confidence: 99%

The Influence of Dietary Habits and Meat Consumption on Plasma 3‐Methylhistidine—A Potential Marker for Muscle Protein Turnover

Kochlik

Gerbracht

Grune

et al. 2018

Molecular Nutrition Food Res

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Scope3‐Methylhistidine (3‐MH) as a potential biomarker for muscle protein turnover is influenced by meat intake but data on the impact of meat on plasma 3‐MH are scarce. We determined the association of plasma 3‐MH, 1‐methylhistidine (1‐MH), and creatinine with dietary habits and assessed the impact of a single white meat intervention during a meat‐free period.Methods and resultsPlasma 3‐MH, 1‐MH, and creatinine concentrations of healthy young omnivores (n = 19) and vegetarians (n = 16) were analyzed together with data on anthropometry, body composition, grip strength, and nutrition. After baseline measurements omnivores adhered to a meat‐free diet for 6 days and received a defined administration of chicken breast on day four. At baseline, omnivores had higher plasma 3‐MH and 1‐MH concentrations than vegetarians. White meat administration led to a slight increase in plasma 3‐MH in omnivores. The elevated 3‐MH concentrations significantly declined within 24 h after white meat intake.Conclusion1‐MH concentrations in plasma seem to be suitable to display (white) meat consumption and its influence on 3‐MH plasma concentration. 3‐MH in plasma may be used as a biomarker for muscle protein turnover if subjects have not consumed meat in the previous 24 h.

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“…Plasma 3-methylhistidine (3-MH; N-tau-methylhistidine) seems to be a potential biomarker to display an elevated muscle protein turnover [14,15,16]. 3-MH is formed in the muscle by the post-translational methylation of histidine residues in actin and myosin [17,18,19].…”

Section: Introductionmentioning

confidence: 99%

“…Normalizing 3-MH to Crea concentrations (3-MH/Crea) showed smaller inter-individual variations and therefore, these ratios are recommended for the assessment of muscle protein breakdown in heterogeneous populations [24]. The amount of 3-MH in the muscle and the excretion of 3-MH/Crea remained constant in healthy subjects (20–70 years) [14,25]. Contrarily, 3-MH excretion was increased in muscle wasting diseases [14,15,16,25,26].…”

Section: Introductionmentioning

confidence: 99%

Associations of Plasma 3-Methylhistidine with Frailty Status in French Cohorts of the FRAILOMIC Initiative

Kochlik

Stuetz

Pérès

et al. 2019

JCM

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Frailty and sarcopenia are characterized by a loss of muscle mass and functionality and are diagnosed mainly by functional tests and imaging parameters. However, more muscle specific biomarkers are needed to improve frailty diagnosis. Plasma 3-methylhistidine (3-MH), as well as the 3-MH-to-creatinine (3-MH/Crea) and 3-MH-to-estimated glomerular filtration rate (3-MH/eGFR) ratios might support the diagnosis of frailty. Therefore, we investigated the cross-sectional associations between plasma 3-MH, 3-MH/Crea and 3-MH/eGFR with the frailty status of community-dwelling individuals (>65 years). 360 participants from two French cohorts of the FRAILOMIC initiative were classified into robust, pre-frail and frail according to Fried’s frailty criteria. General linear models as well as bivariate and multiple linear and logistic regression models, which were adjusted for several confounders, were applied to determine associations between biomarkers and frailty status. The present study consisted of 37.8% robust, 43.1% pre-frail and 19.2% frail participants. Frail participants had significantly higher plasma 3-MH, 3-MH/Crea and 3-MH/eGFR ratios than robust individuals, and these biomarkers were positively associated with frailty status. Additionally, the likelihood to be frail was significantly higher for every increase in 3-MH (1.31-fold) and 3-MH/GFR (1.35-fold) quintile after adjusting for confounders. We conclude that 3-MH, 3-MH/Crea and 3-MH/eGFR in plasma might be potential biomarkers to identify frail individuals or those at higher risk to be frail, and we assume that there might be biomarker thresholds to identify these individuals. However, further, especially longitudinal studies are needed.

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Content of methylhistidines in normal and pathological human skeletal muscles

Cited by 20 publications

References 32 publications

Chronic AMPK stimulation attenuates adaptive signaling in dystrophic skeletal muscle

Chronic AMPK stimulation attenuates adaptive signaling in dystrophic skeletal muscle

The Influence of Dietary Habits and Meat Consumption on Plasma 3‐Methylhistidine—A Potential Marker for Muscle Protein Turnover

Associations of Plasma 3-Methylhistidine with Frailty Status in French Cohorts of the FRAILOMIC Initiative

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