Protein breakdown on whole-body and organ level in non-cachectic tumour-bearing mice undergoing surgery

Clinical Nutrition

Volumn 26, Issue 4, 2007, Pages 483-490

  Vissers, Yvonne L J ^a   von Meyenfeldt, Maarten F ^a   Argilés, Josep M ^b   Luiking, Yvette C ^a   Dejong, Cornelis H C ^a   Deutz, Nicolaas E P ^a  

^a MAASTRICHT UNIVERSITY MEDICAL CENTER   (Netherlands)

^b UNIVERSITY OF BARCELONA   (Spain)

Author keywords

Amino acid; Body composition; Cancer; Myofibrillar protein; Proteasome; Protein breakdown; Stable isotopes; Surgery

Indexed keywords

3 METHYLHISTIDINE; ADENOSINE TRIPHOSPHATE; CHYMOTRYPSIN; ISOTOPE; MUSCLE PROTEIN; PHENYLALANINE; PROTEASOME; PROTEIN; UBIQUITIN;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; BODY COMPOSITION; CANCER SURGERY; CONTROLLED STUDY; INTESTINE; KIDNEY; LAPAROTOMY; LIVER; MALE; MALIGNANT NEOPLASTIC DISEASE; MOUSE; MUSCLE; NONHUMAN; ORGAN; POSTOPERATIVE PERIOD; PROTEIN DEGRADATION; SARCOMA; STEADY STATE;

ANIMALS; BODY COMPOSITION; ENERGY METABOLISM; INTESTINES; KIDNEY; LAPAROTOMY; LIVER; MALE; METHYLHISTIDINES; MICE; MUSCLE PROTEINS; MUSCLE, SKELETAL; MYOFIBRILS; NEOPLASMS, EXPERIMENTAL; ORGAN SPECIFICITY; POSTOPERATIVE PERIOD; PROTEINS; RANDOM ALLOCATION;

EID: 34447639238     PISSN: 02615614     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.clnu.2007.03.005     Document Type: Article

References (38)

1. de Blaauw I., Deutz N.E.P., and von Meyenfeldt M.F. Cancer reduces the metabolic response of muscle to surgical stress in the rat. J Surg Res 80 1 (1998) 94-101
2. de Blaauw I., Deutz N.E.P., Hulsewé K.W.E., et al. Attenuated metabolic response to surgery in tumor-bearing rats. J Surg Res 110 2 (2003) 371-377
3. Jeevanandam M., Horowitz G.D., Lowry S.F., et al. Cancer cachexia and protein metabolism. Lancet 1 8392 (1984) 1423-1426
4. Norton J.A., Stein T.P., and Brennan M.F. Whole body protein synthesis and turnover in normal man and malnourished patients with and without known cancer. Ann Surg 194 2 (1981) 123-128
5. Vissers Y.L.J., von Meyenfeldt M.F., Braulio V.B., et al. Measuring actin-myosin protein breakdown in mice using a primed constant stable isotope infusion protocol. Clin Sci 104 6 (2003) 585-590
6. Boyland E., and Warren F. The induction of tumours by methylcholantrene in two strains of mice. J Pathol Bacteriol 45 (1937) 171-177
7. Lundholm K., Edstrom S., Ekman L., et al. A comparative study of the influence of malignant tumor on host metabolism in mice and man: evaluation of an experimental model. Cancer 42 2 (1978) 453-461
8. Hallemeesch M.M., ten Have G.A.M., and Deutz N.E.P. Metabolic flux measurements across portal drained viscera, liver, kidney and hindquarter in mice. Lab Anim 35 (2001) 101-110
9. van Eijk H.M.H., Rooyakkers D.R., and Deutz N.E.P. 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 (1993) 143-148
10. van Eijk H.M., Rooyakkers D.R., Soeters P.B., et al. Determination of amino acid isotope enrichment using liquid chromatography-mass spectrometry. Anal Biochem 271 1 (1999) 8-17
11. Wolfe R.R. Radioactive and stable isotope tracers in biomedicine. Principles and practice of kinetic analysis (1992), Wiley-Liss, Inc., New York
12. Hallemeesch M.M., Soeters P.B., and Deutz N.E.P. Renal arginine and protein synthesis are increased during early endotoxemia in mice. Am J Physiol Renal Physiol 282 2 (2002) F316-F323
13. Ruderman N.B., Houghton C.R.S., and Hems R. Evaluation of the isolated perfused rat hindquarter for the study of muscle metabolism. Biochem J 124 (1971) 639-651
14. Bruins M.J., Soeters P.B., and Deutz N.E.P. Endotoxemia affects organ protein metabolism differently during prolonged feeding in pigs. J Nutr 130 12 (2000) 3003-3013
15. Orino E., Tanaka K., Tamura T., et al. ATP-dependent reversible association of proteasomes with multiple protein components to form 26S complexes that degrade ubiquitinated proteins in human HL-60 cells. FEBS Lett 284 2 (1991) 206-210
16. Whitehouse A.S., Smith H.J., Drake J.L., et al. Mechanism of attenuation of skeletal muscle protein catabolism in cancer cachexia by eicosapentaenoic acid. Cancer Res 61 9 (2001) 3604-3609
17. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
18. McCabe B.J., and Previs S.F. Using isotope tracers to study metabolism: application in mouse models. Metab Eng 6 (2004) 25-35
19. Dawson N.J., Stephenson S.K., and Fredline D.K. Body composition of mice subjected to genetic selection for different body proportions. Comp Biochem Physiol B 42 4 (1972) 679-691
20. SPSS I. SPSS for Windows Version 11.0.1. 1st ed (2001), SPSS Inc., Chicago
21. Murray A.J., Nield M.K., Jones L.M., et al. Metabolism of N tau-methylhistidine by mice. Biochem J 232 2 (1985) 409-413
22. Harris C.I., Rucklidge G.J., McDiarmid R.M., et al. Sex- and phenotype-dependent metabolism of N tau-methylhistidine by mice. Biochem J 239 1 (1986) 229-232
23. Lundholm K., Bennegard K., Eden E., et al. Efflux of 3-methylhistidine from the leg in cancer patients who experience weight loss. Cancer Res 42 11 (1982) 4807-4811
24. Rennie M.J., and Millward D.J. 3-Methylhistidine excretion and the urinary 3-methylhistidine/creatinine ratio are poor indicators of skeletal muscle protein breakdown. Clin Sci 65 3 (1983) 217-225
25. Eyden B. The myofibroblast: a study of normal, reactive and neoplastic tissues, with an emphasis on ultrastructure. Part 2-tumours and tumour-like lesions. J Submicrosc Cytol Pathol 37 3-4 (2005) 231-296
26. Melville S., McNurlan M.A., Calder A.G., et al. Increased protein turnover despite normal energy metabolism and responses to feeding in patients with lung cancer. Cancer Res 50 4 (1990) 1125-1131
27. Lazarus D.D., Destree A.T., Mazzola L.M., et al. A new model of cancer cachexia: contribution of the ubiquitin- proteasome pathway (in process citation). Am J Physiol 277 2, Part 1 (1999) E332-E341
28. Temparis S., Asensi M., Taillandier D., et al. Increased ATP-ubiquitin-dependent proteolysis in skeletal muscles of tumor-bearing rats. Cancer Res 54 21 (1994) 5568-5573
29. Costelli P., Garcia-Martinez C., Llovera M., et al. Muscle protein waste in tumor-bearing rats is effectively antagonized by a beta 2-adrenergic agonist (clenbuterol). Role of the ATP-ubiquitin- dependent proteolytic pathway. J Clin Invest 95 5 (1995) 2367-2372
30. Williams A., Sun X., Fischer J.E., et al. The expression of genes in the ubiquitin-proteasome proteolytic pathway is increased in skeletal muscle from patients with cancer. Surgery 126 4 (1999) 744-749 [Discussion 49-50]
31. Jagoe R.T., Redfern C.P., Roberts R.G., et al. Skeletal muscle mRNA levels for cathepsin B, but not components of the ubiquitin-proteasome pathway, are increased in patients with lung cancer referred for thoracotomy. Clin Sci (Lond) 102 3 (2002) 353-361
32. Khal J., Hine A.V., Fearon K.C., et al. Increased expression of proteasome subunits in skeletal muscle of cancer patients with weight loss. Int J Biochem Cell Biol 37 10 (2005) 2196-2206
33. Khal J., Wyke S.M., Russell S.T., et al. Expression of the ubiquitin-proteasome pathway and muscle loss in experimental cancer cachexia. Br J Cancer 93 7 (2005) 774-780
34. Lowell B.B., Ruderman N.B., and Goodman M.N. Evidence that lysosomes are not involved in the degradation of myofibrillar proteins in rat skeletal muscle. Biochem J 234 1 (1986) 237-240
35. Lee V.M., Hansen R.J., Wolfe B.M., et al. Muscle protein metabolism of rats in surgical trauma. J Parenter Enteral Nutr 12 5 (1988) 445-451
36. Carli F., Ramachandra V., Gandy J., et al. Effect of general anaesthesia on whole body protein turnover in patients undergoing elective surgery. Br J Anaesth 65 3 (1990) 373-379
37. Clague M.B., Keir M.J., Wright P.D., et al. The effects of nutrition and trauma on whole-body protein metabolism in man. Clin Sci (Lond) 65 2 (1983) 165-175
38. Waterlow J.C., Golden J., and Picou D. The measurements of rates of protein turnover, synthesis, and breakdown in man and the effects of nutritional status and surgical injury. Am J Clin Nutr 30 8 (1977) 1333-1339