Genetic and Enzymatic Characteristics of CYP2A13 in Relation to Lung Damage
Abstract
:1. Introduction
2. Tissue Distribution
3. Substrates and Inhibitors
3.1. AFB1
3.2. NNK
3.3. Skatole
4. Genetic Polymorphisms
5. Transcription Regulation
6. Conclusions
Funding
Acknowledgments
Conflicts of Interest
Abbreviations
3MI | 3-methylindole |
8-MOP | 8-methoxypsoralen |
AFB1 | aflatoxin B1 |
AFG1 | aflatoxin G1 |
ATM | ATM serine/threonine kinase |
ATR | ATR serine/threonine kinase |
BRCA1 | Breast cancer type 1 susceptibility protein |
ChIP | Chromatin immunoprecipitation |
Chk2 | Checkpoint kinase 2 |
FOXA2 | Forkhead box A |
γH2AX | Phosphorylated H2A.X variant histone |
Km | Michaelis–Menten constant |
NF-kB | Nuclear factor kappa-light-chain-enhancer of activated B cells |
NNK | 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone |
p53 | tumor protein P53 |
TNFα | Tumor necrosis factor alpha |
Vmax | maximal velocity |
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Compound | Relation to CYP2A13 | Parameter | Reference |
---|---|---|---|
Coumarin | Substrate | Km = 2.21 ± 0.63 or 0.48 ± 0.07 µM, Vmax = 0.69 ± 0.16 or 0.15 ± 0.006 | [19,30] |
Testosterone | Substrate | Km = 13 ± 3 µM, Vmax = 1.7 ± 0.11 | [23] |
4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK) | Substrate | Km = 10.4 µM, Vmax = 3.6 | [21] |
Nicotine | Substrate/Inhibitor # | Km = 20.2 µM, Vmax = 8.7, Ki = 6.57−25.01 µM ## | [21,24] |
Cotinine | Substrate | Km = 45.2 µM, Vmax = 0.7 | [21] |
4-aminobiphenyl | Substrate | Km = 38.5 ± 0.6 µM, Vmax = 7.8 ± 0.00 | [11] |
Naphthalene | Substrate | Km = N.D., Vmax = 6.1 ± 0.88 | [31] |
Phenanthrene | Substrate | Km = N.D., Vmax = 3.14 ± 0.35 | [31] |
Biphenyl | Substrate | Km = N.D., Vmax = 3.1 ± 0.19 | [31] |
Pyrene | Substrate | Km = 1.2 ± 0.2 µM, Vmax = 2.0 ± 0.06 | [32] |
5-hydroxymethyfurfural | Substrate | Km = 50.9 ± 8.3 µM, Vmax = 2.7 ± 0.2 | [33] |
Scoparone | Substrate | Km = 10.1 µM, Vmax = 22 µmol/min/g | [34] |
Aflatoxin B1 | Substrate | Km = N.D., Vmax = 1.7–6.2 ## | [35] |
3-methylindole (skatole) | Substrate/Inhibitor # | Km = 14.3−14.8 µM, Vmax = 1.5−1.9 ## Ki = 10 µM | [36] |
(R,S)-N-nitrosoanatabine (NAT) | Inhibitor # | Ki = 0.21−0.71 µM ## | [24] |
(R,S)-N-nitrosoanabasine (NAB) | Inhibitor # | Ki = 0.23−0.87 µM ## | [24] |
1-methyl-4-(3-pyridinyl) pyrrole (beta-nicotyrine) | Inhibitor * | Ki = 0.17 µM | [25] |
Menthofuran | Inhibitor * | Ki = 1.24 µM | [25] |
(-)-menthol | Inhibitor * | Ki = 8.2 µM | [25] |
8-methoxypsoralen (8-MOP) | Inhibitor * | Ki = 0.11 µM | [23] |
Benzyl selenocyanate (BSC) | Inhibitor * | IC50 = 1.2 ± 0.19 µM | [37] |
1,2-phenylenebis(methylene)selenocyanate (o-XSC) | Inhibitor * | IC50 = 1.2 ± 0.13 µM | [37] |
1,3-phenylenebis(methylene)selenocyanate (m-XSC) | Inhibitor * | IC50 = 0.22 ± 0.03 µM | [37] |
1,4-phenylenebis(methylene)selenocyanate (p-XSC) | Inhibitor * | IC50 = 1.4 ± 0.21 µM | [37] |
Apigenin | Inhibitor * | IC50 = 0.05 ± 0.01 µM | [29] |
Luteolin | Inhibitor * | IC50 = 0.18 ± 0.02 µM | [29] |
Chrysoeriol | Inhibitor * | IC50 = 0.82 ± 0.05 µM | [29] |
Quercetin | Inhibitor * | IC50 = 0.80 ± 0.01 µM | [29] |
2-(penta-1,3-diyn-1-yl)-5-(4-acetoxy-3-hydroxybuta-1-yn-1-yl) thiophene | Inhibitor * | IC50 = 6.18 ± 0.28 µM | [29] |
2-(prop-1-inyl)-5-(6-acetoxy-5-hydroxyhexa-1,3-diinyl) thiophene | Inhibitor * | IC50 = 2.94 ± 0.01 µM | [29] |
2-(prop-1-inyl)-5-(5, 6-dihydroxyhexa-1,3-diinyl) thiophene | Inhibitor * | IC50 = 2.40 ± 0.33 µM | [29] |
Rhinacanthin-A | Inhibitor * | IC50 = 1.42 ± 0.05 µM | [38] |
Rhinacanthin-B | Inhibitor * | IC50 = 1.58 ± 0.17 µM | [38] |
Rhinacanthin-C | Inhibitor * | IC50 = 7.1 ± 0.81 µM | [38] |
Rhinacanthin-H/I | Inhibitor * | IC50 = 6.5 ± 1.4 µM | [38] |
Phenylpropyl isothiocyanate (PPITC) | Inhibitor * | Ki = 0.14 µM | [39] |
Phenylhexyl isothiocyanate (PHITC) | Inhibitor * | Ki = 1.1 µM | [39] |
1-hexyl-1H imidazole B | Inhibitor * | IC50 = 2.1 ± 0.1 µM | [30] |
Benzyl isothiocyanate (BITC) | Inhibitor * | Ki = 1.3 µM | [40] |
Phenethyl isothiocyanate (PEITC) | Inhibitor * | Ki = 0.03 µM | [40] |
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Vrzal, R. Genetic and Enzymatic Characteristics of CYP2A13 in Relation to Lung Damage. Int. J. Mol. Sci. 2021, 22, 12306. https://doi.org/10.3390/ijms222212306
Vrzal R. Genetic and Enzymatic Characteristics of CYP2A13 in Relation to Lung Damage. International Journal of Molecular Sciences. 2021; 22(22):12306. https://doi.org/10.3390/ijms222212306
Chicago/Turabian StyleVrzal, Radim. 2021. "Genetic and Enzymatic Characteristics of CYP2A13 in Relation to Lung Damage" International Journal of Molecular Sciences 22, no. 22: 12306. https://doi.org/10.3390/ijms222212306