Studies on physiological functions of ovalbumin and occurrence of neural tube defects due to deprivation of ovalbumin in chick embryo.

2009 Fiscal Year Final Research Report

• Project/Area Number: 19580343
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Single-year Grants
• Section: 一般
• Research Field: Basic veterinary science/Basic zootechnical science
• Research Institution: Kagoshima University
• Principal Investigator: SUGIMOTO Yasushi Kagoshima University, 大学院・連合農学研究科, 教授 (10100736)
• Co-Investigator(Kenkyū-buntansha): OKA Tatsuzou 鹿児島大学, 農学部, 教授 (50116795) ; KUSAKABE Takahiro 九州大学, (連合)農学研究科(研究院), 准教授 (30253595)
• Project Period (FY): 2007 – 2009
• Keywords: オボアルブミン / セルピン / 形態形成因子 / 神経管閉鎖障害 / 遺伝子発現

Research Abstract

Ovalbumin has been classified as a homolog of serine protease inhibitor (serpin), although little is known of its function except that it may be a nutrient source. We have shown that, during embryonic development, native molecules of ovalbumin (N-ovalbumin) are incorporated into tissues without degradation while undergoing configurational changes into a heat-stable form called 'HS-ovalbumin.' Here, to investigate the indispensability of HS-ovalbumin, we utilized an in vitro culture method by which chick embryos isolated from eggs at Stage 7 (before the neural tube begins to close) could develop normally for up to 24h. When endogenous, remnant ovalbumin was blocked by adding anti-ovalbumin polyclonal IgG to the medium, the isolated embryos became irregular particularly in brain tissue, resulting in the so-called neural tube deficiency (NTD). The embryos with NTD showed reduced signals for apoptosis and cell proliferation. Moreover, IgG-treated embryos were rescued by adding a sufficient amount of HS-ovalbumin to the medium, attaining normal morphologies without NTD. HS-ovalbumin exhibited a higher rescue rate than N-ovalbumin and S-ovalbumin, the latter being another heat-stable counterpart that occurs artificially by heating N-ovalbumin in vitro. These results indicate that ovalbumin (particularly in the HS-form) is essential in embryonic organogenesis, including neural tube formation. present results show also that the ovalbumin-deprived embryos gave decreased in situ signals for TUNEL reagents and for PCNA/c-Myc proteins, which mirror changes in apoptosis and cell proliferation, respectively. Also the ovalbumin deprival affect the embryos on many gene expressions including differentiation-inducing factors related to morphogenesis. Expressions of FGF8 and slug have decreased markedly, whereas those of BMP4 and Pax3 have increased over 3-fold. However, whether each of these alterations is a cause or a result of morphogenetic aberrancy is unclear. Since ovalbumin belongs to the serpin superfamily, there is a possibility that it shows direct interactions with some crucial differentiation-inducing factors.

Research Products

• [Journal Article] Gene cloning and characterization of Streptococcus intermedius fimbriae involved in saliva-mediated aggregation. (2009)
  • Author(s): Yamaguchi, T, Matsumoto, M., Sugimoto, Y., Soutome, S., Oho, T.
  • Journal Title: Research in Microbiology 160 Pages: 809-816
  • Peer Reviewed
• [Journal Article] Effects of humidity-stabilizing sheets on the quality of bigeye tuna meat. (2009)
  • Author(s): Saito, K., Sugimoto, Y., et al
  • Journal Title: Food Science & Technology Research 15 Pages: 283-292
  • Peer Reviewed
• [Journal Article] Evaluation of the performance of osmotic dehydration sheets on freshness parameters in cold-stored beef biceps femoris... (2009)
  • Author(s): Saito, K., Ahhmed, A.M. Kawahara, S. Sugimoto, Y., et al
  • Journal Title: Meat Science 82 Pages: 260-265
  • Peer Reviewed
• [Journal Article] Improvement of foaming propertiy of egg white protein by phosphrorylation through dry-heating in the presence of pyrophosphate. (2009)
  • Author(s): Hayashi,. Y.H., Nagano, Enomoto, H., C-P. Li., Sugimoto, Y., Ubrahim., H.R., Hatta., H., Takeda, C., Aoki, T.
  • Journal Title: J Food Sci 74 Pages: 68-72
  • Peer Reviewed
• [Journal Article] Improvement of functional properties of bovine serum albumin through phosphorylation by dry-heating in the presence of pyrophosphate. (2008)
  • Author(s): Enomoto, H, Li CP, Morizane, K, Ibrahim HR, Sugimoto, Y, Ohki, S, Ohtomo, H, Aoki, T.
  • Journal Title: J. Food Sci 73(2) Pages: 84-91
  • Peer Reviewed
• [Journal Article] Improvement of Functional Properties of Ovotransferrin by Phosphorylation through Dry-heating in the Presence of Pyrophosphate. (2008)
  • Author(s): Hayashi, Y. Can-Peng Li, Enomoto, H. Ibrahim, HR, Sugimoto, Y. Aoki. T
  • Journal Title: Asian-Aust. J. Anim. Sci 21(4) Pages: 596-602
  • Peer Reviewed
• [Journal Article] ブナシメジ来ポリテンペルのHL-60細胞におけるアポトーシス誘導機構 (2008)
  • Author(s): 水本裕子、大野木宏、水谷滋利、榎木竜嗣、浅田起代蔵、杉元康志、加藤郁之進
  • Journal Title: 日本食品科学工学会誌 55 Pages: 612-618
  • Peer Reviewed
• [Journal Article] ブナシメジ由来Hypsiziprenol A9によるcAMP経路の抑制を介したHL-60細胞のアポトーシス誘導. (2008)
  • Author(s): 水本裕子, 大野木宏, 水谷滋利, 榎木竜嗣, 浅田起代蔵, 杉元康志, 加藤郁之0進
  • Journal Title: 日本きのこ学会会誌 16
  • Peer Reviewed
• [Journal Article] Transition of ovalbumin to thermostable structure entails conformational changes involving the reactive center loop. (2007)
  • Author(s): Shinohara, H, Horiuchi, M, Sato, M, Kurisaki, J, Kusakabe, T, Koga, K, Minami, Y, Aoki, T, Kato, I, Sugimoto, Y.
  • Journal Title: Biochim Biophys Acta 1770 Pages: 5-11
  • Peer Reviewed
• [Journal Article] Glycation and phosphorylation of beta-lactoglobulin by dry-heating: effect on protein structure and some properties. (2007)
  • Author(s): Enomoto, H, Li CP, Morizane, K, Ibrahim, HR, Sugimoto, Y, Ohki, S, Ohtomo, H, Aoki, T
  • Journal Title: J Agric Food Chem 55(6) Pages: 2392-2398
  • Peer Reviewed
• [Presentation] 日本分子生物学会、リゾチームアミロイド線維が細胞に与える影響 (2009)
  • Author(s): 木戸玲奈杉元康志, 他
  • Place of Presentation: 横浜市
  • Year and Date: 2009-12-10