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Enhancement by Cysteinyl Thiols of Acetyltransferase‐mediated, but Not of Sulfotransferase‐mediated, Binding of a Pyrolysate‐derived N‐Hydroxyarylamine, 2‐Hydroxyamino‐6‐methyldipyrido[1,2‐<i>a</i>:3′,2′‐<i>d</i>]imidazole, to DNA
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Description
<jats:p>The effect of thiols on the activation of a pyrolysate‐derived N‐hydroxyarylamine, 2‐hydroxyamino‐6‐methyldipyrido[1,2‐<jats:italic>a</jats:italic>:3′,2′‐<jats:italic>d</jats:italic>]imidazole (N‐hydroxy‐Glu‐P‐1), was studied <jats:italic>in vitro</jats:italic>. In hepatic cytosol of rats, [<jats:sup>3</jats:sup>H]‐N‐hydroxy‐Glu‐P‐1 bound covalently to calf thymus DNA in the presence of acetyl CoA or 3′‐phosphoadenosine‐5′‐phosphosulfate (PAPS). The extent of the binding of N‐hydroxy‐Glu‐P‐1 in a PAPS‐dependent system was decreased by the addition of 10 m<jats:italic>M</jats:italic> glutathione, N‐acetyl‐<jats:sc>l</jats:sc>‐cysteine, 2‐mercaptoethanol or dithiothreitol. However, acetyl CoA‐dependent binding of N‐hydroxy‐Glu‐P‐1 was stimulated by the addition of 10 m<jats:italic>M</jats:italic> N‐acetyl‐<jats:sc>l</jats:sc>‐cysteine (3 fold), <jats:sc>l</jats:sc>‐cysteine (2 fold) or glutathione (1.2 fold), but not 10 m<jats:italic>M</jats:italic> 2‐mercaptoethanol or <jats:sc>l</jats:sc>‐methionine. After hydrolysis of the modified DNA, no difference was detected in the physicochemical properties of the nucleoside adduct formed in the acetyl CoA‐supported system with and without thiols. These results indicate that thiols with a cysteine residue are able to affect the activation of carcinogenic heterocyclic arylamines selectively by the modulation of the acetyltransferase‐mediated, but not the sulfotransferase‐mediated, pathway.</jats:p>
Journal
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- Japanese Journal of Cancer Research
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Japanese Journal of Cancer Research 81 653-659, 1990-06-01
Wiley
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Keywords
Details 詳細情報について
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- CRID
- 1870302168202634752
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- HANDLE
- 11588/305076
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- ISSN
- 09105050
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- PubMed
- 2119366
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- Data Source
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- OpenAIRE