1.
2.
3.
4.
5.
6.
7.
8.
9.
10.
11.
Kryukov, G.V.; Castellano, S.; Novoselov, S.V.; Lobanov, A.V.; Zehtab, O.; Guigó, R.; Gladyshev, V.N. Characterization of
mammalian selenoproteomes. Science 2003, 300, 1439–1443. [CrossRef] [PubMed]
Gladyshev, V.N.; Arnér, E.S.; Berry, M.J.; Brigelius-Flohé, R.; Bruford, E.A.; Burk, R.F.; Carlson, B.A.; Castellano, S.; Chavatte, L.;
Conrad, M.; et al. Selenoprotein Gene Nomenclature. J. Biol. Chem. 2016, 291, 24036–24040. [CrossRef] [PubMed]
Brigelius-Flohé, R.; Flohé, L. Selenium and redox signaling. Arch. Biochem. Biophys. 2017, 617, 48–59. [CrossRef] [PubMed]
Arnér, E.S.J. Common modifications of selenocysteine in selenoproteins. Essays Biochem. 2020, 64, 45–53. [CrossRef] [PubMed]
Ogasawara, Y.; Lacourciere, G.M.; Ishii, K.; Stadtman, T.C. Characterization of potential selenium-binding proteins in the
selenophosphate synthetase system. Proc. Natl. Acad. Sci. USA 2005, 102, 1012–1016. [CrossRef] [PubMed]
Bansal, M.P.; Oborn, C.J.; Danielson, K.G.; Medina, D. Evidence for two selenium binding proteins distinct from glutathione
peroxidase in mouse liver. Carcinogenesis 1989, 10, 541–546. [CrossRef]
Bansal, M.P.; Mukhopadhyay, T.; Scott, J.; Cook, R.G.; Mukhopadhyay, R.; Medina, D. DNA sequencing of a mouse liver protein
that binds selenium- implications for selenium’s mechanism of action in cancer prevention. Carcinogenesis 1990, 11, 2071–2073.
[CrossRef]
Steinbrenner, H.; Micoogullari, M.; Hoang, N.A.; Bergheim, I.; Klotz, L.-O.; Sies, H. Selenium-binding protein 1 (SELENBP1) is a
marker of mature adipocytes. Redox Biol. 2019, 20, 489–495. [CrossRef]
Pol, A.; Renkema, G.H.; Tangerman, A.; Winkel, E.G.; Engelke, U.F.; de Brouwer, A.P.M.; Lloyd, K.C.; Araiza, R.S.;
van den Heuvel, L.; Omran, H.; et al. Mutations in SELENBP1, encoding a novel human methanethiol oxidase, cause extraoral
halitosis. Nat. Genet. 2018, 50, 120–129. [CrossRef]
Chen, G.; Wang, H.; Miller, C.T.; Thomas, D.G.; Gharib, T.G.; Misek, D.E.; Giordano, T.J.; Orringer, M.B.; Hanash, S.M.; Beer, D.G.
Reduced selenium-binding protein 1 expression is associated with poor outcome in lung adenocarcinomas. J. Pathol. 2004,
202, 321–329. [CrossRef] [PubMed]
Li, T.; Yang, W.; Li, M.; Byun, D.S.; Tong, C.; Nasser, S.; Zhuang, M.; Arango, D.; Mariadason, J.M.; Augenlicht, L.H. Expression of
selenium-binding protein 1 characterizes intestinal cell maturation and predicts survival for patients with colorectal cancer.
Mol. Nutr. Food Res. 2008, 52, 1289–1299. [CrossRef] [PubMed]
Int. J. Mol. Sci. 2021, 22, 5334
12.
13.
14.
15.
16.
17.
18.
19.
20.
21.
22.
23.
24.
25.
26.
27.
28.
29.
30.
31.
32.
33.
34.
35.
36.
37.
