1993
DOI: 10.1016/0006-2952(93)90268-2
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Sulphate conjugation of minoxidil in rat skin

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Cited by 9 publications
(4 citation statements)
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“…SULT activity toward minoxidil was observed in the cytosolic fraction of rat skin. The thermostability and inhibition by the little specific aryl (phenol) SULT inhibitors 2,6-dichloro-4-nitrophenol and para-nitrophenol with good inhibitory activity for SULT 1A1 (Wang et al 2009 ) and lack of inhibition by low concentrations of dopamine and tyramine (substrates of SULT1A3) suggested that SULT1A1 is responsible for the observed activity (Wong et al 1993 ). The enzymatic transfer of 35 S from sodium 35 sulphate to minoxidil was also demonstrated, suggesting that the rat skin is capable of synthesizing 3′-phosphoadenosine-5′-phosphosulphate (PAPS), the required cofactor of SULT.…”
Section: Xenobiotic-metabolizing Enzymes In the Rat Skinmentioning
confidence: 99%
See 1 more Smart Citation
“…SULT activity toward minoxidil was observed in the cytosolic fraction of rat skin. The thermostability and inhibition by the little specific aryl (phenol) SULT inhibitors 2,6-dichloro-4-nitrophenol and para-nitrophenol with good inhibitory activity for SULT 1A1 (Wang et al 2009 ) and lack of inhibition by low concentrations of dopamine and tyramine (substrates of SULT1A3) suggested that SULT1A1 is responsible for the observed activity (Wong et al 1993 ). The enzymatic transfer of 35 S from sodium 35 sulphate to minoxidil was also demonstrated, suggesting that the rat skin is capable of synthesizing 3′-phosphoadenosine-5′-phosphosulphate (PAPS), the required cofactor of SULT.…”
Section: Xenobiotic-metabolizing Enzymes In the Rat Skinmentioning
confidence: 99%
“…The enzymatic transfer of 35 S from sodium 35 sulphate to minoxidil was also demonstrated, suggesting that the rat skin is capable of synthesizing 3′-phosphoadenosine-5′-phosphosulphate (PAPS), the required cofactor of SULT. Thus, it is conceivable that the metabolism-dependent action of minoxidil as a promoter of hair growth could be carried out by the skin itself (Wong et al 1993 ).…”
Section: Xenobiotic-metabolizing Enzymes In the Rat Skinmentioning
confidence: 99%
“…It is not merely a passive structural barrier between the body and environmental chemicals but also may be important site of metabolism. In recent years, although cutaneous metabolic reactions with skin preparations, tissue-cultured skin, and slices have been well studied, most of the work has dealt with oxidative reactions catalyzed by cytochrome P450 (Kao and Carver, 1990;Jugert et al, 1994;Ahmad et al, 1996;Cotovio et al, 1996) and alcohol dehydrogenase (Boehnlein et al, 1994); conjugative reactions catalyzed by glutathione S-transferase (Mukhtar and Bickers, 1981;Agarwal et al, 1992), UDP-glucuronosyltransferase (Moloney et al, 1982), and sulfotransferase (Wong et al, 1993); and hydrolytic reac- tions catalyzed by esterases (McCracken et al, 1993). Little is known about reductive reactions in skin.…”
mentioning
confidence: 99%
“…Wong et al (1993) noticed that the antihypertonic drug minoxidil, which possesses interesting hair growth promoting activity, appears in the rat skin to be a substrate of SULT1A1. This conclusion was based on the following observations: The SULT activity of the rat skin cytosolic fraction toward minoxidil was thermostable and was inhibited by para-nitrophenol and by 2,6-dichloro-4-nitrophenol [which are good inhibitors of SULT1A1 (Wang et al 2009)], but not by low concentrations of tyramine or dopamine (substrates of SULT1A3).…”
Section: Xenobiotica-metabolizing Enzymes In the Rat Skinmentioning
confidence: 99%