Linked Life Data

18554542

Source:http://linkedlifedata.com/resource/pubmed/id/18554542

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2008-6-16
pubmed:abstractText
Nitrosative stress, a nitric oxide (NO)-mediated nitrosylation of redox-sensitive thiols, has been linked to the regulation of signal transduction, gene expression, and cell growth and apoptosis and thus may be widely implicated in both physiological and pathological actions of NO. Protein S-nitrosylation has been observed to occur in vitro and in vivo in pathophysiological conditions. Apoptosis can be regulated by S-nitrosylation of the redox-sensitive cysteine residue in the active site of all caspase family proteases. Detection and measurement for the modification and inactivation of caspases by S-nitrosylation remain a new challenge because of the lability of the S-nitrosothiol moiety. This chapter describes approaches for assaying and identifying S-nitrosylated caspase enzymes in vitro and in vivo. These methods permit rapid and reproducible assays of S-nitrosylated caspases in biological and clinical specimens and should be useful for studies defining a pathophysiological role of NO in several apoptosis-associated human diseases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0076-6879
pubmed:author
pubmed:issnType
Print
pubmed:volume
441
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
317-27
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Detection and measurement for the modification and inactivation of caspase by nitrosative stress in vitro and in vivo.
pubmed:affiliation
Vascular System Research Center, Kangwon National University, Chunchon, Korea.
pubmed:publicationType
Journal Article, Comparative Study, Review, Research Support, Non-U.S. Gov't