Aspartic Proteinases

1. Front Matter

   Pages i-xxvi

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2. Gastric Aspartic Proteinases: Plenary Lectures

   1. Comparison of the Active Site Specificity of the Aspartic Proteinases Based on a Systematic Series of Peptide Substrates

      • Ben M. Dunn, Paula E. Scarborough, W. Todd Lowther, Chetana Rao-Naik

      Pages 1-9

   2. The Molecular Structure of Human Progastricsin and its Comparison with that of Porcine Pepsinogen

      • Nadezhda Tarasova, Michael James, Stanley Moore, Anita Sielecki, Maia Chernaia

      Pages 11-18

   3. A New Way of Looking at Aspartic Proteinase Structures: A Comparison of Pepsin Structure to other Aspartic Proteinases in the Near Active Site Region

      • Natalia S. Andreeva, Alexey Bochkarev, Igor Pechik

      Pages 19-32

   4. Rearranging Pepsinogen and Pepsin by Protein Engineering

      • Xinli Lin, Jordan Tang

      Pages 33-40

   5. Comparative Investigations on Pig Gastric Proteases and Their Zymogens

      • Bent Foltmann, Kenneth Harlow, Gunnar Houen, Peter K. Nielsen, Per Sangild

      Pages 41-51

   6. Non-Mammalian Vertebrate Pepsinogens and Pepsins: Isolation and Characterization

      • Kenji Takahashi, Masao Tanji, Etsuko Yakabe, Akira Hirasawa, Senerath B. P. Athauda, Takashi Kageyama

      Pages 53-65

   7. Transcription Regulation of Human and Porcine Pepsinogen A

      • G. Pals, P. H. S. Meijerink, J. Defize, J. P. Bebelman, M. Strunk, F. Arwert et al.

      Pages 67-75

3. Gastric Aspartic Proteinases: Poster Reports

   1. A Comparative Study on Amino Acid Sequences of Three Major Isoforms of Human Pepsin A

      • Nadezhda Tarasova, Nancy D. Denslow, Benny F. Parten, Nha Tran, Hung P. Nhuyen, Arwyn Jones et al.

      Pages 77-81

   2. Molecular Mass Determination by Electrospray Mass Spectrometry of Human Pepsins, Gastricsin, and Porcine Pepsin A Variants

      • A. T. Jones, B. N. Green, S. P. Wood, N. B. Roberts

      Pages 83-89

   3. Evidence for Electrostatic Interactions in the S2 Subsite of Porcine Pepsin

      • Chetana Rao, Ben M. Dunn

      Pages 91-94

   4. Protein Engineering of Surface Loops: Preliminary X-Ray Analysis of the Chy155–165rhi Mutant

      • Raj R. V. Dhanaraj, Jim E. Pitts, Phil Nugent, Poonsook Orprayoon, Jon B. Cooper, Tom L. Blundell et al.

      Pages 95-99

   5. Seminal Progastricsin

      • Pal Bela Szecsi, Hans Lilja

      Pages 101-105

   6. Effects of Hydrocortisone on the Pepsinogen-Producing Cells in Rat Stomach Mucosa

      • Masao Ichinose, Shinko Tsukada, Kazumasa Miki, Nobuyuki Kakei, Masashi Matsushima, Naohisa Yahagi et al.

      Pages 107-113

   7. Effects of Omeprazole, a Proton Pump Inhibitor, on Pepsinogen-Producing Cells, with Special Reference to Neonatal Development

      • Nobuyuki Kakei, Masao Ichinose, Shinko Tsukada, Masae Tatematsu, Noriaki Tezuka, Naohisa Yahagi et al.

      Pages 115-123

   8. Transcription of Embryonic Chick Pepsinogen Gene is Affected by Mesenchymal Signals through its 5′-Flanking Region

      • Kimiko Fukuda, Hidetoshi Saiga, Sadao Yasugi

      Pages 125-129

   9. Serum Pepsinogen Values as Possible Markers for Evaluating the Possibility of Peptic Ulcer Recurrence under H2-Blocker Half-Dose Maintenance Therapy

      • Masashi Matsushima, Kazumasa Miki, Masao Ichinose, Nobuyuki Kakei, Naohisa Yahagi, Masahiro Kido et al.

      Pages 131-137

   10. The Clinical Application of the Serum Pepsinogen I And II Levels as a Mass Screening Method for Gastric Cancer

       • Masashi Matsushima, Kazumasa Miki, Masao Ichinose, Nobuyuki Kakei, Naohisa Yahagi, Takehisa Suzuki et al.

       Pages 139-143

   11. A Minute Gastric Cancer Detected by a New Screening Method Using Serum Pepsinogen I and II

       • Masashi Matsushima, Kazumasa Miki, Masao Ichinose, Nobuyuki Kakei, Naohisa Yahagi, Masahiro Kido et al.

       Pages 145-148

   12. Two Cases of Early Colorectal Cancer Associated with Gastric Adenoma Detected by Serum Pepsinogen Screening Method

       • Masashi Matsushima, Tomonori Wada, Kazumasa Miki, Masao Ichinose, Nobuyuki Kakei, Naohisa Yahagi et al.

       Pages 149-154

The 5th International Conference on Aspartic Proteinases was held on September 19 through 24, 1993, at Naito Museum of Pharmaceutical Science and Industry, Kawashima­ cho, Gifu Prefecture, Japan, about 15 miles northwest of Nagoya City. About 100 scientists attended the conference, including 52 from 14 countries outside Japan, and 32 papers were presented by invited speakers, and 58 papers as posters. The purpose of this conference was to present and discuss new information on the structure, function, and biology, and related topics, including biomedical implications, of aspartic proteinases, and this book is a collec­ tion of nearly all the papers presented at the meeting. Aspartic proteinases belong to one of the four major classes of proteinases, the others being serine, cysteine, and metalloproteinases, and are so called since they have two catalytic aspartic acid residues in common in their active sites. Most of them are optimally active at acidic pH, hence the long-used name "acid proteinases," which, indeed, was the major title of the first conference of this series. However, some of them are active at around neutral pH, indicating their physiological roles in a wider range of pH than hitherto considered.

• Amino acid
• Embryo
• Nucleotide
• Termination
• biosynthesis
• gene expression
• genes
• proteins
• saccharomyces cerevisiae
• transcription

• The University of Tokyo, Tokyo, Japan

  Kenji Takahashi

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