Measuring whole-body actin/myosin protein breakdown in mice using a primed constant stable isotope-infusion protocol

Clinical Science

Volumn 104, Issue 6, 2003, Pages 585-590

  Vissers, Yvonne L J ^a   Von Meyenfeldt, Maarten F ^a   Braulio, Valeria B ^a   Luiking, Yvette C ^a   Deutz, Nicolaas E P ^a  

^a MAASTRICHT UNIVERSITY   (Netherlands)

Author keywords

3 methylhistidine; Lipopolysaccharide; Protein metabolism; Starvation

Indexed keywords

3 METHYLHISTIDINE; 3 METHYLHISTIDINE H 3; ACTIN; DEUTERIUM; LIPOPOLYSACCHARIDE; MUSCLE PROTEIN; MYOSIN; PHENYL 2 PHENYLALANINE H 5; PHENYL 2 TYROSINE H 2; STABLE ISOTOPE; TRACER; TRITIUM; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; DRUG BLOOD LEVEL; ISOTOPE LABELING; LIQUID CHROMATOGRAPHY; MALE; MASS SPECTROMETRY; MEASUREMENT; METHODOLOGY; MODEL; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN METABOLISM; STARVATION; WHOLE BODY COUNTING;

ACTINS; ANIMALS; BODY WEIGHT; CHROMATOGRAPHY, LIQUID; DEUTERIUM; INFUSIONS, INTRAVENOUS; LIPOPOLYSACCHARIDES; MALE; MASS SPECTROMETRY; METHYLHISTIDINES; MICE; MICE, INBRED STRAINS; MODELS, ANIMAL; MUSCLES; MYOSINS; PHENYLALANINE; RADIOACTIVE TRACERS; STARVATION; TYROSINE;

EID: 0037565041     PISSN: 01435221     EISSN: None     Source Type: Journal    
DOI: 10.1042/CS20020283     Document Type: Article

References (42)

