Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0002895 (sickle cell disease)
 11,747 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The purpose of this study was to measure the cytotoxicity of six endodontic irrigants on cultured gingival fibroblasts using the CyQuant assay. Human gingival fibroblasts were grown in Dulbecco's Modified Eagle Medium (DMEM) containing 10% fetal bovine serum at 37 degrees C and 5% CO(2). At confluence, cells were split, plated in 96-well plates and incubated for 24-h to allow attachment. The following irrigants were tested at various concentrations: Sodium hypochlorite (NaOCl); iodine potassium-iodide (IKI); Betadine scrub (BS); calcium hydroxide [Ca(OH)2]; chlorine dioxide (SCD) and DMEM (positive control). Experimental groups were compared by the logarithmic difference between the clinical and LD50 concentrations of a particular irrigant. The results showed that IKI and Ca(OH)2 were significantly less cytotoxic than SCD, NaOCl, and BS. In conclusion, IKI and Ca(OH)2 are well tolerated by human gingival fibroblasts.
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PMID:An in vitro evaluation of the cytotoxicity of various endodontic irrigants on human gingival fibroblasts. 1604 47

Glyoxalase II enzymes catalyze the hydrolysis of a thioester substrate and have been found to coordinate a variety of dimetal combinations, including Fe(III)Zn(II), within the enzyme active site. Of relevance to these enzymes, the thioester hydrolysis reactivity of the Fe(III)Zn(II) compound [(BPBPMP)Fe(III)Zn(II)(mu-OAc)(2)]ClO(4) (1) was evaluated in CH(3)CN/H(2)O (50:50; buffered) at 26.5 degrees C. Thioester hydrolysis in the absence and presence of 1 was monitored using (2)H NMR by following the loss of the thioester -SCD(3) signal. Two products are generated in the reaction involving the metal complex, D(3)CSSCD(3) and CD(3)SH. Kinetic studies of this reaction as a function of pH revealed maximum rate above the pK(a) of a Zn-OH(2) moiety of [(BPBPMP)Fe(III)(OH)(mu-OH)Zn(II)(OH(2))](+), which forms from 1 in CH(3)CN/H(2)O (50:50). UV-vis and electron paramagnetic resonance (EPR) studies of a single turnover thioester hydrolysis reaction in the presence of 1 equiv of 1 at pH = 9.0 suggest that the thioester does not initially interact with the Fe(III) center, but that changes occur at this site over the course of the reaction. The formation of a Fe(III)-SCD(3) moiety is proposed based on the observed D(3)CSSCD(3) formation, which likely results from redox activity involving a iron(III) thiolate species. A mechanism for thioester hydrolysis is proposed involving initial coordination of the deprotonated alpha-hydroxy thioester to the zinc center followed by nucleophilic attack by a terminal Fe(III)-OH moiety and thiolate leaving group stabilization by the Fe(III) center. Overall, this study outlines a novel approach of using an aliphatic thioester substrate and (2)H NMR to provide mechanistic insight into thioester hydrolysis involving an Fe(III)Zn(II) complex of relevance to glyoxalase II.
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PMID:Thioester hydrolysis reactivity of an Fe(III)Zn(II) complex. 1982 73

The mononuclear zinc complex [(bpta)Zn](ClO(4))(2).0.5H(2)O promotes the hydrolysis of the thioester PhCH(OH)C(O)SCD(3) when dissolved in CH(3)CN:H(2)O (50:50 buffered at pH 9.0). This reaction results in the formation of a mixture of CD(3)SH and a zinc thiolate complex, the latter of which can be protonated to generate additional CD(3)SH. Kinetic studies revealed an overall second-order reaction with an activation energy that is similar to that found for aqueous OH(-) promoted thioester hydrolysis. These studies represent the first investigation of chemistry relevant to that occurring in the monozinc-containing form of human glyoxalase II.
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PMID:Thioester hydrolysis promoted by a mononuclear zinc complex. 2003 13