Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-2-1
pubmed:abstractText
Recent evidence provided by the in vivo measure of the activity of phenylalanine hydroxylase in humans indicates that the kidney plays a role greater than previously presumed in phenylalanine conversion to tyrosine, an amino acid which has been considered nonessential so far. Homeostasis of tyrosine pools is only partially restored by a reduced uptake of the same amino acid by splanchnic organs in the well-nourished noncatabolic patient with chronic renal failure. Tyrosine pools in uremia can also be restored by an increase in endogenous net protein catabolism, because it occurs during treatment with nonbiocompatible membranes or during acidosis. However, these are trade-offs that are associated with a progressive decrease in muscle mass. Based on these findings, one can argue that with progressively declining renal function and kidney metabolic activity, the nutritional requirements for tyrosine increase progressively. This mechanism could in part account for the increased protein requirements in dialysis-treated end-stage renal disease patients, as compared with predialysis patients.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1051-2276
pubmed:author
pubmed:copyrightInfo
Copyright 2002 by the National Kidney Foundation, Inc.
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8-16
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
The metabolic conversion of phenylalanine into tyrosine in the human kidney: does it have nutritional implications in renal patients?
pubmed:affiliation
Division of Nephrology, Department of Internal Medicine, University of Genova, Genova, Italy. gari@unige.it
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't