Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/70355
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dc.contributor.authorChen, Y.J.en_US
dc.contributor.authorKu, W.C.en_US
dc.contributor.authorFeng, L.T.en_US
dc.contributor.authorTsai, M.L.en_US
dc.contributor.authorHsieh, C.H.en_US
dc.contributor.authorHsu, W.H.en_US
dc.contributor.authorLiaw, W.F.en_US
dc.contributor.authorHung, C.H.en_US
dc.date2008zh_TW
dc.date.accessioned2014-06-11T05:59:43Z-
dc.date.available2014-06-11T05:59:43Z-
dc.identifier.issn0002-7863zh_TW
dc.identifier.urihttp://hdl.handle.net/11455/70355-
dc.description.abstractDinitrosyl-iron complexes (DNICs) are stable carriers for nitric oxide (NO), an important biological signaling molecule and regulator. However, the insolubility of synthetic DNICs, such as Roussin's red ester (RRE), in water has impaired efforts to unravel their biological functions. Here, we report a water-soluble and structurally well-characterized FIRE [Fe(mu-SC(2)H(4)COOH)(NO)(2)](2) (DNIC-1) and a{(Fe(NO)(2)}(10) DNIC [(PPh(2)(Ph-3-SO(3)Na))(2)Fe(NO)(2)] (DNIC-2), their NO-induced protein regulation, and their cellular uptake mechanism using immortalized vascular endothelial cells as a model. Compared with the most common NO donor, S-nitroso-N-acetyl-penicillamine (SNAP), the in vitro NO release assay showed that both DNICs acted as much slower yet higher stoichiometric NO-release agents with low cytotoxicity (IC(50) > 1 mM). Furthermore, L-cysteine facilitated NO release from SNAP and DNIC-1,, but not DNIC-2, in a dose- and time-dependent manner. EPR spectroscopic analysis showed, for the first time, that intact DNIC-1 can either diffuse or be transported into cells independently and can transform to either paramagnetic protein bound DNIC in the presence of serum or [DNIC-(CyS)(2)] with excess L-cysteine under serum-free conditions. Both DNICs subsequently induced NO-dependent upregulation of cellular heat shock protein 70 and in vivo protein S-nitrosylation. We conclude that both novel water-soluble DNICs have potential to release physiologically relevant quantities of NO and can be a good model for deciphering how iron-sulfur-nitrosyl compounds permeate into the cell membrane and for elucidating their physiological significance.en_US
dc.language.isoen_USzh_TW
dc.relationJournal of the American Chemical Societyen_US
dc.relation.ispartofseriesJournal of the American Chemical Society, Volume 130, Issue 33, Page(s) 10929-10938.en_US
dc.relation.urihttp://dx.doi.org/10.1021/ja711494men_US
dc.subjectdinitrosyl-iron complexesen_US
dc.subjectelectron-paramagnetic-resonanceen_US
dc.subjectmetalen_US
dc.subjectnitrosyl complexesen_US
dc.subjectthiol-containing ligandsen_US
dc.subjectprotein s-nitrosylationen_US
dc.subjectisolated tail arteryen_US
dc.subjectblack salten_US
dc.subjectnoradrenaline releaseen_US
dc.subjectpickleden_US
dc.subjectvegetablesen_US
dc.subjectcell-proliferationen_US
dc.titleNitric oxide physiological responses and delivery mechanisms probed by water-soluble Roussin's red ester and {Fe(NO)(2)}(10) DNICen_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1021/ja711494mzh_TW
item.languageiso639-1en_US-
item.openairetypeJournal Article-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.fulltextno fulltext-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
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