Disease relevance of NSC4123

• When sulfation of harmol was inhibited by 2,6-dichloro-4-nitrophenol, cholestasis occurred at lower infusion rates of harmol [1].

High impact information on NSC4123

• The propensity of these N-hydroxy arylamines and N-hydroxy heterocyclic amines to serve as selective substrates for human TS-PST was further confirmed by inhibition with 2,6-dichloro-4-nitrophenol and by thermostability studies [2].
• The transfected cells expressed a high level of DHEA ST activity, and this enzyme activity displayed a pattern of inhibition by the ST inhibitor 2,6-dichloro-4-nitrophenol identical to that of human liver DHEA ST [3].
• N-OH-FAABP was a substrate for sulfotransferases in vitro and sulfation was inhibited by the sulfotransferase inhibitors pentachlorophenol (PCP) and 2,6-dichloro-4-nitrophenol (DCNP) [4].
• [35S]PAPS formation in slices was completely and rather potently blocked by 2,6-dichloro-4-nitrophenol (IC50 = 10 microM), an inhibitor of the PAPS-synthesizing enzyme system in a cytosolic preparation [5].
• Several biochemical properties of each enzyme that included apparent K(m) values, thermal stabilities, and responses to the inhibitors 2,6-dichloro-4-nitrophenol and NaCl were used to further characterize the SULT activities [6].

Biological context of NSC4123

• The pharmacokinetics of 2,6-dichloro-4-nitrophenol (DCNP) have been studied in the rat [7].
• Moreover, DNA damage induced by NDELA, NHMOR and other hydroxylated N-nitroso compounds is strongly reduced by pretreatment with the sulfotransferase inhibitor, 2,6-dichloro-4-nitrophenol (DCNP) [8].
• Using a focussed microarray (genechip) of 22 housekeeping genes we show this in apoptosis induced in human Chang liver cells by DCNP (2,6-dichloro-4-nitrophenol), a non-genotoxic inhibitor of sulfate detoxification [9].

Anatomical context of NSC4123

• However, the binding of HNOH-MeIQx to DNA in hepatocytes was independent of sulfotransferase since inhibitors of this enzyme, 2,6-dichloro-4-nitrophenol (DCNP) and pentachlorophenol (PCP), did not diminish DNA binding [10].
• The appearance of each required the presence of PAPS and cytosol and was inhibited by the sulfotransferase inhibitor 2,6-dichloro-4-nitrophenol [11].
• The pH optimum of 6.6, a 50% inhibitory concentration for 2,6-dichloro-4-nitrophenol of 1.0 mumol/L, and retention of 56% of activity after preincubation at 45 degrees C for 15 minutes were the same for the granulocytes as for platelet thermostable PST [12].
• 1-Naphthol metabolism and metabolite transport in the small and large intestine. II: Effect of sulphate and phosphate ion omission, and of 2,6-dichloro-4-nitrophenol in the isolated guinea pig mucosa [13].

Associations of NSC4123 with other chemical compounds

• Selective inhibition of sulfate conjugation in the rat: pharmacokinetics and characterization of the inhibitory effect of 2,6-dichloro-4-nitrophenol [7].
• As in the case of the in vitro studies, pentachlorophenol and 2,6-dichloro-4-nitrophenol inhibited the in vitro formation of 8-aminoguanosine and 8-oxoguanosine [14].
• In kinetic studies using isolated hamster hepatocytes, 2,6-dichloro-4-nitrophenol competitively inhibited acetaminophen sulfotransferase with a Ki of 2.5 X 10(-6) M [15].
• Although less potent in this intact cell system (IC50 2-5 microM), quercetin was still more potent than 2,6-dichloro-4-nitrophenol, the classical P-form PST inhibitor that has been shown to be an inhibitor also in vivo [16].
• Male Fischer rats (4-8/group) were administered one of the following intraperitoneal (ip) pretreatment (dose, pretreatment time) prior to NDPS (0.6 mmol/kg) or NDPS vehicle (sesame oil, 2.5 ml/kg): (1) no pretreatment, (2) dehydroepiandrosterone (DHEA) (0.5 mmol/kg, 1 h), or (3) 2,6-dichloro-4-nitrophenol (DCNP) (0.04 mmol/kg, 1 h) [17].

Gene context of NSC4123

• Our results demonstrated 2 forms of the pituitary enzyme that were similar to the thermostable (TS) and thermolabile (TL) forms of platelet PST with regard to assay conditions, pH optima, Km values for multiple substrates, responses to 2,6-dichloro-4-nitrophenol (DCNP), and thermal stability properties [18].
• Human liver arylamine N-sulfotransferase (AANST) activity was similar to that of TS but not TL PST with regard to thermal stability, inhibition by 2,6-dichloro-4-nitrophenol (DCNP), and regulation among individuals [19].
• Biochemical properties of each skin enzyme were the same as the platelet enzymes with respect to apparent Km values for substrates, pH optima, thermal stabilities and responses to inhibition by 2,6-dichloro-4-nitrophenol (DCNP) [20].
• Since 2,6-dichloro-4-nitrophenol (DCNP) produces a prolonged and selective inhibition of the sulfoconjugation of exogenous phenols by the liver, we decided to examine the applicability of DCNP to studies of sulfation of CCK-8 and other compounds by brain [21].
• H-PST was sensitive to inhibition by DCNP (2,6-dichloro-4-nitrophenol) [22].

Analytical, diagnostic and therapeutic context of NSC4123

• Inhibition of a purified recombinant homodimeric bovine PST by 2,6-dichloro-4-nitrophenol (DCNP) and pentachlorophenol (PCP) displayed very sharp titration curves that required modeling with Hill equations with slope factors of 2 and 3, respectively [23].
• We applied the method for fitting of several sets of metabolic data obtained from rat liver perfusion studies performed with salicylamide (SAM) (i) without and (ii) with the presence of 2,6-dichloro-4-nitrophenol (DCNP), a SAM sulfation inhibitor [24].

References