rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
8
|
pubmed:dateCreated |
2007-7-26
|
pubmed:abstractText |
Oxidative damage to proteins, lipids, and DNA has been suggested to be a mechanism for age-related macular degeneration (AMD). The retina is particularly susceptible to lipid peroxidation due to high concentrations of easily oxidized polyunsaturated fatty acids in the presence of abundant oxygen. One of the most toxic products of lipid peroxidation, 4-hydroxy-2-nonenal (HNE), can modify and inactivate proteins. The hypothesis was that 4-HNE-modified proteins would accumulate and serve as a marker for progressive stages of AMD.
|
pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0146-0404
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
48
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
3469-79
|
pubmed:dateRevised |
2010-6-17
|
pubmed:meshHeading |
pubmed-meshheading:17652714-Adult,
pubmed-meshheading:17652714-Aged,
pubmed-meshheading:17652714-Aged, 80 and over,
pubmed-meshheading:17652714-Aging,
pubmed-meshheading:17652714-Aldehydes,
pubmed-meshheading:17652714-Animals,
pubmed-meshheading:17652714-Biological Markers,
pubmed-meshheading:17652714-Blotting, Western,
pubmed-meshheading:17652714-Disease Progression,
pubmed-meshheading:17652714-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:17652714-Female,
pubmed-meshheading:17652714-Humans,
pubmed-meshheading:17652714-Lipid Peroxidation,
pubmed-meshheading:17652714-Macular Degeneration,
pubmed-meshheading:17652714-Male,
pubmed-meshheading:17652714-Middle Aged,
pubmed-meshheading:17652714-Oxidative Stress,
pubmed-meshheading:17652714-Rats,
pubmed-meshheading:17652714-Rats, Inbred F344,
pubmed-meshheading:17652714-Sensitivity and Specificity,
pubmed-meshheading:17652714-Spectrometry, Mass, Matrix-Assisted Laser...
|
pubmed:year |
2007
|
pubmed:articleTitle |
Age-related macular degeneration and retinal protein modification by 4-hydroxy-2-nonenal.
|
pubmed:affiliation |
Department of Biochemistry, University of Minnesota, Minneapolis, Minnesota, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|