Linked Life Data

20536835

Source:http://linkedlifedata.com/resource/pubmed/id/20536835

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2010-6-11
pubmed:abstractText
Aging is a complex process accompanied by a decreased capacity of cells to cope with random molecular damages. Damaged proteins can form aggregates and have cytotoxic properties, a feature of many age-associated diseases. Small Hsps are chaperones involved in the refolding and/or disposal of protein aggregates. In Drosophila melanogaster, the mitochondrial DmHsp22 is preferentially upregulated during aging. Its over-expression results in an extension of lifespan (>30%) and an increased resistance to stress. Although DmHsp22 has a chaperone-like activity in vitro, additional mechanisms by which it may extend lifespan in vivo are unknown. Genome-wide transcriptional analysis and comparative mitochondrial proteomic analysis by MALDI-TOF were performed to unveil differences in long-lived DmHsp22 over-expressing flies. Flies over-expressing DmHsp22 display an upregulation of genes normally downregulated with age and involved in energy production and protein biosynthesis. Interestingly, DmHsp22 over-expression extended lifespan of normal fibroblasts by slowing the aging process. However, its expression also increased the malignant properties of human transformed cells. The delicate balance between beneficial and noxious effects of this small chaperone are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1749-6632
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
1197
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
67-75
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Protection from aging by small chaperones: A trade-off with cancer?
pubmed:affiliation
Laboratory of Cell and Developmental Genetics, Department of Molecular Biology, Medical Biochemistry and Pathology, Institut de Biologie Intégrative et des Systèmes and PROTEO Université Laval, Québec, Canada.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't