Pentamines as Substrate for Human Spermine Oxidase

スポンサーリンク

概要

• 論文の詳細を見る

• Substrate activities of various linear polyamines to human spermine oxidase (hSMO) were investigated. The activities were evaluated by monitoring the amount of H2O2 released from sample polyamines by hSMO. H2O2 was measured by a HPLC method that analyzed fluorescent dimers derived from the oxidation of homovanillic acid in the presence of horseradish peroxidase. Six triamines were tested and were found not to be hSMO substrates. Of sixteen tetramines tested, spermine (Spm) was the most active substrate, followed by homospermine and N-butylated Spm. Pentamines showed a characteristic pattern of substrate activity. Of thirteen pentamines tested, 3343 showed higher substrate activity than Spm, and 4343 showed similar activity to Spm. The activities of the other pentamines were as follows: 3443, 4443, 4344, 3344, 4334, 4444, and 3334 (in decreasing order). Product amines released from these pentamines by hSMO were then analyzed by HPLC. Triamine was the only observed product, and the amount of triamine was nearly equivalent to that of released H2O2. A marked difference in the pH dependency curves between tetramines and pentamines suggested that hSMO favored reactions with a non-protonated secondary nitrogen at the cleavage site. The Km and Vmax values for Spm and 3343 at pH 7.0 and 9.0 were consistent with the higher substrate activity of 3343 compared to Spm, as well as with the concept of a non-protonated secondary nitrogen at the cleavage site being preferred, and 3343 was well degraded at a physiological pH by hSMO.

• 公益社団法人 日本薬学会の論文

著者

• Shirahata Akira

  Faculty Of Pharmaceutical Science Josai University

• Takao Koichi

  Laboratory Of Cellular Physiology Department Of Clinical Dietetics & Human Nutrition Faculty Of

• Sugita Yoshiaki

  Laboratory of Cellular Physiology, Department of Clinical Dietetics & Human Nutrition, Faculty of Ph

• Samejima Keijiro

  Department Of Analytical Chemistry Faculty Of Pharmaceutical Sciences Josai University

• Casero Jr.

  Department of Oncology, School of Medicine, Johns Hopkins University

• Igarashi Kazuei

  Amine Pharma Research Institute, Innovation Plaza at Chiba University

• Sugita Yoshiaki

  Laboratory of Bioorganic Chemistry, Department of Pharmaceutical Technochemistry, Josai University

• Casero Robert

  Department of Oncology, School of Medicine, Johns Hopkins University

• 杉田 義昭

  Laboratory of Bioorganic Chemistry, Department of Pharmaceutical Technochemistry, Josai University

関連論文

• Assay of N1-Acetylpolyamine Oxidase Activity with N1,N11-Didansylnorspermine as the Substrate by Ion-Pair Reversed Phase High Performance Liquid Chromatography
• Formation of Spermidine or Norspermidine from Synthetic Diacetylpolyamines by Acetylpolyamine Oxidase in Cultured Cells(Biochemistry)
• Regulation of estrogenic and nuclear factor κB functions by polyamines and their role in polyamineanalog-induced apoptosis of breast cancer cells
• Antitumor effect of bis(ethyl)polyamine analogs on mammarytumor development in FVB /NTgN (MMTVneu) transgenic mice
• Fluorometric Determination of 1,2,3,4-Tetrahydro-6,7-dihydroxyisoquinoline in Biological Materials by HPLC
• Conformational Stabilization of Rat S-Adenosylmethionine Decarboxylase by Putrescine
• Structural and Functional Relationship among Diamines in Terms of Inhibition of Cell Growth
• Polyamine Cytotoxicity in the Presence of Bovine SerumAmine Oxidase
• Inhibition of Cell Growth by Combination of α-Difluromethylornithine and an Inhibitor of Spermine Synthase
• A Molecular Beacon Strategy for ThermodynamicCharacterization of Triplex DNA : Triplex Formation atthe Promoter Region of Cyclin D1
• Control of Spermidine and Spermine Levels in Rat Tissues by trans-4-Methylcyclohexylamine, a Spermidine-Synthase Inhibitor(Analytical Biochemistry)
• Mammalian Spermidine Synthase : Identification of Cysteine Residues and Investigation of the Putrescine Binding Site(Analytical Biochemistry)
• Synthetic Decarboxylated S-Adenosyl-L-methionine as a Substrate for Aminopropyl Transferases
• Measurements of Macromolecule-Bound and Ultra-Filtrable Polyamines in Rat Liver Homogenized without Buffer
• Primary Structure of Rat Spermidine Synthase : An Example of Refining the cDNA-Derived Amino Acid Sequence
• Determination of Covalently Bound Hypusine and Deoxyhypusine to Protein Using Submilligram of Protein Samples by HPLC
• Specific Depletion of Spermidine and Spermine in HTC Cells Treated with Inhibitors of Aminopropyltransferases^1
• Long-Term Oral Polyamine Intake Increases Blood Polyamine Concentrations
• Antagonistic Effect of N - (3 - Aminopropyl)cyclohexylamine on Neurotrophic Action of Spermine in Primary Cultured Rat Hippocampal and Cerebellar Neurons
• Structural Requirement for Neurotrophic Activity of Spermine in Cultured Rat Hippocampal Neurons
• Mass Spectrometric Separation and Determination of N^1,N^-Diacetylspermine in the Urine of Cancer Patients
• Identification of the Primary Structure and Post-translational Modification of Rat S-Adenosylmethionine Decarboxylase
• Enhancement of Gastrointestinal Absorption of Ovalbumin Caused by Spermine Induces an Increase in Plasma Histamine Levels in Mice Sensitized to Ovalbumin
• Studies on Inhibition of Enzymatic Arginyltransfer Reaction
• Arginyl-tRNA-Protein Transferase Activities in Crude Supernatants of Rat Tissues
• Effects of Dehydroepiandrosterone on Oleic Acid Formation in the Liver of Rats, Mice and Guinea Pigs
• ACTIVE SITE OF AMINOPROPYLTRANSFERASES AND DEVELOPMENT OF INHIBITORS
• Pentamines as Substrate for Human Spermine Oxidase

もっと見る 閉じる

スポンサーリンク