Future

I am looking for some information to convince a doctor to leg a stage 4 cancer patient to supplement glutamine and possibly BCAA's in her diet. Any information would be helpful. Please, the sooner the better.

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milkstud

Why wouldn't he allow it haha?

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RollinsClone

"Oral glutamine ameliorates chemotherapy-induced changes of intestinal permeability and does not interfere with the antitumor effect of chemotherapy in patients with breast cancer: a prospective randomized trial."
ABSTRACT:
AIMS AND BACKGROUND: Sixty patients with breast cancer were randomly assigned to oral glutamine or placebo pre-neoadjuvant chemotherapy (CEF regimen). METHODS AND STUDY DESIGN: Oral glutamine supplementation was continued for at least 12 days. Patients kept a daily record of diarrhea and stomatitis. The plasma glutamine level, intestinal permeability (lactulose-mannitol test), and tumor size were analyzed. The expression of Ki-67 and PCNA antigens in breast carcinoma was assessed. RESULTS: The plasma glutamine level was significantly higher in the glutamine group than in the placebo group (420.39 +/- 52.39 mmol/L vs 309.76 +/- 42.34 mmol/L, P < 0.05). After one cycle of chemotherapy, the lactulose-mannitol ratio was higher in the placebo group than in the glutamine group (0.0630 +/- 0.0091 vs 0.0471 +/- 0.0094, P < 0.05). No differences were observed in the grades of stomatitis and diarrhea, in the changes in tumor size, and in the expression of Ki-67 and PCNA antigens between the two groups. CONCLUSIONS: Prophylactic oral glutamine could ameliorate the neoadjuvant chemotherapy-induced increase in intestinal permeability, but had no significant positive clinical effect on stomatitis and diarrhea and did not interfere with the antitumor effect of chemotherapy.

there's one example that supports the use of glutamine while undergoing chemotherapy.

I will try and get you more when i have time, how long you have future? i may just make it my research paper if you can wait till next thursday for a complete view, and shit loads of facts.

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Future

What you can do man! Thanks. Sooner the better.

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homonunculus

Future,

WRT BCAA's, If you have cancerous cells growing at a high rate and metastasizing (stage 4), shifting towards anabolism might speed the rate of cancer growth more so than prevent muscle loss from chemo.

http://www.ncbi.nlm.nih.gov/pubmed/1...ubmed_RVDocSum

J Nutr. 2006 Jan;136(1 Suppl):237S-42S.Click here to read Links
Investigations of branched-chain amino acids and their metabolites in animal models of cancer.
Baracos VE, Mackenzie ML.

Department of Agricultural, Food, and Nutritional Science, University of Alberta, Edmonton, Alberta, Canada. vickieb@cancerboard.ab.ca

Many of the features of BCAA metabolism in the tumor-bearing state are similar to the other disease states that feature involuntary weight loss and skeletal muscle atrophy. These states are generally characterized by altered BCAA availability (low BCAA intakes, elevated rates of BCAA oxidation, and gluconeogenesis), which are concurrent with activation of proteolysis and suppression of protein synthesis in skeletal muscle and ultimately lead to erosion of lean tissue mass. These features in turn imply BCAA deficiency compared with whole-body requirements and are the basis of suggestions for dietary supplementation with BCAA or their metabolites. Recent studies on BCAA supplementation in cancer focus on leucine and its derivative, beta-methyl beta-hydroxybutyrate, as regulators of skeletal muscle metabolism, although their relative efficacy is unknown. However, what would otherwise be a relatively straightforward consideration of amino acid supply and demand is confounded by the presence of the tumor and its potential utilization of BCAA for its proliferative and invasive activities. Positron emission tomography with (11)C-leucine, used for in vivo tumor imaging, points to the high avidity of tumor amino acid uptake. These features have incited research in opposing directions, probing BCAA deprivation, with a view to limiting tumor growth, as well as BCAA supplementation, with a view to supporting maintenance of host lean tissue. No clear conclusion is presently available from the sum of these efforts. Animal models with relevant clinical features are essential to determine if amino acid therapy can alter the balance between the host and the tumor in a manner that favors the host overall.

