![[Feedback]](/icons/banner/feedbackACT.gif){kind=icon}
![[For Subscribers]](/icons/banner/subscriberACT.gif){kind=icon}
![[Archive]](/icons/banner/archiveACT.gif){kind=icon}
![[Search]](/icons/banner/searchACT.gif){kind=icon}
![[Contents]](/icons/banner/tocACT.gif){kind=icon}
|
|
|
|
|
||
Department of Surgery, Maastricht University, 6200 MD, Maastricht, The Netherlands
3 To whom correspondence should be addressed. E-mail: pb.soeters{at}ah.unimaas.nl.
Amino acid utilization and, therefore, demand differ between the healthy state and various disease states. In the healthy state most circulating amino acids are derived from dietary proteins that are stored and broken down in the gut and released gradually into the portal circulation, and from continuous turnover of body protein. In disease states, the amino acid composition of amino acids derived from periferal protein breakdown and released in the circulation, is different, for example because a substantial part of the branched-chain amino acids is broken down to yield glutamine and alanine, which are released in the circulation. It appears to be advantageous to mimic this continuous autoinfusion in patients, dependent of parenteral of enteral tube feeding. In disease, different endpoints should be used to assess the adequacy of the administered amino acid mix. Maintenance of a positive nitrogen balance and growth is less important than support of wound healing and immune function. Several amino acids such as glutamine, cysteine, and taurine are shown or suggested to be conditionally essential in disease, and to form substrate in the stressed patient for anabolic processes in liver, immune system, and injured sites. Amino acid toxicity is rare, and protein restriction for patients with renal or liver failure is obsolete because this only aggravated malnutrition. A true example of protein toxicity consists of gastrointestinal hemorrhage that precipitates hepatic encephalopathy in liver insufficiency, most likely because hemoglobin is an unbalanced protein because it lacks the essential amino acid isoleucine.
KEY WORDS: • nutrition • supplementation • amino acid toxicity • stress • disease
This article has been cited by other articles:
|
|
 |
|
  V. C. Taveira, M. R. C. G. Novaes, M. dos Anjos Reis, and M. F. da Silva Hematologic and Metabolic Effects of Dietary Supplementation with Agaricus sylvaticus Fungi on Rats Bearing Solid Walker 256 Tumor Experimental Biology and Medicine, November 1, 2008; 233(11): 1341 - 1347. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 E. Roth Nonnutritive Effects of Glutamine J. Nutr., October 1, 2008; 138(10): 2025S - 2031S. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Kidd, I. M. Modlin, B. I. Gustafsson, I. Drozdov, O. Hauso, and R. Pfragner Luminal regulation of normal and neoplastic human EC cell serotonin release is mediated by bile salts, amines, tastants, and olfactants Am J Physiol Gastrointest Liver Physiol, August 1, 2008; 295(2): G260 - G272. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. S. Hughes, P. Kazmier, T. A. Burd, J. Anglen, A. M. Stoker, K. Kuroki, W. L. Carson, and J. L. Cook Enhanced Fracture and Soft-Tissue Healing by Means of Anabolic Dietary Supplementation J. Bone Joint Surg. Am., November 1, 2006; 88(11): 2386 - 2394. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 V. H. Castellanos, M. D. Litchford, and W. W. Campbell Modular Protein Supplements and Their Application to Long-Term Care Nutr Clin Pract, October 1, 2006; 21(5): 485 - 504. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. C. G. van de Poll, C. H. C. Dejong, and P. B. Soeters Adequate Range for Sulfur-Containing Amino Acids and Biomarkers for Their Excess: Lessons from Enteral and Parenteral Nutrition J. Nutr., June 1, 2006; 136(6): 1694S - 1700S. [Abstract] [Full Text] [PDF]
|
|
