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Drug-Target Interaction

Drug

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PubChem ID:2336
Structure:
Synonyms:
(B(a)P)
1,2-Benzpyrene
3,4 Benzopyrene
3,4 Benzpyrene
3,4-Benz(a)pyrene
3,4-Benzo(a)pyrene
3,4-Benzopirene
3,4-Benzopirene [Italian]
3,4-Benzopyrene
3,4-Benzopyrene (carcinogen)
3,4-Benzpyren
3,4-Benzpyren [German]
3,4-Benzpyrene
3,4-benzylpyrene
3,4-Benzypyrene
3,4-Benz[a]pyrene
3,4-BP
34505-58-3
36952_RIEDEL
4,5-Benzpyrene
42299-33-2
48564_SUPELCO
50-32-8
6,7-Benzopyrene
6699-27-0
819804-28-9
AC1L1DG9
AC1Q1HKZ
AG-F-69091
AI3-50461
AR-1H7844
B(a)P
B0085
B1760_SIGMA
BaP
Benz(a)pyrene
benzo(3,4)pyrene, radical ion(1)
Benzo(3,4)pyrene, radical ion(1+)
BENZO(A)PYRENE
BENZO(A)PYRENE (SEE ALSO: BENZO(E)PYRENE (CAS 192-97-2))
Benzo(a)pyrene radical cation
Benzo(a)pyrene [Polycyclic aromatic compounds]
Benzo(a)pyrene [Polycyclic aromatic hydrocarbons]
Benzo(a)pyrene, labeled with tritium
benzo(a)pyrene, radical ion(1)
Benzo(a)pyrene, radical ion(1+)
Benzo(a)pyrene, radical ion(1-)
Benzo(d,e,f)chrysene
Benzo(def)chrysene
Benzo[a]pyrene
Benzo[a]pyrene (BaP)
Benzo[a]pyrene solution
Benzo[d,e,f]chrysene
benzo[def]chrysene
benzo[pqr]tetraphene
Benzpyrene
Benz[a]pyrene
BIDD:ER0497
BP
BRD-K09668667-001-02-0
BSPBio_003250
B[a]p
C07535
c0950
CCG-39759
CCRIS 76
CHEBI:29865
CHEMBL31184
Coal tar pitch volatiles: benzo(a)pyrene
D001564
DivK1c_007049
EINECS 200-028-5
EN002216
HSDB 2554
I14-2877
KBio1_001993
KBio2_002385
KBio2_004953
KBio2_007521
KBio3_002470
KBioGR_001138
KBioSS_002390
LS-139
MLS002695983
MolPort-001-785-827
NCGC00178185-01
NCGC00178185-02
NCI60_001824
NSC 21914
NSC21914
RCRA waste no. U022
RCRA waste number U022
SBB061395
SMR000393676
SPBio_001122
SpecPlus_000953
Spectrum2_001081
Spectrum3_001695
Spectrum4_000609
Spectrum5_001824
Spectrum_001871
WLN: L D6 B6666 2AB TJ
ZINC01530818

Target

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Uniprot ID:CP1A1_HUMAN
Synonyms:
CYPIA1
Cytochrome P450 1A1
P450 form 6
P450-C
P450-P1
EC-Numbers:1.14.14.1
Organism:Homo sapiens
Human
PDB IDs:-

Binding Affinities:

Ki: Kd:Ic 50:Ec50/Ic50:
----
----

References:

18372000
Inhibition of aryl hydrocarbon receptor transactivation and DNA adduct formation by CYP1 isoform-selective metabolic deactivation of benzo[a]pyrene.. Kaori Endo; Shigeyuki Uno; Taiichiro Seki; Toyohiko Ariga; Yoshiaki Kusumi; Masako Mitsumata; Sachiko Yamada; Makoto Makishima (2008) Toxicology and applied pharmacology display abstract
Benzo[a]pyrene (BaP), a polyaromatic hydrocarbon produced by the combustion of cigarettes and coke ovens, is a known procarcinogen. BaP activates the aryl hydrocarbon receptor (AhR) and induces the expression of a battery of genes, including CYP1A1, which metabolize BaP to toxic compounds. The possible role of CYP1 enzymes in mediating BaP detoxification or metabolic activation remains to be elucidated. In this study, we assessed the effects of CYP1 enzymes (CYP1A1, CYP1A2 and CYP1B1) on BaP-induced AhR transactivation and DNA adduct formation in HEK293 cells and HepG2 cells. Transfection of CYP1A1 and CYP1B1, but not CYP1A2, suppressed BaP-induced activation of AhR. Expression of CYP1A1 and CYP1A2, but not CYP1B1, inhibited DNA adduct formation in BaP-treated HepG2 cells. These results indicate that CYP1A1 and CYP1B1 play a role in deactivation of BaP on AhR and that CYP1A1 and CYP1A2 are involved in BaP detoxification by suppressing DNA adduct formation. BaP treatment did not induce DNA adduct formation in HEK293 cells, even after transfection of CYP1 enzymes, suggesting that expression of CYP1 enzymes is not sufficient for DNA adduct formation. Lower expression of epoxide hydrolase and higher expression of glutathione S-transferase P1 (GSTP1) and GSTM1/M2 were observed in HEK293 cells compared with HepG2 cells. Dynamic expression of CYP1A1, CYP1A2 and CYP1B1 along with expression of other enzymes such as epoxide hydrolase and phase II enzymes may determine the detoxification or metabolic activation of BaP.
8170947
Inhibition of cytochromes P4501A by nitric oxide.. J Stadler; J Trockfeld; W A Schmalix; T Brill; J R Siewert; H Greim; J Doehmer (1994) Proceedings of the National Academy of Sciences of the United States of America display abstract
Inflammatory stimulation of the liver leads to the induction of nitric oxide (NO) biosynthesis. Because NO binds to the catalytic heme moiety of cytochromes P450 (CYPs), we investigated whether NO interferes with specific CYP-dependent metabolic pathways. In a first experimental approach V79 Chinese hamster cells genetically engineered for stable expression of rat and human CYP1A1 and -1A2 were used. Incubation with the NO donors sodium nitroprusside and S-nitrosylacetylpenicillamine led to a concentration-dependent inhibition of all four CYP enzymes. CYP1A1 was more sensitive to the inhibitory effect of NO than CYP1A2. In the second part of the study, endogenous NO synthesis was induced in rat hepatocytes by incubation with a mixture of cytokines and endotoxin. Concurrently, as NO production in hepatocytes increased within 24 hr, a decrease in CYP1A1-dependent benzo[a]pyrene turnover was observed to almost undetectable levels. The competitive inhibitor of NO synthesis, NG-monomethyl-L-arginine, was able to significantly restore CYP1A1 activity in the presence of cytokines and endotoxin. Inhibition of hepatocellular CYP activity by NO was predominantly due to a direct effect on the enzymes. However, NO-dependent inhibition of CYP expression at a transcriptional level was also demonstrated. Our results indicate that inhibition of NO biosynthesis in patients suffering from systemic inflammatory response syndromes may help to restore biotransformation capacity of the liver.