Nτ-Methylhistidine content of mixed proteins in various rat tissues

Haverberg, Linda N.; Omstedt, Per T.; Munro, Hamish N.; Young, Vernon R.

doi:10.1016/0005-2795(75)90315-3

Cited by 125 publications

(48 citation statements)

References 25 publications

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“…This view is consistent with our earlier observation that clofibrate treatment decreases the protein concentration in the muscle (17). Assuming that the rates of myofibrillar and sarcoplasmic protein breakdown are of approximately the same magnitude (42), and that the 3-methylhistidine content of rat skeletal muscle is 3.85 ,mol/g protein (43), the rate of muscle protein degradation can be estimated from the urinary 3-methylhistidine excretion data. As shown in Table III, the amount of muscle protein degraded over the entire 2-wk experiment was 35% higher in clofibrate-fed than in control rats.…”

Section: Discussionmentioning

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: Discussionmentioning

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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“…For the special case of muscle, the method introduced by Haverberg and co-workers has been widely used, in which the 24 h excretion of 3-methylhistidine (3-MH) is taken as a measure of the rate of breakdown of myofibrillar proteins in skeletal muscle (Haverberg, Omstedt, Munro & Young, 1975;Young & Munro, 1978;Tomas, Ballard & Pope, 1979). It has recently been suggested that significant amounts of 3-MH are derived from tissues other than skeletal muscle.…”

Section: Measurement Ofprotein Turnover Rates In Individual Tissuesmentioning

confidence: 99%

Protein Turnover With Special Reference to Man

1984

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This review is concerned with rates of N flux in the living animal rather than with mechanisms of protein synthesis and breakdown at the cellular level. Methods of measuring protein turnover in the whole body are discussed, with special emphasis on studies in man, and results obtained by different methods have been compared. Aspects of whole body protein turnover which are of physiological interest include its relation to body size, growth and development, energy metabolism and food intake. There are substantial increases in protein turnover in injury, and changes that occur in exercise are beginning to be explored. From the physiological point of view these results point the need for future research along two main lines. The first is that of regulation: a wide variety of hormones stimulate or repress protein synthesis and breakdown, with varying actions in different tissues. These effects, however, do not in themselves explain the mechanism by which a balance between synthesis and breakdown is maintained. Secondly, the fact that all cellular proteins are in a dynamic state poses questions about the relation between structure and function in tissues such as muscle and brain, which physiologists have hardly begun to tackle.

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“…The amino acid released during breakdown is not recycled; it is instead excreted in urine as such. Measurements of total organ content of 3-MH from different tissue [7] have revealed that skeletal muscle tissue has more than 100 times the amount of amino acid than any other tissue examined. These workers have further stressed that 3-MH obtained in the urine is largely derived from skeletal muscle.…”

Section: Discussionmentioning

confidence: 99%

“…Total muscle proteins were extracted according to the details described elsewhere [7]. A weighed amount of tissue was homogenized in nine volumes of cold distilled water.…”

Section: -Methylhistidine Measurementmentioning

confidence: 99%

Beta Adrenoceptor Agonists, Clenbuterol, and Isoproterenol Retard Denervation Atrophy in Rat Gastrocnemius Muscle: Use of 3-Methylhistidine as a Marker of Myofibrillar Degeneration.

Agrawal

Thakur²,

Katoch³

2003

JJP

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Beta adrenergic agonists such as clenbuterol, salbutamol, and albuterol are sympathomimetic substances capable of activating beta receptors in vivo. One important function of these substances is to produce effects resembling those of the impulses transmitted by postganglionic fibers of the central nervous system, thereby mimicking normal innervation control in tissues such as skeletal muscle. A dietary administration of these beta adrenoceptor agonists in rat produce growth-promoting protein anabolic effects in skeletal muscle [1,15,21,23,28]. The chronic administration of these agonists causes a hypertrophy of skeletal muscle in mice [17] and in the diaphragm of hamster [31]. The stimulation of the growth of skeletal muscle as a result of an application of beta adrenergic agonists is believed to be largely because of an accelerated protein turnover rate [10] coupled with a decrease degradation rate [27], or a combination of both these processes.The growth-promoting effects of beta adrenergic agonists are not only restricted to normal innervated muscle, but also have been equally confirmed under conditions characterized by the atrophy of constituent muscle fibers such as aging, denervation atrophy, and/or dystrophic conditions. An administration of these agonists to denervated rats not only limited, but also even reversed the process of denervation atrophy [13,19,20,35]. Similarly, an examination of the effects of clenbuterol on dystrophic mice has established that the drug could serve as a valuable adjunct Key words: beta adrenergic agonists, isoproterenol, clenbuterol, gastrocnemius muscle, denervation atrophy, 3-methylhistidine, myofibrillar degeneration. Abstract:The effects of beta adrenergic agonists, clenbuterol (2 mg/kg body weight/d) and isoproterenol (12 mg/kg body weight/d), in normal innervated and denervated rat gastrocnemius muscle were investigated. The daily administration of beta adrenergic agonists to normal innervated rats for a short period (7 d) resulted in the hypertrophy of gastrocnemius as confirmed from the measurement of total tissue protein contents. The development of denervation atrophy witnessed a stimulation in the expression of acid and alkaline phosphatases, pointing to an enhanced myofibrillar degeneration. An administration of beta adrenergic agonists inhibited the expression of raised levels of these enzymes in denervated muscle. A measurement of 3-methylhistidine in muscle revealed a loss of amino acid with the progress in the development of denervation atrophy. Serum and urine samples from denervated rats showed a progressive accumulation of 3-methylhistidine. Clenbuterol and isoproterenol treatment to these rats resulted in an inhibition of 3-methylhistidine accumulation. When 3-methylhistidine was used as a marker of myofibrillar degeneration, the results seemed to suggest that the degeneration of cyto-contractile apparatus accompanying denervation atrophy is attenuated in the presence of beta adrenergic agonists, implying that these sympathomimetic drugs are capable of re...

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Nτ-Methylhistidine content of mixed proteins in various rat tissues

Cited by 125 publications

References 25 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

Protein Turnover With Special Reference to Man

Beta Adrenoceptor Agonists, Clenbuterol, and Isoproterenol Retard Denervation Atrophy in Rat Gastrocnemius Muscle: Use of 3-Methylhistidine as a Marker of Myofibrillar Degeneration.

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