Ornithine decarboxylase antizyme - Its structure, role, regulation, and comparative biochemistry

鸟氨酸脱羧酶抗酶 - 其结构、作用、调节和比较生物化学

• 批准号: 63480131
• 负责人: HAYASHI Shin-ichi
• 金额: $ 4.35万
• 依托单位: The Jikei University School of Medicine
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for General Scientific Research (B)
• 财政年份: 1988
• 资助国家: 日本
• 起止时间: 1988 至 1989
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/en/grant/KAKENHI-PROJECT-63480131/
• 关键词: Ornithine decarboxylase; Antizyme; cDNA; Translational regulation; Frame-shift; mRNA; Half-life; Polyamines; アンチザイムインヒビター; 酵素分解; ラット; カエル

Ornithine decarboxylase (ODC) antizyme is a unique regulatory protein involved in feedback inhibition and possibly degradation of the enzyme. Following results were obtained in this second year of supported research.(1) Determination of base sequence of antizyme MRNASequence analysis of newly cloned CDNA and genomic DNA indicated that rat liver antizyme is consisted of 227 amino acids and that translation of antizyme MRNA is likely to involve a frame-shift, a very unusual process in bukaryotic cells. (Matsufuji)(2) Tissue distribution of antizyme MRNANorthern blot analysis demonstrated that a single species of antizyme MRNA of 1.3 kb was widely and amply distributed in various murine tissues. The MRNA was quite stable in vivo (T_<1/2> = 12 h) and its amount did not increase upon putrescine treatment, indicating that the induction of antizyme by polyamines is due to translational stimulation. (Matsufuji)Role of antizymeProtein synthesis inhibitors like emetine and pactamycin inhibited antizyme synthesis as well as polyamine-caused acceleration of ODC decay, while amino acid analogs like ethionine and 5-fluorotryptophan inhibited neither antizyme induction nor polyamine-caused acceleration of ODC decay, indicating a close relationship between these two processes. An antizyme overproducing variant cell line was obtained from ODC-overproducing CHO cells. Studies on half-lives of free and antizyme-bound ODC in this cell line strongly suggested antizyme-mediated degradation of ODC. (Murakami)(4) Presence and role of antizyme in the frog Xenopus laevisInduction of antizyme and acceleration of ODC decay were both observed in primary cultured frog hepatocytes. (Hayashi & Murakami)

鸟氨酸脱羧酶（ODC）抗酶是参与反馈抑制和可能降解酶的独特调节蛋白。 （1）确定新克隆的cDNA和基因组DNA的抗酶mrnasequence分析的基本序列（1）大鼠肝抗酶的确定基本序列，其中227个氨基酸由227个氨基酸组成，并且可能涉及抗iflesmeme mRNA的翻译，这可能涉及帧速度较差的细胞，这是一个非常不使用的bukaryotic in bukaryotial in bukaryorical in bukaryotial in bukaryotial in bukaryoric in bukaryorical in bukaryotil in bukaryotial in bukaryotil in bukaryotil in。 （Matsufuji）（2）抗酶mrnanorthern印迹分析的组织分布表明，在各种鼠组织中，一种单一的抗卵mRNA种类广泛且充分分布。 mRNA在体内非常稳定（T_ <1/2> = 12 h），其量子治疗后其量没有增加，这表明多胺通过转化刺激引起的抗酶。 （Matsufuji）抗卵蛋白合成抑制剂（如艾甲氨酸和帕塔梅霉素）的作用抑制了抗卵形合成以及odc衰变的多胺造成的加速度，而氨基酸类似物类似物（如乙氨酸和5-氟二磷蛋白）均不抑制了抗氮蛋白，均不相互抑制了这些指标的这些指标，这些指标是这些指标的od偶性散热量。两个过程。从ODC过多产生的CHO细胞获得了抗卵形过量生产的变异细胞系。在该细胞系中，对自由和抗体结合的ODC的半衰期的研究强烈建议抗酶介导的ODC降解。 （村上）（4）在原代培养的青蛙肝细胞中观察到抗卵形在抗卵形的青蛙爪蟾laevisy诱导中的存在和作用。 （Hayashi＆Murakami）

项目成果

S. Matsufuji, R. Kanamoto, Y. Murakami and S. Hayashi: "Monoclonal antibody studies on the properties and regulation of murine ornithine decarboxylase antizymes." J. Biochem. 107: 87-91 (1990).

S. Matsufuji、R. Kanamoto、Y. Murakami 和 S. Hayashi：“关于鼠鸟氨酸脱羧酶抗酶特性和调节的单克隆抗体研究”。

S.Hayashi: "Ornithine Decarboxylase:Biology,Enzymology,and Molecular Genetics." Pergamon Press, 147 (1989)

S.Hayashi：“鸟氨酸脱羧酶：生物学、酶学和分子遗传学。”

S. Matsufuji, T.G. Baby, R. Kanamoto, T. Kameji, Y. Murakamiand S. Hayashi: "Distribution and properties of ornithine decarboxylase antizyme." In: The Biology and Chemistry of Polyamines. (S.H. Goldemberg and I.D. Algranati, eds.) IRL Press Oxford, pp. 81

S.松藤，T.G.

S.Matsufuji: "Distribution and properties of ornithine decarboxylase antizyme.In S.H.Goldemberg and I.D.Algranati(eds.)The Biology and Chemistry of Polymines." IRL Press,Oxford, 81-90 (1989)

S.Matsufuji：“鸟氨酸脱羧酶抗酶的分布和特性。见 S.H.Goldemberg 和 I.D.Algranati（编辑）《多胺的生物学和化学》。”

Y.Murakami: Biochem.J.254. 367-372 (1988)

Y.Murakami：Biochem.J.254。