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Vanillin reduction in the biosynthetic pathway of capsiate, a non-pungent component of Capsicum fruits, is catalyzed by cinnamyl alcohol dehydrogenase
Get PDFCapsicum fruits synthesize capsaicin from vanillylamine, which is produced from vanillin in a reaction catalyzed by a putative aminotransferase (pAMT). Capsiate, a non-pungent compound that is structurally similar to capsaicin, is synthesized from vanillyl alcohol rather than vanillylamine. Vanillyl alcohol is possibly generated by the enzymatic reduction of vanillin, but the enzyme responsible for this reaction is unknown. In the present study, we revealed that the vanillin reductase in the capsiate biosynthetic pathway is cinnamyl alcohol dehydrogenase (CAD), which is an enzyme involved in lignin synthesis. The reduction of vanillin to vanillyl alcohol was greater in the mature red fruit placental extract than in the immature green fruit placental extract. This reduction was suppressed by both N-(O-hydroxyphenyl) sulfinamoyltertiobutyl acetate, a specific inhibitor of CAD, and ethylenediaminetetraacetic acid, a metalloenzyme inhibitor. The CaCAD1 transcript levels in the placenta were higher in the red fruits than in the green fruits. A recombinant CaCAD1 protein obtained using an Escherichia coli expression system reduced vanillin to vanillyl alcohol. This reaction was suppressed by the CAD inhibitors. These results strongly suggest that CAD is the enzyme that catalyzes the reduction of vanillin to vanillyl alcohol during capsiate biosynthesis. Syntenic analyses indicated that genes encoding CAD and capsaicin synthase (Pun1) involved in capsiate biosynthesis were acquired before the pAMT gene during the evolution of the family Solanaceae. This raises the possibility that in the genus Capsicum, the capsiate biosynthetic pathway emerged before the pAMT-encoding gene was acquired as the final trigger for capsaicin biosynthesis.Article No.12384. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/
第八届 城西大学 中文演讲比赛
Get PDF日時：2022年10月30日(日)13：00～ オンラインで実施 主催：城西大学語学教育センター 後援：埼玉県・坂戸市・坂戸市教育委員会・鶴ヶ島市・鶴ヶ島市教育委員会・テレ玉・毎日新聞社・埼玉新聞社・坂戸市商工会・西入間青年会議所・城西大学同窓会・城西大学父母講演会 協力：NPO法人埼玉県日本中国友好協会・HSK日本実施委員
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Get PDF講師：宮田 真也（学校法人城西大学水田記念博物館大石化石ギャラリー（紀尾井町キャンパス）学芸員、城西大学理学部助教授） 学内（学生、教職員、学内勤務者）向け 開催日 ： 2022年6月15日（水）①10：00～11：00 ②15：10～16：10 ③17：20～18：20 各回先着12名 会場 ： 水田三喜男記念館 ２階 203教室 学外向け 開催日 ： 2022年7月30日（土）①10：00～11：00 ②15：00～16：00 会場 ： 水田三喜男記念館 ２階 203教室 対象：小学生以上 各回先着5組（1組3名まで）【申込先着順】 材料費：1000
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Get PDF運営メンバー【学⽣】⽥中真奈実、津⾦彩花、奈良原茉、祢津愛加、⼆⽊若菜、⼩鷹⿇湖、菅原楓、杉⼭咲樹、関⼤成、濵岡万珠、⾵澤愛海、相川花⾳、相原華⼦、⼿塚莉奈、坂井尚⼦、⼩野純鈴、⼟屋明寿美、椎名葵、久保美涼、⻑沢美歩、成⽥佳蓮、⽯島太⼦郎、⼤澤幸之助【教員】中⾥⾒真紀、⼭⽥ 沙奈恵、君羅好
S-Allyl-L-cysteine Promotes Cell Proliferation by Stimulating Growth Hormone Receptor/Janus Kinase 2/Phospholipase C Pathways and Promoting Insulin-Like Growth Factor Type-I Secretion in Primary Cultures of Adult Rat Hepatocytes
Get PDFThe mechanism of insulin-like growth factor type-I (IGF-I) secretion stimulated by S-allyl-L-cysteine (SAC) was investigated as part of a study of SAC-induced DNA synthesis and cell proliferation in primary cultures of adult rat hepatocytes. When 10−6 M SAC was added to the culture, the amount of IGF-I in the medium was significantly increased at 10 min. The peak IGF-I level (140 pg/mL) was observed 20 min after SAC stimulation. The SAC-induced IGF-I secretion was completely suppressed by a selective Janus kinase 2 (JAK2) inhibitor (TG101209), a selective phospholipase C (PLC) inhibitor (U-73122), an intracellular Ca2+ chelating agent (BAPTA-AM), and a granule secretion inhibitor (somatostatin). On the other hand, 10−6 M SAC-stimulated hepatocytes showed increased intracellular Ca2+ concentration in a time-dependent manner from 0 to 10 min. Phosphorylation of SAC-induced JAK2 and IGF-I receptor tyrosine kinase (RTK) was completely suppressed by TG101209. In addition, U-73122, BAPTA-AM, and somatostatin did not suppress SAC-induced JAK2 phosphorylation, but significantly suppressed SAC-induced IGF-I RTK phosphorylation. Furthermore, binding of the monoclonal antibody against growth hormone (GH) to GH receptor was dose-dependently suppressed by SAC on immunofluorescence. These results showed that SAC promotes cell proliferation by stimulating GH receptor/JAK2/phospholipase C pathways and promoting autocrine secretion of IGF-I in primary cultures of adult rat hepatocytes