Disease relevance of C01152

• Forearm 3-methylhistidine efflux in myotonic dystrophy [1].
• Efflux of 3-methylhistidine from the leg in cancer patients who experience weight loss [2].
• Studies on 3-methylhistidine metabolism in children with protein-energy malnutrition [3].
• Some amino acid alterations became worse with renal failure such as 3-methylhistidine increase or tyrosine/phenylalanine decrease, but group 3 patients had the greatest number of individual amino acid alternations [4].
• Actin degradation was quantitated by analysis of 3-methylhistidine which was significantly (P < 0.05) decreased by 15% following 30 min ischemia and 60 min reperfusion [5].

Psychiatry related information on C01152

• The groups did not differ in reaction time nor in excretion of urinary 3-methylhistidine [6].
• Whole body protein turnover, using [15N]glycine as a tracer, and 3-methylhistidine excretion were not different in the two groups, despite lower physical activity of the middle-aged men [7].

High impact information on C01152

• An improved method for measurement of 3-methylhistidine in blood samples has been used to assess efflux of 3-methylhistidine from the leg in cancer patients experiencing weight loss [2].
• In nine cirrhotics and nine age- and sex-matched controls, similar correlations were found between 3-methylhistidine and the areas under 24-hr glucagon or insulin/glucagon curves [8].
• Although it is a 3-methylhistidine in the vast majority of actins, His(73) is unmethylated in S. cerevisiae actin [9].
• 3-Methylhistidine (unbound) levels in skeletal muscle of unperfused diabetic rats as well as in skin decreased, whereas they increased twofold in the gastrointestinal tract [10].
• We have also examined the amino acid sequence of a 3-methyl-histidine-containing peptide which originates from the 20-kDa fragment of pectoralis muscle MHC in dystrophic chicks: Val-Leu-Asn-Ala-Ser-Ala-Ile-Pro-Glu-Gly-*Gln-Phe-*Ile-Asp-Ser-Lys-Lys- Ala-Ser-Leu-Gln-Lys-Leu-Gly-Ser-Ile-Asp-Val-(Asp, 3-methylhistidine, Gln) [11].

Chemical compound and disease context of C01152

• The arm muscle area, derived fat-free mass, urinary excretion of 3-methylhistidine and creatinine were measured serially in a group of patients with an intestinal fistula receiving prolonged nutritional support [12].
• 1. We have investigated arteriovenous exchanges of tyrosine and 3-methylhistidine across leg tissue in the postabsorptive state as specific indicators of net protein balance and myofibrillar protein breakdown, respectively, in eight patients with emphysema and in 11 healthy controls [13].
• The glucose uptake during clamping was 3.9 mg kg(-1) min(-1) (7.0 is normal), which, during the second day after hysterectomy, correlated with the dehydration of the intracellular space (r=0.77; P<0.002) and with the protein catabolism as indicated by the urinary excretion of 3-methylhistidine (r=-0.76, P<0.002) [14].
• The effects of adequate total parenteral nutrition (TPN) on nitrogen excretion, urea N percentage, 3-methylhistidine excretion, and leg amino acid output, were studied during the ten-day period following abdominal surgery for generalized peritonitis in nine patients [15].
• Urinary excretion of 3-methylhistidine and creatine in carriers of Duchenne muscular dystrophy [16].

Biological context of C01152

• Fat-free mass as a function of maximal oxygen consumption and 24-hour urinary creatinine, and 3-methylhistidine excretion [17].
• The skeletal muscle content of 3-methylhistidine has been measured in two fetuses and four infants of 15 to 38 wk of gestation [18].
• In growing fed rats in three separate experiments, measurements of the methylation rate of protein-bound 3-methylhistidine by either [14C]- or [3H]-methyl-labelled S-adenosylmethionine show that 3-methylhistidine synthesis is slower than the overall rate of protein synthesis indicated by [14C]tyrosine incorporation [19].
• In a second experiment, urinary and skeletal muscle 3-methylhistidine content was used to compare the rate of muscle protein breakdown between phenotypes at 8 weeks of age [20].
• RESULTS: Resting energy expenditure did not increase from preoperative values; however, urinary nitrogen and 3-methylhistidine increased significantly after liver transplantation, an indication of protein catabolism from a myofibrillar source [21].

