16R-HETE and 16S-HETE alter human cytochrome P450 1B1 enzyme activity probably through an allosteric mechanism.

التفاصيل البيبلوغرافية
العنوان:	16R-HETE and 16S-HETE alter human cytochrome P450 1B1 enzyme activity probably through an allosteric mechanism.
المؤلفون:	Hidayat R; Faculty of Pharmacy & Pharmaceutical Sciences, 2142J Katz Group-Rexall Centre for Pharmacy and Health Research, University of Alberta, Edmonton, AL, T6G 2E1, Canada., Shoieb SM; Faculty of Pharmacy & Pharmaceutical Sciences, 2142J Katz Group-Rexall Centre for Pharmacy and Health Research, University of Alberta, Edmonton, AL, T6G 2E1, Canada., Mosa FES; Faculty of Pharmacy & Pharmaceutical Sciences, 2142J Katz Group-Rexall Centre for Pharmacy and Health Research, University of Alberta, Edmonton, AL, T6G 2E1, Canada., Barakat K; Faculty of Pharmacy & Pharmaceutical Sciences, 2142J Katz Group-Rexall Centre for Pharmacy and Health Research, University of Alberta, Edmonton, AL, T6G 2E1, Canada., Brocks DR; Faculty of Pharmacy & Pharmaceutical Sciences, 2142J Katz Group-Rexall Centre for Pharmacy and Health Research, University of Alberta, Edmonton, AL, T6G 2E1, Canada., Isse FA; Faculty of Pharmacy & Pharmaceutical Sciences, 2142J Katz Group-Rexall Centre for Pharmacy and Health Research, University of Alberta, Edmonton, AL, T6G 2E1, Canada., Gerges SH; Faculty of Pharmacy & Pharmaceutical Sciences, 2142J Katz Group-Rexall Centre for Pharmacy and Health Research, University of Alberta, Edmonton, AL, T6G 2E1, Canada., El-Kadi AOS; Faculty of Pharmacy & Pharmaceutical Sciences, 2142J Katz Group-Rexall Centre for Pharmacy and Health Research, University of Alberta, Edmonton, AL, T6G 2E1, Canada. aelkadi@ualberta.ca.
المصدر:	Molecular and cellular biochemistry [Mol Cell Biochem] 2024 Jun; Vol. 479 (6), pp. 1379-1390. Date of Electronic Publication: 2023 Jul 12.
نوع المنشور:	Journal Article
اللغة:	English
بيانات الدورية:	Publisher: Springer Country of Publication: Netherlands NLM ID: 0364456 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1573-4919 (Electronic) Linking ISSN: 03008177 NLM ISO Abbreviation: Mol Cell Biochem Subsets: MEDLINE
أسماء مطبوعة:	Publication: New York : Springer Original Publication: The Hague, Dr. W. Junk B. V. Publishers.
مواضيع طبية MeSH:	Cytochrome P-450 CYP1B1/metabolism , Cytochrome P-450 CYP1B1/genetics , Hydroxyeicosatetraenoic Acids/metabolism , Hydroxyeicosatetraenoic Acids/pharmacology, Humans ; Allosteric Regulation/drug effects
مستخلص:	Cytochrome P450 1B1 (CYP1B1) has been widely associated with the development of cardiac pathologies due to its ability to produce cardiotoxic metabolites like midchain hydroxyeicosatetraenoic acids (HETEs) from arachidonic acid (AA) through an allylic oxidation reaction. 16-HETE is a subterminal HETE that is also produced by CYP-mediated AA metabolism. 19-HETE is another subterminal HETE that was found to inhibit CYP1B1 activity, lower midchain HETEs, and have cardioprotective effects. However, the effect of 16-HETE enantiomers on CYP1B1 has not yet been investigated. We hypothesized that 16(R/S)-HETE could alter the activity of CYP1B1 and other CYP enzymes. Therefore, this study was carried out to investigate the modulatory effect of 16-HETE enantiomers on CYP1B1 enzyme activity, and to examine the mechanisms by which they exert these modulatory effects. To investigate whether these effects are specific to CYP1B1, we also investigated 16-HETE modulatory effects on CYP1A2. Our results showed that 16-HETE enantiomers significantly increased CYP1B1 activity in RL-14 cells, recombinant human CYP1B1, and human liver microsomes, as seen by the significant increase in 7-ethoxyresorufin deethylation rate. On the contrary, 16-HETE enantiomers significantly inhibited CYP1A2 catalytic activity mediated by the recombinant human CYP1A2 and human liver microsomes. 16R-HETE showed stronger effects than 16S-HETE. The sigmoidal binding mode of the enzyme kinetics data demonstrated that CYP1B1 activation and CYP1A2 inhibition occurred through allosteric regulation. In conclusion, our study provides the first evidence that 16R-HETE and 16S-HETE increase CYP1B1 catalytic activity through an allosteric mechanism. (© 2023. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.)
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معلومات مُعتمدة:	PS 168846 Canada CAPMC CIHR; PS 168846 Canada CAPMC CIHR
فهرسة مساهمة:	Keywords: 16-HETE; Allosteric modulation; CYP1A2; CYP1B1; EROD; MROD
المشرفين على المادة:	EC 1.14.14.1 (Cytochrome P-450 CYP1B1) 0 (Hydroxyeicosatetraenoic Acids) EC 1.14.14.1 (CYP1B1 protein, human) 79551-85-2 (19-hydroxy-5,8,11,14-eicosatetraenoic acid)
تواريخ الأحداث:	Date Created: 20230712 Date Completed: 20240704 Latest Revision: 20240704
رمز التحديث:	20240704
DOI:	10.1007/s11010-023-04801-4
PMID:	37436655
قاعدة البيانات:	MEDLINE

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تدمد:	1573-4919
DOI:	10.1007/s11010-023-04801-4