Literature DB >> 7908865

Tumour and host tissue responses to branched-chain amino acid supplementation of patients with cancer.

M A McNurlan1, S D Heys, K G Park, J Broom, D S Brown, O Eremin, P J Garlick.   

Abstract

1. Rates of protein synthesis have been measured from the incorporation of 57 mg of L-[1-13C]leucine/kg for 90 min into muscle tissue and colorectal tumours removed at surgery from cancer patients. 2. For the 20 h preceding surgery and during the measurement of protein synthesis, the patients received intravenous saline, conventional intravenous nutrition (0.2 g of N and 103 non-protein kJ/kg body weight) or intravenous nutrition enriched with the branched-chain amino acids leucine, isoleucine and valine (0.2 g of N with 30% from branched-chain amino acids and 103 non-protein kJ/kg body weight). 3. Conventional intravenous nutrition resulted in a significant stimulation of the rate of protein synthesis in both muscle tissue (2.64 +/- 0.75%/day versus 1.78 +/- 0.51%/day in saline control, means +/- SD) and tumour tissue (43.9 +/- 10.3%/day versus 22.6 +/- 5.6%/day in saline control). 4. Pre-operative nutrition enriched with branched-chain amino acids was less effective than conventional intravenous nutrition in stimulating protein synthesis in both muscle and tumour. The rates of protein synthesis were 2.12 +/- 0.41%/day in muscle and 33.7 +/- 5.3%/day in the tumours. 5. The expression of proliferating cell nuclear antigen in sections of the tumours showed changes with intravenous feeding of the two different amino acid mixtures that were similar to the changes in protein synthesis, and these two variables were significantly correlated. This is evidence that feeding with conventional mixtures and mixtures enriched with branched-chain amino acids stimulates tumour growth.(ABSTRACT TRUNCATED AT 250 WORDS)

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Year:  1994        PMID: 7908865     DOI: 10.1042/cs0860339

Source DB:  PubMed          Journal:  Clin Sci (Lond)        ISSN: 0143-5221            Impact factor:   6.124


  7 in total

1.  Glucose regulates protein catabolism in ras-transformed fibroblasts through a lysosomal-dependent proteolytic pathway.

Authors:  C Tournu; A Obled; M P Roux; M Ferrara; S Omura; D M Béchet
Journal:  Biochem J       Date:  2001-07-01       Impact factor: 3.857

Review 2.  Observations of branched-chain amino acid administration in humans.

Authors:  Dwight E Matthews
Journal:  J Nutr       Date:  2005-06       Impact factor: 4.798

Review 3.  Effects of leucine-rich protein supplements on anthropometric parameter and muscle strength in the elderly: a systematic review and meta-analysis.

Authors:  B Komar; L Schwingshackl; G Hoffmann
Journal:  J Nutr Health Aging       Date:  2015-04       Impact factor: 4.075

4.  Effect of glucagon on protein synthesis in human rectal cancer in situ.

Authors:  W H Hartl; H Demmelmair; K W Jauch; B Koletzko; F W Schildberg
Journal:  Ann Surg       Date:  1998-03       Impact factor: 12.969

Review 5.  Inflammatory burden and amino acid metabolism in cancer cachexia.

Authors:  William J Durham; Edgar Lichar Dillon; Melinda Sheffield-Moore
Journal:  Curr Opin Clin Nutr Metab Care       Date:  2009-01       Impact factor: 4.294

6.  Leucine supplementation differentially enhances pancreatic cancer growth in lean and overweight mice.

Authors:  Kristyn A Liu; Laura M Lashinger; Audrey J Rasmussen; Stephen D Hursting
Journal:  Cancer Metab       Date:  2014-03-31

Review 7.  Non-surgical oncology - Guidelines on Parenteral Nutrition, Chapter 19.

Authors:  J Arends; G Zuercher; A Dossett; R Fietkau; M Hug; I Schmid; E Shang; A Zander
Journal:  Ger Med Sci       Date:  2009-11-18
  7 in total

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