3-Methylhistidine in actin and other muscle proteins

Johnson, Peter; Harris, C. I.; Perry, S. V.

doi:10.1042/bj1050361

Cited by 237 publications

(113 citation statements)

References 43 publications

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“…To investigate the physiological relevance of increased muscle protein degradation in vitro as shown above, we measured the urinary excretion of 3-methylhistidine in control and clofibrate-fed rats. This amino acid is formed by methylation of specific histidine residues of peptide chains and is largely confined to actin and myosin of skeletal muscle (36,37). Unlike other amino acids, 3-methylhistidine when released by degradation of muscle proteins is not reutilized for protein synthesis nor catabolized as an energy source, but is quantitatively excreted in the urine (25).…”

Section: Resultsmentioning

confidence: 99%

Leucine Oxidation and Protein Turnover in Clofibrate-induced Muscle Protein Degradation in Rats

Paul¹,

Adibi²

1980

J. Clin. Invest.

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A B S T R A C T Treatment of hvperlipidemia withclofibrate may result in development of a muscular svndrome. Our previous investigation (1979. J. ClitG. Ivce.st. 64: 405.) showed that chronic administration of clofibrate to rats causes mvotonia and decreases glucose and fatty acid oxidation and total protein of skeletal muscle. In the present experimiients we have investigated amino acid and protein metabolism in these rats. Clofibrate administratioin decreased the concenitration of all three branched-chain amino acids without affecting those of others in muscle. Studies to examine the mechanism of decreases in muscle concenitrationis of branched-chain amiiino acids showed the followiing: (a)

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Section: Resultsmentioning

confidence: 99%

Leucine Oxidation and Protein Turnover in Clofibrate-induced Muscle Protein Degradation in Rats

Paul¹,

Adibi²

1980

J. Clin. Invest.

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“…This unusual amino acid is present in both muscle actin (Asatoor & Armstrong, 1967;Johnson et a/., 1967) and in a number of cytoplasmic actins (Pollard & Weihing, 1974). The analysis was carried out on cultures of fibroblasts which had been radioactively labelled with [3fl]histidine.…”

Section: Resultsmentioning

confidence: 99%

The actin content of fibroblasts

Bray¹,

Thomas²

1975

Biochemical Journal

107

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Cultures of chick skin fibroblasts were dissolved in solutions of sodium dodecyl sulphate, and their entire protein content was examined by gel electrophoresis. The most abundant species migrated in the same position as muscle actin. It gave a similar pattern of iodinated peptides after reaction with radioactive sodium iodide and digestion with proteinases, and contained comparable amounts of N-methylhistidine. Its amount was estimated by quantitative densitometry of stained gels with bovine serum albumin as an internal standard, and by radioactive assay ofcultures that had been grown in the presence of [35S]methionine. The values obtained ranged from 7 to 14% of the total cellular protein, with an average of 8.5 %. A protein band in the position of muscle myosin was also present and accounted for about 2.5 % of the total protein. Both this and the actin band increased in relative amount with the age of the cultures.

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“…The NHz-terminal sequence of non-muscle actin from Schneider L-2 cells of D. melitnogasrev is predicted from the electrophoretic properties of the [14C]carboxymethylated peptide and its secondary fragments (for details see text). BI represents an NHZ-terminal blocking group which, in analogy with rabbit skeletal muscle actin [28,29] and Dictyosieliurn actin [36], is most likely the acetyl group. The presence of such a group in yeast actin has not yet been determined.…”

Section: Table 1 Amino Acid Sequences Of Rhe Nhz-rerminal Rrypric Pementioning

confidence: 99%

Actin Typing on Total Cellular Extracts

Vandekerckhove

Weber

1981

European Journal of Biochemistry

213

106

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Based on the finding that the amino-terminal tryptic peptide of actin is a reliable marker for actin divergence, we describe in detail a highly sensitive protein-chemical procedure for actin typing. The method is performed on non-radioactively labelled cells and tissues and six actins can be identified unambiguously in warm-blooded vertebrates. The method is quantitative and gives directly the ratio of the different actins present in the specimens. It does not require previous purification of actin and can be used on total cellular extracts without any prior fractionation. The procedure can be extended to actins not previously characterized by amino acid sequence analysis and makes certain predictions possible about the partial amino acid sequences of the amino-terminal tryptic peptides, mostly sufficient for a correlation with DNA sequences derived from cloned actin genes. This is done as an example for the cytoplasmic actin present in Schneider L-2 Drosophilu melunoguster cells. Although the method is currently used routinely on lo5 cells, modifications are discussed, which should allow the analysis to be performed with even higher sensitivity.Actin is a major protein expressed probably in all different eukaryotic cell types (for a review see [1,2]). Mammals and most likely also birds express at least six different actin genes in a tissue-specific and species-independent manner : two nonmuscle actins, two smooth-muscle actins, cardiac-muscle actin and skeletal-muscle actin [3,4] (and our unpublished results). The complete amino acid sequences now available show that these six actin polypeptides are extremely closely related. Their polypeptide length differs by maximally one amino acid residue and the highest number of amino acid exchanges observed is 25 in a comparison of non-muscle y-actin and skeletal-muscle actin [4-101. The four muscle actins are even more similar and in the most extreme case, i.e. skeletal-muscle actin and one type of smooth-muscle actin, differ by only eight residues [4].Actin differentiation is routinely assessed by one-dimensional or two-dimensional polyacrylamide gel electrophoresis using isoelectric focussing analysis in the first dimension [11 -131. This system resolves three actin types easily: fi and y nonmuscle actins and the so-called a-actins typical of sarcomeric actins [12]. The two smooth-muscle actins are not easily distinguished from a and y-actin, i.e. the a-type smooth-muscle actin is easily confused with sarcomeric actins [3,4] and the y-type smooth-muscle actin with non-muscle y-actin [14], potentially giving rise to erroneous assignments. The latter results, however, explain the different isoelectric points of various actins. Thus for instance the a and y-like smooth-muscle actins, which differ by as much as a full charge, show only three amino acid differences [4], whereas non-muscle y-actin and y-like smooth-muscle actin which are only marginally separated by isoelectric focussing analysis differ by up to 17 residues [10,15]. Similar difficulties can be expected in ...

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3-Methylhistidine in actin and other muscle proteins

Cited by 237 publications

References 43 publications

Leucine Oxidation and Protein Turnover in Clofibrate-induced Muscle Protein Degradation in Rats

Leucine Oxidation and Protein Turnover in Clofibrate-induced Muscle Protein Degradation in Rats

The actin content of fibroblasts

Actin Typing on Total Cellular Extracts

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