Linked Life Data

18616999

Source:http://linkedlifedata.com/resource/pubmed/id/18616999

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2008-10-17
pubmed:abstractText
Oxidative stress and protein modifications are frequently observed in numerous disease states. Albumin, the major circulating protein in blood, can undergo increased glycoxidation in diabetes. Protein glycoxidation can lead to the formation of advanced glycoxidation end products, which induce various deleterious effects on cells. Herein, we report the effect of glucose or methylglyoxal-induced oxidative modifications on BSA or HSA protein structures and on THP1 monocyte physiology. The occurrence of oxidative modifications was found to be enhanced in glycoxidized BSA and HSA, after determination of their free thiol group content, relative electrophoretic migration, carbonyl content, and antioxidant activities. Cells treated with glycoxidized albumin exhibited an overgeneration of intracellular reactive oxygen species, impairments in proteasomal activities, enhancements in RAGE expression, and an accumulation of carbonylated proteins. These novel observations made in the presence of a range of modified BSA and HSA facilitate the comparison of the glycoxidation extent of albumin with the oxidative stress induced in cultured monocytes. Finally, this study reconfirms the influence of experimental conditions in which AGEs are generated and the concentration levels in experiments designed to mimic pathological conditions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0891-5849
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
45
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
799-812
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Oxidative stresses induced by glycoxidized human or bovine serum albumin on human monocytes.
pubmed:affiliation
Laboratoire de Biochimie et Génétique Moléculaire (LBGM), Université de La Réunion, Saint Denis de La Réunion, 15, avenue René Cassin, BP 7151 Cedex 09, 97715 Saint Denis de La Réunion, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't