18 of 20
Schott, M.; de Jel, M.M.; Engelmann, J.C.; Renner, P.; Geissler, E.K.; Bosserhoff, A.K.; Kuphal, S. Selenium-binding protein 1 is
down-regulated in malignant melanoma. Oncotarget 2018, 9, 10445–10456. [CrossRef] [PubMed]
Glatt, S.J.; Everall, I.P.; Kremen, W.S.; Corbeil, J.; Sásik, R.; Khanlou, N.; Han, M.; Liew, C.C.; Tsuang, M.T. Comparative gene expression analysis of blood and brain provides concurrent validation of selenbp1 up-regulation in schizophrenia.
Proc. Natl. Acad. Sci. USA 2005, 102, 15533–15538. [CrossRef] [PubMed]
Porat, A.; Sagiv, Y.; Elazar, Z. A 56-kDa selenium-binding protein participates in intra-Golgi protein transport. J. Biol. Chem. 2000,
275, 14457–14465. [CrossRef] [PubMed]
Jeong, J.Y.; Wang, Y.; Sytkowski, A.J. Human selenium binding protein-1 (hSP56) interacts with VDU1 in a selenium-dependent
manner. Biochem. Biophys. Res. Commun. 2009, 379, 583–588. [CrossRef]
Miyaguchi, K. Localization of Selenium-binding protein at the tips of rapidly extending protrusions. Histochem. Cell. Biol. 2004,
121, 371–376. [CrossRef]
Jamba, L.; Nehru, B.; Bansal, M.P. Redox modulation of selenium binding proteins by cadmium exposures in mice.
Mol. Cell Biochem. 1997, 177, 169–175. [CrossRef]
Lanfear, J.; Fleming, J.; Walker, M.; Harrison, P. Different patterns of regulation of the genes encoding the closely related 56 kDa
selenium-and acetaminophen-binding proteins in normal tissues and during carcinogenesis. Carcinogenesis 1993, 14, 335–340.
[CrossRef] [PubMed]
Pumford, N.R.; Martin, B.M.; Hinson, J.A. A metabolite of acetaminophen covalently binds to the 56 KDa selenium binding
protein. Biochem. Biophys. Res. Commun. 1992, 182, 1348–1355. [CrossRef]
Poland, A.; Knutson, J.C. 2,3,7,8-tetrachlorodibenzo-p-dioxin and related halogenated aromatic hydrocarbons: Examination of
the mechanism of toxicity. Annu. Rev. Pharmacol. Toxicol. 1982, 22, 517–554. [CrossRef] [PubMed]
Reyes, H.; Reisz-Porszasz, S.; Hankinson, O. Identification of the Ah receptor nuclear translocator protein (Arnt) as a component
of the DNA binding form of the Ah receptor. Science 1992, 256, 1193–1195. [CrossRef]
Fernandez-Salguero, P.M.; Hilbert, D.M.; Rudikoff, S.; Ward, J.M.; Gonzalez, F.J. Aryl-hydrocarbon receptor-deficient mice
are resistant to 2,3,7,8-tetrachlorodibenzo-p-dioxin-induced toxicity. Toxicol. Appl. Pharmacol. 1996, 140, 173–179. [CrossRef]
[PubMed]
Ishii, Y.; Hatsumura, M.; Ishida, T.; Ariyoshi, N.; Oguri, K. Significant induction of a 54-kDa protein in rat liver with homologous
alignment to mouse selenium binding protein by a coplanar polychlorinated biphenyl, 3,4,5,30 ,40 -pentachlorobiphenyl and
3-methylcholanthrene. Toxicol. Lett. 1996, 87, 1–9. [CrossRef]
Tsujimoto, S.; Ishida, T.; Takeda, T.; Ishii, Y.; Onomura, Y.; Tsukimori, K.; Takechi, S.; Yamaguchi, T.; Uchi, H.; Suzuki, S.O.; et al.
Selenium-binding protein 1: Its physiological function, dependence on aryl hydrocarbon receptors, and role in wasting syndrome
by 2,3,7,8-tetrachlorodibenzo-p-dioxin. Biochim. Biophys. Acta. 2013, 1830, 3616–3624. [CrossRef] [PubMed]
Murphy, R.C.; Gijón, M.A. Biosynthesis and metabolism of leukotrienes. Biochem. J. 2007, 405, 379–395. [CrossRef] [PubMed]
Coulthard, G.; Erb, W.; Aggarwal, V.K. Stereocontrolled organocatalytic synthesis of prostaglandin PGF2α in seven steps. Nature
2012, 489, 278–281. [CrossRef]
Figueiredo-Pereira, M.E.; Corwin, C.; Babich, J. Prostaglandin J2: A potential target for halting inflammation-induced neurodegeneration. Ann. N. Y. Acad. Sci. 2016, 1363, 125–137. [CrossRef] [PubMed]
Li, X.; Li, H.; Zhao, J.; Dai, Q.; Huang, C.; Jin, L.; Yang, F.; Chen, F.; Wang, O.; Gao, Y. Plasma ω-3 and ω-6 fatty acids in thyroid
diseases. Oncol. Lett. 2018, 16, 5433–5440. [CrossRef]
Asztalos, I.B.; Gleason, J.A.; Sever, S.; Gedik, R.; Asztalos, B.F.; Horvath, K.V.; Dansinger, M.L.; Lamon-Fava, S.; Schaefer, E.J.
Effects of eicosapentaenoic acid and docosahexaenoic acid on cardiovascular disease risk factors: A randomized clinical trial.
Metabolism 2016, 65, 1636–1645. [CrossRef]
Capdevila, J.; Chacos, N.; Werringloer, J.; Prough, R.A.; Estabrook, R.W. Liver microsomal cytochrome P-450 and the oxidative
metabolism of arachidonic acid. Proc. Natl. Acad. Sci. USA 1981, 78, 5362–5366. [CrossRef]
Johnson, A.L.; Edson, K.Z.; Totah, R.A.; Rettie, A.E. Cytochrome P450 ω-Hydroxylases in Inflammation and Cancer.
Adv. Pharmacol. 2015, 74, 223–262. [CrossRef] [PubMed]
Bardot, O.; Aldridge, T.C.; Latruffe, N.; Green, S. PPAR-RXR heterodimer activates a peroxisome proliferator response element
upstream of the bifunctional enzyme gene. Biochem. Biophys. Res. Commun. 1993, 192, 37–45. [CrossRef] [PubMed]
Reddy, J.K.; Hashimoto, T. Peroxisomal beta-oxidation and peroxisome proliferator-activated receptor alpha: An adaptive
metabolic system. Annu. Rev. Nutr. 2001, 21, 193–230. [CrossRef] [PubMed]
Zhang, J.; Lu, A.; Kong, L.; Zhang, Q.; Ling, E. Functional analysis of insect molting fluid proteins on the protection and regulation
of ecdysis. J. Biol. Chem. 2014, 289, 35891–35906. [CrossRef] [PubMed]
Kim, T.; Yang, Q. Peroxisome-proliferator-activated receptors regulate redox signaling in the cardiovascular system.
World J. Cardiol. 2013, 5, 164–174. [CrossRef] [PubMed]
Kunau, W.H.; Dommes, V.; Schulz, H. Beta-oxidation of fatty acids in mitochondria, peroxisomes, and bacteria: A century of
continued progress. Prog. Lipid Res. 1995, 34, 267–342. [CrossRef]
Kamijo, Y.; Hora, K.; Kono, K.; Takahashi, K.; Higuchi, M.; Ehara, T.; Kiyosawa, K.; Shigematsu, H.; Gonzalez, F.J.; Aoyama, T.
PPARalpha protects proximal tubular cells from acute fatty acid toxicity. J. Am. Soc. Nephrol. 2007, 18, 3089–3100. [CrossRef]
[PubMed]
Int. J. Mol. Sci. 2021, 22, 5334
38.
39.
40.
41.
42.
43.
44.
45.
46.
47.
48.
49.
50.
51.
52.
53.
54.
55.
56.
57.
58.
59.
60.
61.
62.
63.
19 of 20
Ohkawa, H.; Ohishi, N.; Yagi, K. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal. Biochem. 1979,
95, 351–358. [CrossRef]
Lee, E.K.; Shin, Y.J.; Park, E.Y.; Kim, N.D.; Moon, A.; Kwack, S.J.; Son, J.Y.; Kacew, S.; Lee, B.M.; Bae, O.N.; et al. Selenium-binding
protein 1: A sensitive urinary biomarker to detect heavy metal-induced nephrotoxicity. Arch. Toxicol. 2017, 91, 1635–1648.
[CrossRef]
Hatsumura, M.; Ishida, T.; Ishii, Y.; Ariyoshi, N.; Oguri, K.; Yoshimura, H. Effect of a coplanar PCB on lipid metabolism:
The remarkable difference between rats and guinea pigs. Fukuoka Igaku Zasshi 1995, 86, 135–143. [PubMed]
Rae, S.A.; Davidson, E.M.; Smith, M.J. Leukotriene B4, an inflammatory mediator in gout. Lancet 1982, 2, 1122–1124. [CrossRef]
Rand, A.A.; Barnych, B.; Morisseau, C.; Cajka, T.; Lee, K.S.S.; Panigrahy, D.; Hammock, B.D. Cyclooxygenase-derived proangiogenic metabolites of epoxyeicosatrienoic acids. Proc. Natl. Acad. Sci. USA 2017, 114, 4370–4375. [CrossRef]
Figueiredo-Pereira, M.E.; Rockwell, P.; Schmidt-Glenewinkel, T.; Serrano, P. Neuroinflammation and J2 prostaglandins: Linking
impairment of the ubiquitin-proteasome pathway and mitochondria to neurodegeneration. Front Mol. Neurosci. 2015, 7, 104.
[CrossRef]
Liston, T.E.; Roberts, L.J., 2nd. Transformation of prostaglandin D2 to 9 alpha, 11 beta-(15S)-trihydroxyprosta-(5Z,13E)-dien-1-oic
acid (9 alpha, 11 beta-prostaglandin F2): A unique biologically active prostaglandin produced enzymatically in vivo in humans.
Proc. Natl. Acad. Sci. USA 1985, 82, 6030–6034. [CrossRef] [PubMed]
Koda, N.; Tsutsui, Y.; Niwa, H.; Ito, S.; Woodward, D.F.; Watanabe, K. Synthesis of prostaglandin F ethanolamide by prostaglandin
F synthase and identification of Bimatoprost as a potent inhibitor of the enzyme: New enzyme assay method using LC/ESI/MS.
Arch. Biochem. Biophys. 2004, 424, 128–136. [CrossRef] [PubMed]
Pastel, E.; Pointud, J.C.; Loubeau, G.; Dani, C.; Slim, K.; Martin, G.; Volat, F.; Sahut-Barnola, I.; Val, P.; Martinez, A.; et al. Aldose reductases influence prostaglandin F2α levels and adipocyte differentiation in male mouse and human species. Endocrinology 2015,
156, 1671–1684. [CrossRef] [PubMed]
Avila, J.A.; Kiprowska, M.; Jean-Louis, T.; Rockwell, P.; Figueiredo-Pereira, M.E.; Serrano, P.A. PACAP27 mitigates an agedependent hippocampal vulnerability to PGJ2-induced spatial learning deficits and neuroinflammation in mice. Brain Behav.
2020, 10, 1–18. [CrossRef] [PubMed]
Funk, C.D. Prostaglandins and leukotrienes: Advances in eicosanoid biology. Science 2001, 294, 1871–1875. [CrossRef] [PubMed]
Mayatepek, E.; Hoffmann, G.F. Leukotrienes: Biosynthesis, metabolism, and pathophysiologic significance. Pediatr. Res. 1995,
37, 1–9. [CrossRef]
Kikuta, Y.; Kato, M.; Yamashita, Y.; Miyauchi, Y.; Tanaka, K.; Kamada, N.; Kusunose, M. Human leukotriene B4 omega-hydroxylase
(CYP4F3) gene: Molecular cloning and chromosomal localization. DNA Cell. Biol. 1998, 17, 221–230. [CrossRef]
Sutyak, J.; Austen, K.F.; Soberman, R.J. Identification of an aldehyde dehydrogenase in the microsomes of human polymorphonuclear leukocytes that metabolizes 20-aldehyde leukotriene B4. J. Biol. Chem. 1989, 264, 14818–14823. [CrossRef]
Baumert, T.; Huber, M.; Mayer, D.; Keppler, D. Ethanol-induced inhibition of leukotriene degradation by omega-oxidation.
Eur. J. Biochem. 1989, 182, 223–229. [CrossRef]
Lasker, J.M.; Chen, W.B.; Wolf, I.; Bloswick, B.P.; Wilson, P.D.; Powell, P.K. Formation of 20-hydroxyeicosatetraenoic acid,
a vasoactive and natriuretic eicosanoid, in human kidney. Role of Cyp4F2 and Cyp4A11. J. Biol. Chem. 2000, 275, 4118–4126.
[CrossRef] [PubMed]
Henderson, C.J.; Bammler, T.; Wolf, C.R. Deduced amino acid sequence of a murine cytochrome P-450 Cyp4a protein: Developmental and hormonal regulation in liver and kidney. Biochim. Biophys. Acta 1994, 1200, 182–190. [CrossRef]
Wu, C.C.; Mei, S.; Cheng, J.; Ding, Y.; Weidenhammer, A.; Garcia, V.; Zhang, F.; Gotlinger, K.; Manthati, V.L.; Falck, J.R.; et al.
Androgen-sensitive hypertension associates with upregulated vascular CYP4A12-20-HETE synthase. J. Am. Soc. Nephrol. 2013,
24, 1288–1296. [CrossRef] [PubMed]
Wang, T.; Fu, X.; Chen, Q.; Patra, J.K.; Wang, D.; Wang, Z.; Gai, Z. Arachidonic Acid Metabolism and Kidney Inflammation.
Int. J. Mol. Sci. 2019, 20, 3683. [CrossRef]
Rakhshandehroo, M.; Knoch, B.; Müller, M.; Kersten, S. Peroxisome proliferator-activated receptor alpha target genes. PPAR Res.
2010, 2010, 612089. [CrossRef] [PubMed]
Desvergne, B.; Wahli, W. Peroxisome proliferator-activated receptors: Nuclear control of metabolism. Endocr. Rev. 1999,
20, 649–688. [CrossRef]
Guan, Y.; Breyer, M.D. Peroxisome proliferator-activated receptors (PPARs): Novel therapeutic targets in renal disease. Kidney Int.
2001, 60, 14–30. [CrossRef]
Kroetz, D.L.; Yook, P.; Costet, P.; Bianchi, P.; Pineau, T. Peroxisome proliferator-activated receptor alpha controls the hepatic
CYP4A induction adaptive response to starvation and diabetes. J. Biol. Chem. 1998, 273, 31581–31589. [CrossRef] [PubMed]
Leid, M.; Kastner, P.; Chambon, P. Multiplicity generates diversity in the retinoic acid signalling pathways. Trends Biochem. Sci.
1992, 17, 427–433. [CrossRef]
Westin, M.A.; Hunt, M.C.; Alexson, S.E. Peroxisomes contain a specific phytanoyl-CoA/pristanoyl-CoA thioesterase acting
as a novel auxiliary enzyme in alpha- and beta-oxidation of methyl-branched fatty acids in mouse. J. Biol. Chem. 2007,
282, 26707–26716. [CrossRef] [PubMed]
Ueta, N. Biochemistry of Branched Chain Fatty Acids. J-Stage 1971, 20, 663–669. [CrossRef]
Int. J. Mol. Sci. 2021, 22, 5334
64.
65.
66.
67.
68.
69.
70.
71.
72.
73.
74.
20 of 20
Zhao, C.; Zeng, H.; Wu, R.T.; Cheng, W.H. Loss of Selenium-Binding Protein 1 Decreases Sensitivity to Clastogens and Intracellular
Selenium Content in HeLa Cells. PLoS ONE 2016, 11, e0158650. [CrossRef]
Liu, X.; Jang, S.S.; An, Z.; Song, H.; Kim, W.D.; Yu, J.R.; Park, W.Y. Fenofibrate decreases radiation sensitivity via peroxisome
proliferator-activated receptor α-mediated superoxide dismutase induction in HeLa cells. Radiat. Oncol. J. 2012, 30, 88–95.
[CrossRef]
McAdam, E.; Brem, R.; Karran, P. Oxidative Stress-Induced Protein Damage Inhibits DNA Repair and Determines Mutation Risk
and Therapeutic Efficacy. Mol. Cancer Res. 2016, 14, 612–622. [CrossRef]
Takeda, T.; Komiya, Y.; Koga, T.; Ishida, T.; Ishii, Y.; Kikuta, Y.; Nakaya, M.; Kurose, H.; Yokomizo, T.; Shimizu, T.; et al.
Dioxin-induced increase in leukotriene B4 biosynthesis through the aryl hydrocarbon receptor and its relevance to hepatotoxicity
owing to neutrophil infiltration. J. Biol. Chem. 2017, 292, 10586–10599. [CrossRef] [PubMed]
Iannelli, P.; Zarrilli, V.; Varricchio, E.; Tramontano, D.; Mancini, F.P. The dietary antioxidant resveratrol affects redox changes of
PPARalpha activity. Nutr. Metab. Cardiovasc. Dis. 2007, 17, 247–256. [CrossRef]
Lowry, O.H.; Rosebrough, N.J.; Farr, A.L.; Randall, R.J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 1951,
193, 265–275. [CrossRef]
Want, E.J.; Masson, P.; Michopoulos, F.; Wilson, I.D.; Theodoridis, G.; Plumb, R.S.; Shockcor, J.; Loftus, N.; Holmes, E.;
Nicholson, J.K. Global metabolic profiling of animal and human tissues via UPLC-MS. Nat. Protoc. 2013, 8, 17–32. [CrossRef]
[PubMed]
Jandri´c, Z.; Roberts, D.; Rathor, M.N.; Abrahim, A.; Islam, M.; Cannavan, A. Assessment of fruit juice authenticity using
UPLC-QToF MS: A metabolomics approach. Food Chem. 2014, 148, 7–17. [CrossRef] [PubMed]
Trygg, J.; Holmes, E.; Lundstedt, T. Chemometrics in metabonomics. J. Proteome Res. 2007, 6, 469–479. [CrossRef] [PubMed]
Gentleman, R.; Carey, V.J.; Huber, W.; Irizarry, R.A.; Dudoit, S. Bioinformatics and Computational Biology Solutions Using R
and Bioconductor; Springer: Heidelberg, Germany, 2005; pp. 397–420.
Matsumoto, Y.; Ishida, T.; Takeda, T.; Koga, T.; Fujii, M.; Ishii, Y.; Fujimura, Y.; Miura, D.; Wariishi, H.; Yamada, H. Maternal exposure to dioxin reduces hypothalamic but not pituitary metabolome in fetal rats: A possible mechanism for a fetus-specific
reduction in steroidogenesis. J. Toxicol. Sci. 2010, 35, 365–373. [CrossRef] [PubMed]
...