Linked Life Data

19708990

Source:http://linkedlifedata.com/resource/pubmed/id/19708990

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2009-8-27
pubmed:abstractText
Analysis of tissues, plasma, urine, other body fluids, and dialysate for glycation adducts has revealed the presence of two major forms: glycation adduct residues of proteins and related glycated amino acids--called glycation free adducts. The major effect on protein glycation in uremia is loss of clearance of glycation free adducts and their marked increase in plasma. Changes in glycation adduct residue content of plasma protein in uremia is, in contrast, relatively modest. There is now doubt as to whether the concept of interaction of advanced glycation endproduct (AGE)-modified proteins with putative AGE receptors can be sustained in vivo. A residual important feature of the receptor for AGEs may be decrease in expression of glyoxalase 1 of the antiglycation defence by S100A12 protein leaving the vasculature vulnerable to dicarbonyl stress and related AGE formation. The dicarbonyl proteome, proteins susceptible to dicarbonyl glycation at functional sites, is the likely mediator of glycation damage in uremia. Glycation of type IV collagen with shedding of endothelial cells and glycation of apolipoprotein B100 with increased atherogenicity of low density lipoprotein are two examples which may link protein glycation to increased risk of cardiovascular disease in end-stage renal disease.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1525-139X
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
400-4
pubmed:meshHeading
pubmed:articleTitle
Highlights and hotspots of protein glycation in end-stage renal disease.
pubmed:affiliation
Protein Damage and Systems Biology Research Group, Clinical Sciences Research Institute, Warwick Medical School, University Hospital, University of Warwick, Coventry, United Kingdom. P.J.Thornalley@warwick.ac.uk
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't