Linked Life Data

16825015

Source:http://linkedlifedata.com/resource/pubmed/id/16825015

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2006-7-7
pubmed:abstractText
Cellular and extracellular proteins suffer significant damage in vivo by glycation. Physiological proteolysis of proteins damaged by glycation forms glycation free adducts that are released into plasma for urinary excretion. Inefficient elimination of these free adducts in uremia leads to their accumulation. In mild renal insufficiency, plasma glycation free adducts accumulated as renal clearance declined. In patients with end-stage renal disease, plasma glycation free adducts were increased up to 18-fold on peritoneal dialysis and up to 40-fold on hemodialysis. Glycation free adduct concentrations in peritoneal dialysate increased with dialysate dwell time, achieving concentrations in the dialysate higher than in plasma--suggesting that glycation adduct formation may occur in the peritoneal cavity and active transport into the peritoneal cavity may occur. In hemodialysis, plasma glycation free adducts equilibrated rapidly across the dialysis membrane, with both plasma and dialysate concentrations decreasing during a dialysis session. Therefore, protein glycation free adducts normally excreted efficiently in urine show profound mishandling and accumulation in chronic renal failure. Their accumulation may impair vascular cell function and contribute to morbidity and mortality in renal disease.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1532-8503
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
178-84
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Advanced glycation end products in renal failure.
pubmed:affiliation
Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex, UK. thorp@essex.ac.uk
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't