Wu S., Ootawa T., Sekio R., Smith H., Islam M.Z., Uno Y., Shiraishi M., Miyamoto A. . Involvement of beta3-adrenergic receptors in relaxation mediated by nitric oxide in chicken bas2023 · 記述言語： 英語 掲載種別： 研究論文（学術雑誌） 出版者・発行元： Poultry Science The response of basilar arteries to noradrenaline varies among many animal species, but remains little studied in poultry. Accordingly, we aimed to characterize the adrenergic receptor (AR) subtypes that modulate vascular response in basilar arteries in the chicken, with isometric recording of arterial ring tension using an organ bath. We demonstrated the presence of both alpha and beta (α and β) receptor subtypes through evaluating the response to noradrenaline, with and without a range of β-AR and α-AR antagonists. The concentration-dependent relaxations then induced by a range of β-AR agonists indicated a potency ranking of isoproterenol > noradrenaline > adrenaline > procaterol. We then investigated the effects of β-AR antagonists that attenuate the effect of isoproterenol (propranolol for β1,2,3-ARs, atenolol for β1-ARs, butoxamine for β2-ARs, and SR 59230A for β3-ARs), with Schild regression analysis, ascertaining multiple β-AR subtypes, with neither the β1-AR nor the β2-AR as the dominant subtype. SR 59230A was the only antagonist to yield a pA2 value (7.52) close to the reported equivalent for the relevant receptor subtype. Furthermore, treatment with SR 58611 (a β3-AR agonist) induced relaxation, which was inhibited (P < 0.01) by L-NNA and SR 59230A. Additionally, treating basilar arterial strips (containing endothelium) with SR 58611 induced nitric oxide (NO) production, which was inhibited (P < 0.01) by L-NNA and SR 59230A. Based on this first characterization of AR subtypes in chicken basilar arteries (to our knowledge), we suggest that α- and β-ARs are involved in contraction and relaxation, and that β3-ARs, especially those on the endothelium, may play an important role in vasodilation via NO release. DOI： 10.1016/j.psj.2023.102633 Scopus PubMed
Uno Y, Morikuni S, Shiraishi M, Asano A, Kawaguchi H, Murayama N, Yamazaki H . A comprehensive analysis of six forms of cytochrome P450 2C (CYP2C) in pigs. . Xenobiotica; the fate of f2022 · 記述言語： 英語 掲載種別： 研究論文（学術雑誌） 出版者・発行元： Xenobiotica Pigs are an important species used in drug metabolism studies; however, the cytochromes P450 (P450s or CYPs) have not been fully investigated in pigs. In this study, pig CYP2C32, CYP2C33, CYP2C34, CYP2C36, CYP2C42, and CYP2C49 cDNAs were isolated and found to contain open reading frames of 490 or 494 amino acids that shared 64–82% sequence identity with human CYP2C8/9/18/19. Pig CYP2C genes formed a gene cluster in a genomic region that corresponded to that of the human CYP2C cluster; an additional gene cluster was formed by pig CYP2C33a and CYP2C33b distant from the first cluster but located in the same chromosome. Among the tissues analysed, these pig CYP2C mRNAs were preferentially expressed in liver, small intestine, and/or kidney; pig CYP2C49, CYP2C32, CYP2C34, and CYP2C33 mRNAs were the most abundant CYP2C mRNAs in liver, jejunum, ileum, and kidney, respectively. Metabolic assays showed that pig CYP2C proteins (heterologously expressed in Escherichia coli) metabolised typical human CYP2C substrates diclofenac, warfarin, and/or omeprazole. The results suggest that these pig CYP2Cs are functional enzymes able to metabolise human CYP2C substrates in liver and small intestine, just as human CYP2Cs do. DOI： 10.1080/00498254.2022.2148139 Scopus PubMed
