Linked Life Data

15566968

Source:http://linkedlifedata.com/resource/pubmed/id/15566968

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2004-11-29
pubmed:abstractText
The formation of S-nitrosylated proteins is a nitric oxide-dependent post-translational modification important in signal transduction, yet the in situ detection of S-nitrosylated proteins remains problematic. In this study, we adapted a recently developed biotin derivatization approach to visualize S-nitrosylated proteins in intact cells. This strategy circumvents the use of antibodies directed against S-nitrosocysteine, which may have problematic specificity, due to epitope instability. Endogenous protein S-nitrosylation could be observed in intact cells and in mouse lung sections using fluorophore-conjugated streptavidin and confocal microscopy, and was enhanced by S-nitrosothiols and reduced following treatment with the nitric oxide synthase inhibitor, L-N-monomethyl arginine. Intriguingly, protein S-nitrosylation was detected mainly in the nuclear compartment of cells under baseline conditions and was enhanced when nuclear export was blocked with leptomycin B. We also determined that the small GTPase Ran, a key regulator of nucleocytoplasmic transport, is a target for S-nitrosylation. These findings demonstrate that biotin derivatization is a useful approach to detect S-nitrosylated proteins in situ in cellular compartments or tissues, and will be useful in the assessment of altered S-nitrosylation in pathological conditions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1089-8603
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
216-27
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
In situ detection and visualization of S-nitrosylated proteins following chemical derivatization: identification of Ran GTPase as a target for S-nitrosylation.
pubmed:affiliation
Department of Pathology, University of Vermont, Burlington, VT 05405, USA. kckless@zoo.uvm.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural