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Journal articles on the topic 'Soluble epoxide hydrolase subdomains'

Author: Grafiati

Published: 18 May 2024

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1

Gupta, Nandita C., Catherine M. Davis, Jonathan W. Nelson, Jennifer M. Young, and Nabil J. Alkayed. "Soluble Epoxide Hydrolase." Arteriosclerosis, Thrombosis, and Vascular Biology 32, no. 8 (August 2012): 1936–42. http://dx.doi.org/10.1161/atvbaha.112.251520.

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2

Sontakke, Pooja M., Suraj G. Malpani, Pooja R. Tange, MD Rayees Ahmad, and Vishweshwar M. Dharashive. "Soluble Epoxide Hydrolase." Asian Journal of Pharmaceutical Research and Development 12, no. 2 (April 15, 2024): 87–95. http://dx.doi.org/10.22270/ajprd.v12i2.1369.

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Epoxyeicosatrienoic acids (EETs) have numerous cardiovascular benefits, including vasodilation, anti-inflammatory actions, and anti-migratory effects on vascular smooth muscle cells. However, sEH, an enzyme that breaks down EETs into diols, limits these benefits. The development of sEH inhibitors (sEHIs), particularly those based on 1,3-disubstituted urea, has shown promise in enhancing the therapeutic properties of EETs. These inhibitors are antihypertensive and anti-inflammatory and can protect the heart, brain, and kidneys from damage. While there are still challenges to overcome, such as improving the drug-like properties of sEHIs and finding better ways to target specific tissues, the initiation of clinical trials for sEHIs highlights their potential as therapeutic agents.

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3

Yu, Zhigang, Benjamin B. Davis, Christophe Morisseau, Bruce D. Hammock, Jean L. Olson, Deanna L. Kroetz, and Robert H. Weiss. "Vascular localization of soluble epoxide hydrolase in the human kidney." American Journal of Physiology-Renal Physiology 286, no. 4 (April 2004): F720—F726. http://dx.doi.org/10.1152/ajprenal.00165.2003.

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Epoxyeicosatrienoic acids are cytochrome P-450 metabolites of arachidonic acid with multiple biological functions, including the regulation of vascular tone, renal tubular transport, cellular proliferation, and inflammation. Epoxyeicosatrienoic acids are converted by soluble epoxide hydrolase into the corresponding dihydroxyeicosatrienoic acids, and epoxyeicosatrienoic acid hydration is regarded as one mechanism whereby their biological effects are eliminated. Previous animal studies indicate that soluble epoxide hydrolase plays an important role in the regulation of renal eicosanoid levels and systemic blood pressure. To begin to elucidate the mechanism of these effects, we determined the cellular localization of soluble epoxide hydrolase in human kidney by examining biopsies taken from patients with a variety of non-end-stage renal diseases, as well as those without known renal disease. Immunohistochemical staining of acetone-fixed kidney biopsy samples revealed that soluble epoxide hydrolase was preferentially expressed in the renal vasculature with relatively low levels in the surrounding tubules. Expression of soluble epoxide hydrolase was evident in renal arteries of varying diameter and was localized mostly in the smooth muscle layers of the arterial wall. Western blot analysis and functional assays confirmed the expression of soluble epoxide hydrolase in the human kidney. There were no obvious differences in soluble epoxide hydrolase expression between normal and diseased human kidney tissue in the samples examined. Our results indicate that soluble epoxide hydrolase is present in the human kidney, being preferentially expressed in the renal vasculature, and support an essential role for this enzyme in renal hemodynamic regulation and its potential utility as a target for therapeutic intervention.

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4

Borhan, Babak, A. Daniel Jones, Franck Pinot, David F. Grant, Mark J. Kurth, and Bruce D. Hammock. "Mechanism of Soluble Epoxide Hydrolase." Journal of Biological Chemistry 270, no. 45 (November 10, 1995): 26923–30. http://dx.doi.org/10.1074/jbc.270.45.26923.

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5

Wang, Yi-Xin Jim, Arzu Ulu, Le-Ning Zhang, and Bruce Hammock. "Soluble Epoxide Hydrolase in Atherosclerosis." Current Atherosclerosis Reports 12, no. 3 (April 13, 2010): 174–83. http://dx.doi.org/10.1007/s11883-010-0108-5.

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6

Ma, Liang, Hailing Zhao, Meijie Yu, Yumin Wen, Tingting Zhao, Meihua Yan, Qian Liu, et al. "Association of Epoxide Hydrolase 2 Gene Arg287Gln with the Risk for Primary Hypertension in Chinese." International Journal of Hypertension 2020 (February 28, 2020): 1–7. http://dx.doi.org/10.1155/2020/2351547.

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Background. Epoxide hydrolase 2 (EPHX2) gene coding for soluble epoxide hydrolase is a potential candidate in the pathogenesis of hypertension. Objectives. We aimed to assess the association of a missense mutation, R287Q, in EPHX2 gene with primary hypertension risk and examine its association with enzyme activity of soluble epoxide hydrolase. Methods. This study involved 782 patients with primary hypertension and 458 healthy controls. Genotyping was done using TaqMan technique. Activity of soluble epoxide hydrolase fusion proteins was evaluated by the conversion of 11,12-EET to corresponding 11,12-DHET using ELISA kit. Results. After taking carriers of R287Q variant GG genotype as a reference, those with GA genotype had a significantly reduced risk of hypertension (adjusted odds ratio: 0.72, 95% confidence interval: 0.56 to 0.93, P = 0.013). Five significant risk factors were identified, including age, body mass index, total cholesterol, homocysteine, and R287Q variant. These five risk factors for hypertension were represented in a nomogram, with a descent prediction accuracy (C-index: 0.833, P<0.001). Enzyme activity of soluble epoxide hydrolase was significantly lower in the R287Q group than in the wild type group. Conclusions. We provide evidence that R287Q mutation in EPHX2 gene was associated with reduced risk of primary hypertension and low activity of soluble epoxide hydrolase.

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7

He, Xin, Wen-Yu Zhao, Bo Shao, Bao-Jing Zhang, Tian-Tian Liu, Cheng-Peng Sun, Hui-Lian Huang, Jia-Rong Wu, Jia-Hao Liang, and Xiao-Chi Ma. "Natural soluble epoxide hydrolase inhibitors from Inula helenium and their interactions with soluble epoxide hydrolase." International Journal of Biological Macromolecules 158 (September 2020): 1362–68. http://dx.doi.org/10.1016/j.ijbiomac.2020.04.227.

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8

Anita, Natasha Z., and Walter Swardfager. "Soluble Epoxide Hydrolase and Diabetes Complications." International Journal of Molecular Sciences 23, no. 11 (June 2, 2022): 6232. http://dx.doi.org/10.3390/ijms23116232.

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Type 2 diabetes mellitus (T2DM) can result in microvascular complications such as neuropathy, retinopathy, nephropathy, and cerebral small vessel disease, and contribute to macrovascular complications, such as heart failure, peripheral arterial disease, and large vessel stroke. T2DM also increases the risks of depression and dementia for reasons that remain largely unclear. Perturbations in the cytochrome P450-soluble epoxide hydrolase (CYP-sEH) pathway have been implicated in each of these diabetes complications. Here we review evidence from the clinical and animal literature suggesting the involvement of the CYP-sEH pathway in T2DM complications across organ systems, and highlight possible mechanisms (e.g., inflammation, fibrosis, mitochondrial function, endoplasmic reticulum stress, the unfolded protein response and autophagy) that may be relevant to the therapeutic potential of the pathway. These mechanisms may be broadly relevant to understanding, preventing and treating microvascular complications affecting the brain and other organ systems in T2DM.

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9

Bellevik, Stefan, Jiaming Zhang, and Johan Meijer. "Brassica napus soluble epoxide hydrolase (BNSEH1)." European Journal of Biochemistry 269, no. 21 (October 17, 2002): 5295–302. http://dx.doi.org/10.1046/j.1432-1033.2002.03247.x.

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10

Przybyla-Zawislak, Beata D., Punit K. Srivastava, Johana Vázquez-Matías, Harvey W. Mohrenweiser, Joseph E. Maxwell, Bruce D. Hammock, J. Alyce Bradbury, Ahmed E. Enayetallah, Darryl C. Zeldin, and David F. Grant. "Polymorphisms in Human Soluble Epoxide Hydrolase." Molecular Pharmacology 64, no. 2 (July 17, 2003): 482–90. http://dx.doi.org/10.1124/mol.64.2.482.

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11

Kramer, Jan, and Ewgenij Proschak. "Phosphatase activity of soluble epoxide hydrolase." Prostaglandins & Other Lipid Mediators 133 (November 2017): 88–92. http://dx.doi.org/10.1016/j.prostaglandins.2017.07.002.

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12

Zhao, Ting-Ting, Binaya Wasti, Dan-Yan Xu, Li Shen, Jian-Qing Du, and Shui-Ping Zhao. "Soluble epoxide hydrolase and ischemic cardiomyopathy." International Journal of Cardiology 155, no. 2 (March 2012): 181–87. http://dx.doi.org/10.1016/j.ijcard.2011.05.067.

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13

Zhao, Wen-Yu, Xin-Yue Zhang, Mei-Rong Zhou, Xiang-Ge Tian, Xia Lv, Hou-Li Zhang, Sa Deng, Bao-Jing Zhang, Cheng-Peng Sun, and Xiao-Chi Ma. "Natural soluble epoxide hydrolase inhibitors from Alisma orientale and their potential mechanism with soluble epoxide hydrolase." International Journal of Biological Macromolecules 183 (July 2021): 811–17. http://dx.doi.org/10.1016/j.ijbiomac.2021.04.187.

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14

Draper, A. J., and B. D. Hammock. "Soluble epoxide hydrolase in rat inflammatory cells is indistinguishable from soluble epoxide hydrolase in rat liver." Toxicological Sciences 50, no. 1 (July 1, 1999): 30–35. http://dx.doi.org/10.1093/toxsci/50.1.30.

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15

Nelson, Jonathan W., Rishi M. Subrahmanyan, Sol A. Summers, Xiangshu Xiao, and Nabil J. Alkayed. "Soluble Epoxide Hydrolase Dimerization Is Required for Hydrolase Activity." Journal of Biological Chemistry 288, no. 11 (January 28, 2013): 7697–703. http://dx.doi.org/10.1074/jbc.m112.429258.

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16

Klingler, Franca-Maria, Markus Wolf, Sandra Wittmann, Philip Gribbon, and Ewgenij Proschak. "Bacterial Expression and HTS Assessment of Soluble Epoxide Hydrolase Phosphatase." Journal of Biomolecular Screening 21, no. 7 (July 10, 2016): 689–94. http://dx.doi.org/10.1177/1087057116637609.

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Soluble epoxide hydrolase (sEH) is a bifunctional enzyme that possesses an epoxide hydrolase and lipid phosphatase activity (sEH-P) at two distinct catalytic domains. While the physiological role of the epoxide hydrolase domain is well understood, the consequences of the phosphatase activity remain unclear. Herein we describe the bacterial expression of the recombinant N-terminal domain of sEH-P and the development of a high-throughput screening protocol using a sensitive and commercially available substrate fluorescein diphosphate. The usability of the assay system was demonstrated and novel inhibitors of sEH-P were identified.

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17

Otake, Shinya, Norihiro Ogawa, Yoshikazu Kitano, Keiji Hasumi, and Eriko Suzuki. "Isoprene Side-chain of SMTP is Essential for Soluble Epoxide Hydrolase Inhibition and Cellular Localization." Natural Product Communications 11, no. 2 (February 2016): 1934578X1601100. http://dx.doi.org/10.1177/1934578x1601100223.

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SMTPs, a family of natural small molecules that effectively treat ischemic stroke, are subject to clinical development. SMTPs enhance plasminogen activation and inhibit soluble epoxide hydrolase (sEH), leading to promotion of endogenous thrombolysis and anti-inflammation. The SMTP molecule consists of a tricyclic γ-lactam moiety, an isoprene side-chain, and an N-linked side-chain. Here, we investigate the yet-to-be-characterized function of the isoprene side-chain of SMTPs in sEH inhibition and cellular distribution. The results demonstrated that oxidative modification as well as truncation of the side-chain abolished epoxide hydrolase inhibition. The introduction of a terminal hydroxy group exceptionally unaffected epoxide hydrolase, but led to impaired cellular localization, resulting in diminution of cellular epoxide hydrolase inhibition. Thus, the isoprene side-chain of SMTP is an important pharmacophore for epoxide hydrolase inhibition and cellular localization.

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18

Wang, Zhen-He, Benjamin B. Davis, De-Qian Jiang, Ting-Ting Zhao, and Dan-Yan Xu. "Soluble Epoxide Hydrolase Inhibitors and Cardiovascular Diseases." Current Vascular Pharmacology 11, no. 1 (December 1, 2012): 105–11. http://dx.doi.org/10.2174/1570161111309010105.

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19

Wang, Zhen-He, Benjamin B. Davis, De-Qian Jiang, Ting-Ting Zhao, and Dan-Yan Xu. "Soluble Epoxide Hydrolase Inhibitors and Cardiovascular Diseases." Current Vascular Pharmacology 11, no. 1 (January 1, 2013): 105–11. http://dx.doi.org/10.2174/157016113804547593.

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20

Simpkins, A. N., R. D. Rudic, S. Roy, H. J. Tsai, B. D. Hammock, and J. D. Imig. "Soluble epoxide hydrolase inhibition modulates vascular remodeling." American Journal of Physiology-Heart and Circulatory Physiology 298, no. 3 (March 2010): H795—H806. http://dx.doi.org/10.1152/ajpheart.00543.2009.

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The soluble epoxide hydrolase enzyme (SEH) and vascular remodeling are associated with cardiovascular disease. Although inhibition of SEH prevents smooth muscle cell proliferation in vitro, the effects of SEH inhibition on vascular remodeling in vivo and mechanisms of these effects remain unclear. Herein we determined the effects of SEH antagonism in an endothelium intact model of vascular remodeling induced by flow reduction and an endothelium denuded model of vascular injury. We demonstrated that chronic treatment of spontaneously hypertensive stroke-prone rats with 12-(3-adamantan-1-yl-ureido) dodecanoic acid, an inhibitor of SEH, improved the increment of inward remodeling induced by common carotid ligation to a level that was comparable with normotensive Wistar Kyoto rats. Similarly, mice with deletion of the gene responsible for the production of the SEH enzyme (Ephx2−/−) demonstrated enhanced inward vascular remodeling induced by carotid ligation. However, the hyperplastic response induced by vascular injury that denudes the endothelium was unabated by SEH inhibition or Ephx2 gene deletion. These results suggest that SEH inhibition or Ephx2 gene deletion antagonizes neointimal formation in vivo by mechanisms that are endothelium dependent. Thus SEH inhibition may have therapeutic potential for flow-induced remodeling and neointimal formation.

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21

Burmistrov, Vladimir, Christophe Morisseau, Dmitry Pitushkin, Dmitry Karlov, Robert R. Fayzullin, Gennady M. Butov, and Bruce D. Hammock. "Adamantyl thioureas as soluble epoxide hydrolase inhibitors." Bioorganic & Medicinal Chemistry Letters 28, no. 13 (July 2018): 2302–13. http://dx.doi.org/10.1016/j.bmcl.2018.05.024.

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22

Shen, Hong C. "Soluble epoxide hydrolase inhibitors: a patent review." Expert Opinion on Therapeutic Patents 20, no. 7 (April 29, 2010): 941–56. http://dx.doi.org/10.1517/13543776.2010.484804.

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23

Qiu, Hong, Ning Li, Jun-Yan Liu, Todd R. Harris, Bruce D. Hammock, and Nipavan Chiamvimonvat. "Soluble Epoxide Hydrolase Inhibitors and Heart Failure." Cardiovascular Therapeutics 29, no. 2 (February 24, 2011): 99–111. http://dx.doi.org/10.1111/j.1755-5922.2010.00150.x.

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24

Hwang, Sung Hee, Hsing-Ju Tsai, Jun-Yan Liu, Christophe Morisseau, and Bruce D. Hammock. "Orally Bioavailable Potent Soluble Epoxide Hydrolase Inhibitors." Journal of Medicinal Chemistry 50, no. 16 (August 2007): 3825–40. http://dx.doi.org/10.1021/jm070270t.