1. Young, V. R., Alexis, S. D., Baliga, B. S., Munro, H. N. and Muecke, W. (1972) Metabolism of administered 3-methylhistidine. Lack of muscle transfer ribonucleic acid charging and quantitative excretion as 3-methylhistidine and its N-acetyl derivative. J. Biol. Chem. 247, 3592-3600
2. τ-methylhistidine (3-methylhistidine) and muscle protein turnover: an overview. Fed. Proc. 37, 2291-2300
3. Nissen, S. (1997) Measurement of muscle proteolysis and the impact on muscle wasting. Proc. Nutr. Soc. 56, 793-799
4. Milne, G. and Harris, C. I. (1978) The inadequacy of urinary 3-methylhistidine excretion as an index of muscle protein degradations in the pig. Proc. Nutr. Soc. 37, 18A
5. Ballard, F. J. and Tomas, F. M. (1983) 3-Methylhistidine as a measure of skeletal muscle protein breakdown in human subjects: the case for its continued use. Clin. Sci. 65, 209-215
6. τ-methylhistidine by mice. Biochem. J. 232, 409-413
7. τ-methylhistidine by mice. Biochem. J. 239, 229-232
8. Wolfe, R. R. (1992) Radioactive and Stable Isotope Tracers in Biomedicine. Principles and Practice of Kinetic Analysis. Wiley-Liss, New York
9. Moldawer, L. L., Kawamura, I., Bistrian, B. R. and Blackburn, G. L. (1983) The contribution of phenylalanine to tyrosine metabolism in vivo. Studies in the post-absorptive and phenylalanine-loaded rat. Biochem. J. 210, 811-817
10. 5]phenylalanine model. Am. J. Physiol. 256, E631-E639
11. Waldegrave, W. (1986) Guide for the Care and Use of Laboratory Animals, EEC, publication 86/609
12. ter Steege, J. C., van de Ven, M. W., Forget, P. P., Brouckaert, P. and Buurman, W. A. (1998) The role of endogenous IFN-γ, TNF-α and IL-10 in LPS-induced nitric oxide release in a mouse model. Cytokine 10, 115-123
13. Hallemeesch, M. M., ten Have, G. A. M. and Deutz, N. E. P. (2001) Metabolic flux measurements across portal drained viscera, liver, kidney and hindquarter in mice. Lab. Anim. 35, 101-110
14. van Eijk, H. M. H., Rooyakkers, D. R. and Deutz, N. E. P. (1993) Rapid routine determination of amino acids in plasma by high-performance liquid chromatography with a 2-3 μm Spherisorb ODS II column. J. Chromatogr. 620, 143-148
15. van Eijk, H. M., Rooyakkers, D. R., Soeters, P. B. and Deutz, N. E. P. (1999) Determination of amino acid isotope enrichment using liquid chromatography-mass spectrometry. Anal. Biochem. 271, 8-17
16. Bates, P. C., Grimble, G. K., Sparrow, M. P. and Millward, D. J. (1983) Myofibrillar protein turnover. Synthesis of protein-bound 3-methylhistidine, actin, myosin heavy chain and aldolase in rat skeletal muscle in the fed and starved states. Biochem. J. 214, 593-605
17. Reference deleted
18. Rathmacher, J. A. and Nissen, S. L. (1998) Development and application of a compartmental model of 3-methylhistidine metabolism in humans and domestic animals. Adv. Exp. Med. Biol. 445, 303-324
19. Goodman, M. N. and Ruderman, N. B. (1980) Starvation in the rat. I. Effect of age and obesity on organ weights, RNA, DNA, and protein. Am. J. Physiol. 239, E269-E276
20. Mosoni, L., Malmezat, T., Valluy, M. C., Houlier, M. L., Attaix, D. and Mirand, P. P. (1999) Lower recovery of muscle protein lost during starvation in old rats despite a stimulation of protein synthesis. Am. J. Physiol. 277, E608-E616
21. Lowell, B. B., Ruderman, N. B. and Goodman, M. N. (1986) Regulation of myofibrillar protein degradation in rat skeletal muscle during brief and prolonged starvation. Metab., Clin. Exp. 35, 1121-1127
22. Kadowaki, M., Harada, N., Takahashi, S., Noguchi, T. and Naito, H. (1989) Differential regulation of the degradation of myofibrillar and total proteins in skeletal muscle of rats: effects of streptozotocin-induced diabetes, dietary protein and starvation. J. Nutr. 119, 471-477
23. Dice, J. F. (1987) Molecular determinants of protein half-lives in eukaryotic cells. FASEB J. 1, 349-357
24. Mortimore, G. E., Poso, A. R. and Lardeux, B. R. (1989) Mechanism and regulation of protein degradation in liver. Diabetes Metab. Rev. 5, 49-70
25. Medina, R., Wing, S. S. and Goldberg, A. L. (1995) Increase in levels of polyubiquitin and proteasome mRNA in skeletal muscle during starvation and denervation atrophy. Biochem. J. 307, 631-637
26. Medina, R., Wing, S. S., Haas, A. and Goldberg, A. L. (1991) Activation of the ubiquitin-ATP-dependent proteolytic system in skeletal muscle during fasting and denervation atrophy. Biomed. Biochim. Acta 50, 347-356
27. Wing, S. S., Haas, A. L. and Goldberg, A. L. (1995) Increase in ubiquitin-protein conjugates concomitant with the increase in proteolysis in rat skeletal muscle during starvation and atrophy denervation. Biochem. J. 307, 639-645
28. Lowell, B. B., Ruderman, N. B. and Goodman, M. N. (1986) Evidence that lysosomes are not involved in the degradation of myofibrillar proteins in rat skeletal muscle. Biochem. J. 234, 237-240
29. Tiao, G., Hobler, S., Wang, J. J. et al. (1997) Sepsis is associated with increased mRNAs of the ubiquitin-proteasome proteolytic pathway in human skeletal muscle. J. Clin. Invest. 99, 163-168
30. Tiao, G., Fagan, J. M., Samuels, N. et al. (1994) Sepsis stimulates nonlysosomal, energy-dependent proteolysis and increases ubiquitin mRNA levels in rat skeletal muscle. J. Clin. Invest. 94, 2255-2264
31. Solomon, V., Baracos, V., Sarraf, P. and Goldberg, A. L. (1998) Rates of ubiquitin conjugation increase when muscles atrophy, largely through activation of the N-end rule pathway. Proc Natl. Acad. Sci. U.S.A. 95, 12602-12607
32. Hobler, S. C., Williams, A., Fischer, D. et al. (1999) Activity and expression of the 20S proteasome are increased in skeletal muscle during sepsis. Am. J. Physiol. 277, R434-R440
33. Hallemeesch, M. M. (2001) Role of arginine in endotoxemia. Studies in mice with reduced arginine availability. PhD Thesis, Maastricht University, The Netherlands
34. Tracey, K. J., Legaspi, A., Albert, J. D. et al. (1988) Protein and substrate metabolism during starvation and parenteral refeeding. Clin. Sci. 74, 123-132
35. Goodman, M. N., McElaney, M. A. and Ruderman, N. B. (1981) Adaptation to prolonged starvation in the rat: curtailment of skeletal muscle proteolysis. Am. J. Physiol. 241, E321-E327
36. Sjolin, J., Stjernstrom, H., Arturson, G., Andersson, E., Friman, G. and Larsson, J. (1989) Exchange of 3-methylhistidine in the splanchnic region in human infection. Am. J. Clin. Nutr. 50, 1407-1414
37. Rennie, M. J. and Millward, D. J. (1983) 3-Methylhistidine excretion and the urinary 3-methylhistidine/creatinine ratio are poor indicators of skeletal muscle protein breakdown. Clin. Sci. 65, 217-225
38. τ-methylhistidine and creatine in human urine. Biochem. J. 200, 449-452
39. Lundholm, K., Bennegard, K., Eden, E., Svaninger, G., Emery, P. W. and Rennie, M. J. (1982) Efflux of 3-methylhistidine from the leg in cancer patients who experience weight loss. Cancer Res. 42, 4807-4811
40. Brenner, U., Herbertz, L., Thul, P. et al. (1987) The contribution of small gut to the 3-methylhistidine metabolism in the adult rat. Metab., Clin. Exp. 36, 416-418
41. τ-methylhistidine release: contributions of rat skeletal muscle, GI tract, and skin. Am. J. Physiol. 243, E293-E297
42. Millward, D. J. and Bates, P. C. (1983) 3-Methylhistidine turnover in the whole body, and the contribution of skeletal muscle and intestine to urinary 3-methylhistidine excretion in the adult rat. Biochem. J. 214, 607-615