Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2003-10-13
pubmed:abstractText
HSP60 has long been known as an important chaperonin and as having key folding functions within the mitochondria. However, it has now become evident that significant amounts of HSP60 are found in extra-mitochondrial locations. This extra-mitochondrial HSP60 in the heart has key anti-apoptotic functions. Extra-mitochondrial HSP60 complexes with both bax and bak, but not with bcl-2. Reduction in HSP60 is sufficient to precipitate apoptosis. In the setting of hypoxia and reoxygenation HSP60 decreases with reoxygenation, but the apoptotic cascade has already been triggered by end-hypoxia. Redistribution of cytosolic HSP60 to the plasma membrane during hypoxia appears to contribute to the initiation of the apoptotic cascade with hypoxia and reoxygenation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1530-7905
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
263-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
HSP60, Bax, and cardiac apoptosis.
pubmed:affiliation
Cardiovascular Division, Department of Medicine, University of California, Davis 95616, USA. aaknowlton@ucdavis.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Review