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25

Borhan, B., T. Mebrahtu, S. Nazarian, M. J. Kurth, and B. D. Hammock. "Improved Radiolabeled Substrates for Soluble Epoxide Hydrolase." Analytical Biochemistry 231, no. 1 (October 1995): 188–200. http://dx.doi.org/10.1006/abio.1995.1520.

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26

Kim, Jang Hoon, Bui Huu Tai, Seo Young Yang, Ji Eun Kim, Sang Kyum Kim, and Young Ho Kim. "Soluble Epoxide Hydrolase Inhibitory Constituents fromSelaginella tamariscina." Bulletin of the Korean Chemical Society 36, no. 1 (January 2015): 300–304. http://dx.doi.org/10.1002/bkcs.10068.

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27

Cronin, Annette, Martina Decker, and Michael Arand. "Mammalian soluble epoxide hydrolase is identical to liver hepoxilin hydrolase." Journal of Lipid Research 52, no. 4 (January 7, 2011): 712–19. http://dx.doi.org/10.1194/jlr.m009639.

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28

Serrano-Hervás, Eila, Marc Garcia-Borràs, and Sílvia Osuna. "Exploring the origins of selectivity in soluble epoxide hydrolase from Bacillus megaterium." Organic & Biomolecular Chemistry 15, no. 41 (2017): 8827–35. http://dx.doi.org/10.1039/c7ob01847a.

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Epoxide hydrolase (EH) enzymes catalyze the hydration of racemic epoxides to yield their corresponding vicinal diols. In this work, the Bacillus megaterium epoxide hydrolase (BmEH)-mediated hydrolysis of racemic styrene oxide (rac-SO) and its para-nitro styrene oxide (rac-p-NSO) derivative are computationally investigated using density functional theory (DFT).

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29

Hiesinger, Kerstin, Annika Schott, Jan S. Kramer, René Blöcher, Finja Witt, Sandra K. Wittmann, Dieter Steinhilber, et al. "Design of Dual Inhibitors of Soluble Epoxide Hydrolase and LTA4 Hydrolase." ACS Medicinal Chemistry Letters 11, no. 3 (October 30, 2019): 298–302. http://dx.doi.org/10.1021/acsmedchemlett.9b00330.

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30

Lorthioir, Aurelien, Dominique Guerrot, Robinson Joannides, and Jeremy Bellien. "Diabetic CVD – Soluble Epoxide Hydrolase as A Target." Cardiovascular & Hematological Agents in Medicinal Chemistry 10, no. 3 (July 1, 2012): 212–22. http://dx.doi.org/10.2174/187152512802651042.

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31

Anitha, K. N., and K. M. Geetha. "Soluble Epoxide Hydrolase: A Pharmaceutical Target for Inflammation." Research Journal of Pharmacy and Technology 12, no. 10 (2019): 5113. http://dx.doi.org/10.5958/0974-360x.2019.00886.2.

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32

Imig, John D., Ludek Cervenka, and Jan Neckar. "Epoxylipids and soluble epoxide hydrolase in heart diseases." Biochemical Pharmacology 195 (January 2022): 114866. http://dx.doi.org/10.1016/j.bcp.2021.114866.

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33

El-Sherbeni, Ahmed A., Rabia Bhatti, Fadumo A. Isse, and Ayman O. S. El-Kadi. "Identifying simultaneous matrix metalloproteinases/soluble epoxide hydrolase inhibitors." Molecular and Cellular Biochemistry 477, no. 3 (January 24, 2022): 877–84. http://dx.doi.org/10.1007/s11010-021-04337-5.

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34

Brenneis, Christian, Marco Sisignano, Ovidiu Coste, Kai Altenrath, Michael J. Fischer, Carlo Angioni, Ingrid Fleming, et al. "Soluble Epoxide Hydrolase Limits Mechanical Hyperalgesia during Inflammation." Molecular Pain 7 (January 2011): 1744–8069. http://dx.doi.org/10.1186/1744-8069-7-78.

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35

Hu, Jiong, Sarah Dziumbla, Jihong Lin, Sofia-Iris Bibli, Sven Zukunft, Julian de Mos, Khader Awwad, et al. "Inhibition of soluble epoxide hydrolase prevents diabetic retinopathy." Nature 552, no. 7684 (December 2017): 248–52. http://dx.doi.org/10.1038/nature25013.

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36

Imig, John D. "Cardiovascular Therapeutic Aspects of Soluble Epoxide Hydrolase Inhibitors." Cardiovascular Drug Reviews 24, no. 2 (June 2006): 169–88. http://dx.doi.org/10.1111/j.1527-3466.2006.00169.x.

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37

Nelson, Jonathan W., Anjali J. Das, Anthony P. Barnes, and Nabil J. Alkayed. "Disrupting Dimerization Translocates Soluble Epoxide Hydrolase to Peroxisomes." PLOS ONE 11, no. 5 (May 20, 2016): e0152742. http://dx.doi.org/10.1371/journal.pone.0152742.

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38

Imig, John D. "Epigenetic soluble epoxide hydrolase regulation causes endothelial dysfunction." Acta Physiologica 225, no. 1 (October 26, 2018): e13203. http://dx.doi.org/10.1111/apha.13203.

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39

Burmistrov, Vladimir, Christophe Morisseau, Kin Sing Stephen Lee, Diyala S. Shihadih, Todd R. Harris, Gennady M. Butov, and Bruce D. Hammock. "Symmetric adamantyl-diureas as soluble epoxide hydrolase inhibitors." Bioorganic & Medicinal Chemistry Letters 24, no. 9 (May 2014): 2193–97. http://dx.doi.org/10.1016/j.bmcl.2014.03.016.

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40

Purba, Endang R., Ami Oguro, and Susumu Imaoka. "Isolation and characterization of Xenopus soluble epoxide hydrolase." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1841, no. 7 (July 2014): 954–62. http://dx.doi.org/10.1016/j.bbalip.2014.03.010.

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41

Santos, Julia M., Jung-A. Park, Aby Joiakim, David A. Putt, Robert N. Taylor, and Hyesook Kim. "The role of soluble epoxide hydrolase in preeclampsia." Medical Hypotheses 108 (October 2017): 81–85. http://dx.doi.org/10.1016/j.mehy.2017.07.033.

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42

Imig, John D. "Epoxides and Soluble Epoxide Hydrolase in Cardiovascular Physiology." Physiological Reviews 92, no. 1 (January 2012): 101–30. http://dx.doi.org/10.1152/physrev.00021.2011.

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Epoxyeicosatrienoic acids (EETs) are arachidonic acid metabolites that importantly contribute to vascular and cardiac physiology. The contribution of EETs to vascular and cardiac function is further influenced by soluble epoxide hydrolase (sEH) that degrades EETs to diols. Vascular actions of EETs include dilation and angiogenesis. EETs also decrease inflammation and platelet aggregation and in general act to maintain vascular homeostasis. Myocyte contraction and increased coronary blood flow are the two primary EET actions in the heart. EET cell signaling mechanisms are tissue and organ specific and provide significant evidence for the existence of EET receptors. Additionally, pharmacological and genetic manipulations of EETs and sEH have demonstrated a contribution for this metabolic pathway to cardiovascular diseases. Given the impact of EETs to cardiovascular physiology, there is emerging evidence that development of EET-based therapeutics will be beneficial for cardiovascular diseases.

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43

Harris, Todd R., and Bruce D. Hammock. "Soluble epoxide hydrolase: Gene structure, expression and deletion." Gene 526, no. 2 (September 2013): 61–74. http://dx.doi.org/10.1016/j.gene.2013.05.008.

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44

Cui, Zhen, Bochuan Li, Yanhong Zhang, Jinlong He, Xuelian Shi, Hui Wang, Yinjiao Zhao, et al. "Inhibition of Soluble Epoxide Hydrolase Attenuates Bosutinib-Induced Blood Pressure Elevation." Hypertension 78, no. 5 (November 2021): 1527–40. http://dx.doi.org/10.1161/hypertensionaha.121.17548.

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Endothelial cells play a critical role in maintaining homeostasis of vascular function, and endothelial activation is involved in the initial step of atherogenesis. Previously, we reported that Abl kinase mediates shear stress–induced endothelial activation. Bosutinib, a dual inhibitor of Src and Abl kinases, exerts an atheroprotective effect; however, recent studies have demonstrated an increase in the incidence of side effects associated with bosutinib, including increased arterial blood pressure (BP). To understand the effects of bosutinib on BP regulation and the mechanistic basis for novel treatment strategies against vascular dysfunction, we generated a line of mice conditionally lacking c-Abl in endothelial cells (endothelial cell- Abl KO ). Knockout mice and their wild-type littermates ( Abl f/f ) were orally administered a clinical dose of bosutinib, and their BP was monitored. Bosutinib treatment increased BP in both endothelial cell- Abl KO and Abl f/f mice. Furthermore, acetylcholine-evoked endothelium-dependent relaxation of the mesenteric arteries was impaired by bosutinib treatment. RNA sequencing of mesenteric arteries revealed that the CYP (cytochrome P450)-dependent metabolic pathway was involved in regulating BP after bosutinib treatment. Additionally, bosutinib treatment led to an upregulation of soluble epoxide hydrolase in the arteries and a lower plasma content of eicosanoid metabolites in the CYP pathway in mice. Treatment with 1-Trifluoromethoxyphenyl-3-(1-propionylpiperidin-4-yl) urea, a soluble epoxide hydrolase inhibitor, reversed the bosutinib-induced changes to the eicosanoid metabolite profile, endothelium-dependent vasorelaxation, and BP. Thus, the present study demonstrates that upregulation of soluble epoxide hydrolase mediates bosutinib-induced elevation of BP, independent of c-Abl. The addition of soluble epoxide hydrolase inhibitor in patients treated with bosutinib may aid in preventing vascular side effects.

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45

Horti, A. G., Y. Wang, I. Minn, X. Lan, J. Wang, R. C. Koehler, N. J. Alkayed, R. F. Dannals, and M. G. Pomper. "18F-FNDP for PET Imaging of Soluble Epoxide Hydrolase." Journal of Nuclear Medicine 57, no. 11 (July 14, 2016): 1817–22. http://dx.doi.org/10.2967/jnumed.116.173245.

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46

Stapleton, Andrew, Jeffrey K. Beetham, Franck Pinot, Joan E. Garbarino, David R. Rockhold, Mendel Friedman, Bruce D. Hammock, and William R. Belknap. "Cloning and expression of soluble epoxide hydrolase from potato." Plant Journal 6, no. 2 (August 1994): 251–58. http://dx.doi.org/10.1046/j.1365-313x.1994.6020251.x.

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47

De Vivo, Marco, Bernd Ensing, Matteo Dal Peraro, German A. Gomez, David W. Christianson, and Michael L. Klein. "Proton Shuttles and Phosphatase Activity in Soluble Epoxide Hydrolase." Journal of the American Chemical Society 129, no. 2 (January 2007): 387–94. http://dx.doi.org/10.1021/ja066150c.

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48

Barbosa-Sicard, Eduardo, Timo Frömel, Benjamin Keserü, Ralf P. Brandes, Christophe Morisseau, Bruce D. Hammock, Thomas Braun, Marcus Krüger, and Ingrid Fleming. "Inhibition of the Soluble Epoxide Hydrolase by Tyrosine Nitration." Journal of Biological Chemistry 284, no. 41 (August 24, 2009): 28156–63. http://dx.doi.org/10.1074/jbc.m109.054759.

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Hu, J., S. Dziumbla, J. Lin, S. I. Bibli, K. Devraj, S. Liebner, H. P. Hammes, R. Popp, and I. Fleming. "P377Inhibition of the soluble epoxide hydrolase attenuates diabetic retinopathy." Cardiovascular Research 114, suppl_1 (April 1, 2018): S96. http://dx.doi.org/10.1093/cvr/cvy060.286.

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Hashimoto, Kenji. "Soluble epoxide hydrolase: a new therapeutic target for depression." Expert Opinion on Therapeutic Targets 20, no. 10 (August 24, 2016): 1149–51. http://dx.doi.org/10.1080/14728222.2016.1226284.

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