-R

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RollinsClone

Little is known about the influence of amino acid imbalance by supplementation of branched-chain amino acids (BCAAs) on human hepatocellular carcinoma (HCC). We investigated the effect of various BCAA concentrations in culture medium on the growth and metabolism of two human HCC cell lines: Hep G2 and KYN-1. DNA and protein syntheses were studied by radiolabeled thymidine and leucine uptake, Amino acid concentrations in cell and medium were measured with an amino acid analyzer. Expression and excretion of transforming growth factor (TGF)-alpha and TGF-beta1 were studied by immunostaining and enzyme linked immunosorbent assay methods. The cell growth was suppressed in media with higher and lower BCAA concentrations than Dulbecco's modified Eagle's medium, and this was grossly correlated with the incorporation of [3H]thymidine into DNA and incorporation of [3H]leucine into intracellular protein. Pretreatment with 10,000 nmol/ml of BCAA did not suppress the cell growth in subsequent culture in the standard Dulbecco's modified Eagle's medium, indicating that the effect of BCAAs was not cytocidal but cytostatic and reversible. BCAA and aromatic amino acid concentrations in cells increased in parallel as the BCAA level in medium was increased, despite the fixed aromatic amino acid level. Intracellular expression and extracellular excretion of TGF-alpha were higher at BCAA concentrations of 100 and 1,000 nmol/ml than at 10 or 1,000 nmol/ml. The present finding that the in vitro growth of HCC can be suppressed by enriched BCAA levels in medium may indicate that amino acid-imbalanced therapy with enriched BCAAs is useful in the treatment of HCC.

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RollinsClone

Experimental model in rats:

The purpose of this study was to determine whether a branched chain amino acids (BCAA) enriched intravenous feeding would have an effect on nitrogen retention in the host tissue, without stimulating tumor growth in the malignant tumor bearing animal. NEDH/c rats with an implanted fibrosarcoma were put on one of two total parenteral nutrition regimens, one of an amino acid formula containing 25 per cent BCAA, by weight and the other containing 50 per cent BCAA. Nitrogen retention in the two tumor-bearing groups was similar, although it was 47 per cent greater than observed in the non-tumor bearing animals (p less than 0.05). Skeletal protein synthesis was significantly reduced by the presence of the tumor in rats on the 25 per cent BCAA formula (from 10.1 per cent/day to 6.1 per cent/day) but was increased to 7.9 per cent/day by the 50 per cent BCAA formula. The BCAA enriched intravenous feeding does not enhance tumor growth and supports skeletal protein synthesis, at least in this experimental model.

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RollinsClone

This abstract gives a bunch of data facts but sums it up at the end (in bold)

A prospective randomized trial was conducted to determine the effects of branched chain amino acids (BCAA) as the protein component of total parenteral nutrition (TPN) on protein kinetics in patients with intraabdominal adenocarcinoma. Nine malnourished patients were given both conventional TPN containing 19 per cent BCAA (AA) and isocaloric, isonitrogenous TPN containing 50 per cent BCAA (BCAA-TPN), in random order. Both [13C]leucine and [14C]tyrosine were employed as tracers to avoid the potential bias due to the different amino acid composition of the two TPN solutions. With BCAA-TPN, leucine and tyrosine flux increased significantly from (mean +/- s.d.) 158.0 +/- 37.2 to 243.5 +/- 75.8 mumol kg-1 h-1 (P less than 0.025) and from 35.0 +/- 8.4 to 42.6 +/- 11.0 mumol kg-1 h-1 (P less than 0.05) respectively. Leucine oxidation was significantly higher on BCAA-TPN (24.1 +/- 6.3 on AA versus 68.3 +/- 37.1 mumol kg-1 h-1, P less than 0.025) while tyrosine oxidation was significantly lower (3.7 +/- 1.8 mumol kg-1 h-1 on AA versus 2.5 +/- 2.0 mumol kg-1 h-1 on BCAA-TPN, P less than 0.05). Whole body protein synthesis and breakdown was significantly higher on BCAA-TPN by the tyrosine tracer (31.3 +/- 7.3 on AA versus 40.1 +/- 9.3 mumol kg-1 h-1, P less than 0.025 and 33.0 +/- 8.4 on AA versus 41.3 +/- 11.1 mumol kg-1 h-1, P less than 0.05) respectively. Using the leucine tracers both synthesis and breakdown were increased, but not significantly, from 133.8 +/- 40.0 to 175.3 +/- 65.1 mumol kg-1 h-1 and from 127.9 +/- 33.6 to 167.7 +/- 71.2 mumol kg-1 h-1 respectively. The fractional albumin synthetic rate increased significantly on BCAA-TPN from 4.3 +/- 2.9 on AA to 8.0 +/- 5.1 per cent per day (P less than 0.05). The reduction in tyrosine oxidation, suggesting improved protein utilization, coupled with an increase in protein and albumin synthesis, strongly support a positive benefit from BCAA-TPN in cancer cachexia

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RollinsClone

thats all for today, will find more tomorrow. If anyone has any IL1s effect on lipid metabolism research I'll gladly trade them!

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