Anatomical context of C01152

• Measurements were also made of the steady-state synthesis rate of protein-bound 3-methylhistidine in intestinal smooth muscle in vivo in adult female rats [22].
• Interstitial 3MH concentration was calculated using the internal reference method from microdialysate samples that were obtained from two microdialysis probes placed in the vastus lateralis [23].
• To determine whether this delayed onset of actin methylation occurred simultaneously throughout the organism or differed from tissue to tissue, the 3-methylhistidine content of cardiac muscle actin from Day 2 of embryonic life to hatching and of brain actin at Days 9, 11, and 14 were analyzed [24].
• Rapid analysis of 3-methylhistidine in urine, plasma, muscle and amniotic fluid with a single high-performance liquid chromatographic system but with different ion-pairing reagents [25].
• In methylation experiments employing the fusion actin in the form of inclusion bodies, 3-methylhistidine is the major product, as is the case when soluble muscle or non-muscle actin is used [26].

Associations of C01152 with other chemical compounds

• Additional studies revealed that the addition of excess retinol to the perfusion medium (10 i.u./ml) had no significant effect on the rates of 3-methylhistidine release or [3H]phenylalanine incorporation in vitro [27].
• Excessive vitamin A intake stimulated 3-methylhistidine excretion in vivo and in vitro in both adrenalectomized and sham-operated animals, thus suggesting that the vitamin A-induced acceleration in myofibrillar protein breakdown was not mediated by the adrenals [27].
• Pretreatment of rats with IL-6 for 6 hr induced fever and increased the release of both tyrosine and 3-methylhistidine by the extensor digitorum longus muscle [28].
• Plasma albumin, prealbumin, fibronectin and serum urea concentrations, nitrogen balance and 3-methylhistidine release from the leg and its excretion in the urine were measured [29].
• Body N balance, 3-methylhistidine (MEH) excretion, amino acid (AA) plasma concentration, and fluxes across the leg were investigated both during fasting and during parenteral nutrition of injured patients in order to better understand protein-sparing mechanisms induced by metabolic support in the whole body and in skeletal muscle [30].

Gene context of C01152

• Urinary 3-methylhistidine excretion correlated with mononuclear cell secretion of both IL-1 beta (P less than 0.05) and prostaglandin E2 (P less than 0.05), supporting the concept that these mononuclear cell products contribute to the regulation of muscle proteolysis [31].
• There was no relationship between IL-6, nitrogen balance, and 3-methylhistidine excretion [32].
• Indinavir increased mRNA expression of the ubiquitin ligase MuRF1, but the plasma concentration of 3-methylhistidine remained unaltered [33].
• Interleukin 6 levels correlated positively with protein turnover (phenylalaninemia) and catabolism (3-methylhistidine/creatinine ratio) and negatively with levels of fibronectin and transthyretin [34].
• The mean +/- SEM 3-methylhistidine loss for burned patients on the third day was 9.83 +/- 0.82 mumol/kg compared to 3.6 mol/kg for control patients [35].

Analytical, diagnostic and therapeutic context of C01152

• Plasma 3-methylhistidine levels increased with tumor burden [36].
• Twenty-four hour urinary excretion of 3-methylhistidine (3-MeHis) was determined in children suffering from severe and moderate degrees of protein-energy malnutrition before and after treatment [3].
• Whole body protein breakdown using 15N and skeletal muscle protein breakdown from urinary 3-methylhistidine were measured simultaneously in seven skeletal trauma and eight normal subjects on a standard hypocaloric, protein free diet [37].
• We therefore undertook a prospective, randomized, double blind trial investigating the effects of BCAA enrichment of a total parenteral nutrition (TPN) regimen on nitrogen balance, 3-methylhistidine excretion, morbidity as evidenced by disturbances in organ function, severity of sepsis and mortality [38].
• Rapid high-performance liquid chromatography of 3-methylhistidine in human urine [39].

References