3-(thymin-1--yl)-2-propenal and 9-(3-oxoprop-1-enyl)adenine

3-(thymin-1--yl)-2-propenal has been researched along with 9-(3-oxoprop-1-enyl)adenine* in 2 studies

Other Studies

2 other study(ies) available for 3-(thymin-1--yl)-2-propenal and 9-(3-oxoprop-1-enyl)adenine

Article	Year
Furfural, a precursor of the cytokinin hormone kinetin, and base propenals are formed by hydroxyl radical damage of DNA. Biochemical and biophysical research communications, 1997, Sep-18, Volume: 238, Issue:2 Recently, we have detected kinetin (N6-furfuryladenine), a well known cytokinin plant hormone, in commercially available DNA, in freshly extracted cellular DNA and in plant cell extracts. We had suggested that the furfuryl moiety of kinetin originates from furfural which is one of the primary oxidation products of deoxyribose in DNA. Here we show that the human cell extracts treated with O-(2,3,4,5,6-pentafluorobenzyl) hydroxylamine (PFBHA) give rise to oxime derivatives of various aldehydes present in the cell. Mass spectrometric analysis of silylated oximes showed several mass signals of different species, one of which was identified as furfural. Furthermore, detailed inspection of the mass spectra of DNA showed the mass signals of 165, 180, 189 and 206 m/z which correspond to cytosine-propenal, thymine-propenal, adenine-propenal and guanine-propenal, respectively. The presence of furfural, along with four base-propenals in the cell extract, as the primary oxidation products of deoxyribose, suggests that degradation of sugar residues in DNA is one of the major routes of cellular damage in addition to the modification of nucleic acid bases. Topics: Adenine; Cells, Cultured; DNA Damage; Fibroblasts; Free Radicals; Furaldehyde; Humans; Kinetin; Mass Spectrometry; Oxidation-Reduction; Skin; Thymine	1997
Detoxication of base propenals and other alpha, beta-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases. Proceedings of the National Academy of Sciences of the United States of America, 1994, Feb-15, Volume: 91, Issue:4 Radiation and chemical reactions that give rise to free radicals cause the formation of highly cytotoxic base propenals, degradation products of DNA. Human glutathione transferases (GSTs; RX:glutathione R-transferase, EC 2.5.1.18) of classes Alpha, Mu, and Pi were shown to promote the conjugation of glutathione with base propenals and related alkenes. GST P1-1 was particularly active in catalyzing the reactions with the propenal derivatives, and adenine propenal was the substrate giving the highest activity. The catalytic efficiency of GST P1-1 with adenine propenal (kcat/Km = 7.7 x 10(5) M-1.s-1) is the highest so far reported with any substrate for this enzyme. In general, GST A1-1 and GST M1-1, in contrast to GST P1-1, were more active with 4-hydroxyalkenals (products of lipid peroxidation) than with base propenals. The adduct resulting from the Michael addition of glutathione to the alkene function of one of the base propenals (adenine propenal) was identified by mass spectrometry. At the cellular level, GST P1-1 was shown to provide protection against alpha, beta-unsaturated aldehydes. GST P1-1 added to the culture medium of HeLa cells augmented the protective effect of glutathione against the toxicity of adenine propenal and thymine propenal. No protective effect of the enzyme was observed in the presence of the competitive inhibitor S-hexylglutathione. GST P1-1 introduced into Hep G2 cells by electroporation was similarly found to increase their resistance to acrolein. The results show that glutathione transferases may play an important role in cellular detoxication of electrophilic alpha, beta-unsaturated carbonyl compounds produced by radical reactions, lipid peroxidation, ionizing radiation, and drug metabolism. Topics: Acrolein; Adenine; Aldehydes; Alkenes; Antineoplastic Agents; Cells, Cultured; Free Radicals; Glutathione Transferase; Humans; Inactivation, Metabolic; Isoenzymes; Lipid Peroxidation; Liver; Mass Spectrometry; Oxygen; Recombinant Proteins; Substrate Specificity; Thymine	1994

Article

Year

Furfural, a precursor of the cytokinin hormone kinetin, and base propenals are formed by hydroxyl radical damage of DNA.

Biochemical and biophysical research communications, 1997, Sep-18, Volume: 238, Issue:2

Recently, we have detected kinetin (N6-furfuryladenine), a well known cytokinin plant hormone, in commercially available DNA, in freshly extracted cellular DNA and in plant cell extracts. We had suggested that the furfuryl moiety of kinetin originates from furfural which is one of the primary oxidation products of deoxyribose in DNA. Here we show that the human cell extracts treated with O-(2,3,4,5,6-pentafluorobenzyl) hydroxylamine (PFBHA) give rise to oxime derivatives of various aldehydes present in the cell. Mass spectrometric analysis of silylated oximes showed several mass signals of different species, one of which was identified as furfural. Furthermore, detailed inspection of the mass spectra of DNA showed the mass signals of 165, 180, 189 and 206 m/z which correspond to cytosine-propenal, thymine-propenal, adenine-propenal and guanine-propenal, respectively. The presence of furfural, along with four base-propenals in the cell extract, as the primary oxidation products of deoxyribose, suggests that degradation of sugar residues in DNA is one of the major routes of cellular damage in addition to the modification of nucleic acid bases.

Topics: Adenine; Cells, Cultured; DNA Damage; Fibroblasts; Free Radicals; Furaldehyde; Humans; Kinetin; Mass Spectrometry; Oxidation-Reduction; Skin; Thymine

1997

Detoxication of base propenals and other alpha, beta-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases.

Proceedings of the National Academy of Sciences of the United States of America, 1994, Feb-15, Volume: 91, Issue:4

Radiation and chemical reactions that give rise to free radicals cause the formation of highly cytotoxic base propenals, degradation products of DNA. Human glutathione transferases (GSTs; RX:glutathione R-transferase, EC 2.5.1.18) of classes Alpha, Mu, and Pi were shown to promote the conjugation of glutathione with base propenals and related alkenes. GST P1-1 was particularly active in catalyzing the reactions with the propenal derivatives, and adenine propenal was the substrate giving the highest activity. The catalytic efficiency of GST P1-1 with adenine propenal (kcat/Km = 7.7 x 10(5) M-1.s-1) is the highest so far reported with any substrate for this enzyme. In general, GST A1-1 and GST M1-1, in contrast to GST P1-1, were more active with 4-hydroxyalkenals (products of lipid peroxidation) than with base propenals. The adduct resulting from the Michael addition of glutathione to the alkene function of one of the base propenals (adenine propenal) was identified by mass spectrometry. At the cellular level, GST P1-1 was shown to provide protection against alpha, beta-unsaturated aldehydes. GST P1-1 added to the culture medium of HeLa cells augmented the protective effect of glutathione against the toxicity of adenine propenal and thymine propenal. No protective effect of the enzyme was observed in the presence of the competitive inhibitor S-hexylglutathione. GST P1-1 introduced into Hep G2 cells by electroporation was similarly found to increase their resistance to acrolein. The results show that glutathione transferases may play an important role in cellular detoxication of electrophilic alpha, beta-unsaturated carbonyl compounds produced by radical reactions, lipid peroxidation, ionizing radiation, and drug metabolism.

Topics: Acrolein; Adenine; Aldehydes; Alkenes; Antineoplastic Agents; Cells, Cultured; Free Radicals; Glutathione Transferase; Humans; Inactivation, Metabolic; Isoenzymes; Lipid Peroxidation; Liver; Mass Spectrometry; Oxygen; Recombinant Proteins; Substrate Specificity; Thymine

1994