Nitric oxide-dependent CYP2B degradation is potentiated by a cytokine-regulated pathway and utilizes the immunoproteasome subunit LMP2
| العنوان: | Nitric oxide-dependent CYP2B degradation is potentiated by a cytokine-regulated pathway and utilizes the immunoproteasome subunit LMP2 |
|---|---|
| المؤلفون: | Edward T. Morgan, Haiyan Sun, Shweta Tripathi, Kyung Bo Kim, Choon-Myung Lee |
| المصدر: | Biochemical Journal |
| بيانات النشر: | Portland Press Ltd., 2012. |
| سنة النشر: | 2012 |
| مصطلحات موضوعية: | Male, medicine.medical_treatment, Nitric Oxide Synthase Type II, Biochemistry, chemistry.chemical_compound, 0302 clinical medicine, Genes, Tumor Suppressor, Nuclear protein, chemistry.chemical_classification, 0303 health sciences, biology, interleukin-1 (IL-1), Nuclear Proteins, Long-term potentiation, LMP, large multifunctional peptidase, Cysteine Endopeptidases, NG-Nitroarginine Methyl Ester, Cytokine, GAPDH, glyceraldehyde-3-phosphate dehydrogenase, Aryl Hydrocarbon Hydroxylases, NF-κB, nuclear factor κB, Proteasome Inhibitors, Metabolic Networks and Pathways, Research Article, Proteasome Endopeptidase Complex, cytochrome P450, Protein subunit, In Vitro Techniques, Protein degradation, Nitric Oxide, Models, Biological, Nitric oxide, immunoproteasome, 03 medical and health sciences, L-NAME, NG-nitro-L-arginine methyl ester, otorhinolaryngologic diseases, medicine, Animals, Nitric Oxide Donors, IFN, interferon, CT-L, chymotrypsin-like, nitric oxide (NO), Molecular Biology, 030304 developmental biology, NOx, nitrate and nitrite, NOS2, inducible nitric oxide synthase, Cytochrome P450, Cell Biology, Rats, Inbred F344, Rats, Kinetics, proteasome, IL-1, interleukin-1β, Enzyme, chemistry, PB, phenobarbital, Cytochrome P-450 CYP2B1, Steroid Hydroxylases, Hepatocytes, biology.protein, P450, cytochrome P450, 030217 neurology & neurosurgery, Interleukin-1 |
| الوصف: | CYP2B proteins in rat hepatocytes undergo NO-dependent proteolytic degradation, but the mechanisms and the reasons for the specificity towards only certain P450 (cytochrome P450) enzymes are yet unknown. In the present study we found that down-regulation of CYP2B proteins by the NO donor NOC-18 is accelerated by pretreatment of the hepatocytes with IL-1 (interleukin-1β) in the presence of an NO synthase inhibitor, suggesting that an NO-independent action of IL-1 contributes to the lability of CYP2B proteins. The immunoproteasome subunit LMP2 (large multifunctional peptidase 2) was significantly expressed in hepatocytes under basal conditions, and IL-1 induced LMP2 within 6–12 h of treatment. CYP2B protein degradation in response to IL-1 was attenuated by the selective LMP2 inhibitor UK-101, but not by the LMP7 inhibitor IPSI. The results show that LMP2 contributes to the NO-dependent degradation of CYP2B proteins, and suggest that induction of LMP2 may be involved in the potentiation of this degradation by IL-1. |
| تدمد: | 1470-8728 0264-6021 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1968718a28a4cba4d1a0a93c1862d081Test https://doi.org/10.1042/bj20120820Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....1968718a28a4cba4d1a0a93c1862d081 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14708728 02646021 |
|---|