Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2009-9-14
pubmed:abstractText
The primary function of the eye lens is to focus light on the retina. The major proteins in the lens--alpha, beta, and gamma-crystallins--are constantly subjected to age-related changes such as oxidation, deamidation, truncation, glycation, and methylation. Such age-related modifications are cumulative and affect crystallin structure and function. With time, the modified crystallins aggregate, causing the lens to increasingly scatter light on the retina instead of focusing light on it and causing the lens to lose its transparency gradually and become opaque. Age-related lens opacity, or cataract, is the major cause of blindness worldwide. We review deamidation, and glycation that occur in the lenses during aging keeping in mind the structural and functional changes that these modifications bring about in the proteins. In addition, we review proteolysis and discuss recent observations on how crystallin fragments generated in vivo, through their anti-chaperone activity may cause crystallin aggregation in aging lenses. We also review hyperbaric oxygen treatment induced guinea pig and 'humanized' ascorbate transporting mouse models as suitable options for studies on age-related changes in lens proteins.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:volume
1790
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1095-108
pubmed:dateRevised
2011-5-30
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Lens aging: effects of crystallins.
pubmed:affiliation
Department of Ophthalmology, University of Missouri-Columbia, 1 Hospital Drive, Columbia, MO 65212, USA. sharmak@health.missouri.edu
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural