Literature DB >> 3425710

Leucine metabolism in perfused rat skeletal muscle during contractions.

D A Hood1, R L Terjung.   

Abstract

An isolated single rat hindlimb muscle preparation was used to examine leucine metabolism during steady-state conditions as a function of metabolic rate (VO2) and leucine concentration. The rates of muscle leucine uptake and leucine oxidation (measured as alpha-decarboxylation) were dependent on leucine delivery. At a physiological leucine concentration (0.1 mM), leucine uptake and alpha-ketoisocaproic acid (KIC) release during rest was 12.8 +/- 0.4 and 1.86 +/- 0.06 nmol.min-1.g-1 g, respectively. Leucine oxidation was 2.35 +/- 0.11 nmol.min-1.g-1 (n = 24) and if fully oxidized could account for only 3-4% of the resting VO2. This fraction was reduced to approximately 1% during contractions. The rate of leucine oxidation progressively increased, up to two to three times above rest (6-7 nmol.min-1.g-1), during contractions of graded frequency (7.5, 15, 30, 45, and 60 tetani/min) in a manner related to the eightfold increase in VO2 of the mixed fiber muscle. The fraction of muscle leucine uptake that was transaminated (i.e., leucine decarboxylation + KIC release) increased from 33% at rest to approximately 60% during contractions. The increase in leucine oxidation during contractions was probably primarily due to the high oxidative fast-twitch, red muscle mass, whose VO2 was estimated to increase up to 24-fold above rest. On the basis of our observed rates of muscle leucine alpha-decarboxylation, it is reasonable to attribute the rates of whole-body leucine oxidation of nontrained individuals during exercise to leucine oxidation by the working muscle.

Entities:  

Mesh:

Substances:

Year:  1987        PMID: 3425710     DOI: 10.1152/ajpendo.1987.253.6.E636

Source DB:  PubMed          Journal:  Am J Physiol        ISSN: 0002-9513


  7 in total

Review 1.  The muscle fiber type-fiber size paradox: hypertrophy or oxidative metabolism?

Authors:  T van Wessel; A de Haan; W J van der Laarse; R T Jaspers
Journal:  Eur J Appl Physiol       Date:  2010-07-03       Impact factor: 3.078

Review 2.  Amino acid metabolism during exercise and following endurance training.

Authors:  D A Hood; R L Terjung
Journal:  Sports Med       Date:  1990-01       Impact factor: 11.136

3.  Administration of endotoxin, tumor necrosis factor, or interleukin 1 to rats activates skeletal muscle branched-chain alpha-keto acid dehydrogenase.

Authors:  M D Nawabi; K P Block; M C Chakrabarti; M G Buse
Journal:  J Clin Invest       Date:  1990-01       Impact factor: 14.808

4.  Regulation of ubiquitin proteasome pathway molecular markers in response to endurance and resistance exercise and training.

Authors:  Renae J Stefanetti; Séverine Lamon; Marita Wallace; Mikkel H Vendelbo; Aaron P Russell; Kristian Vissing
Journal:  Pflugers Arch       Date:  2014-08-08       Impact factor: 3.657

5.  Effect of infusing branched-chain amino acid during incremental exercise with reduced muscle glycogen content.

Authors:  M Varnier; P Sarto; D Martines; L Lora; F Carmignoto; G P Leese; R Naccarato
Journal:  Eur J Appl Physiol Occup Physiol       Date:  1994

6.  Bolus ingestion of individual branched-chain amino acids alters plasma amino acid profiles in young healthy men.

Authors:  Takuya Matsumoto; Koichi Nakamura; Hideki Matsumoto; Ryosei Sakai; Tomomi Kuwahara; Yoshihiro Kadota; Yasuyuki Kitaura; Juichi Sato; Yoshiharu Shimomura
Journal:  Springerplus       Date:  2014-01-17

7.  Iron deficiency causes a shift in AMP-activated protein kinase (AMPK) subunit composition in rat skeletal muscle.

Authors:  John F Merrill; David M Thomson; Shalene E Hardman; Squire D Hepworth; Shelby Willie; Chad R Hancock
Journal:  Nutr Metab (Lond)       Date:  2012-11-21       Impact factor: 4.169

  7 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.