2010 Fiscal Year Final Research Report
Biological Function of the M1 Family of Human Aminopeptidases
Project/Area Number |
20590057
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Biological pharmacy
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Research Institution | Kyoto University |
Principal Investigator |
HATTORI Akira Kyoto University, 薬学研究科, 准教授 (50300893)
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Project Period (FY) |
2008 – 2010
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Keywords | アミノペプチダーゼ / M1ファミリー / 抗原提示 / 阻害剤 / 部位特異的変異導入法 / 基質特異性 / 小胞体アミノペプチダーゼ / Laeverin |
Research Abstract |
Adipocyte-derived leucine aminopeptidase, leukocyte-derived arginine aminopeptidase and Laeverin are belonging to the M1 family of zinc-metallo aminopeptidases. In this study, biochemical and cell biological analyses were conducted to comprehend their catalytic mechanisms and characteristic subcellular localization/tissue distribution (endoplasmic reticulum retention or placenta specific expression). Several amino acid residues essential for catalysis were identified and genetic/cell biological tools (reporter plasmids and cell lines) were also established.
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Research Products
(19 results)
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[Journal Article] Probing the S1 specificity pocket of the aminopeptidases that generate antigenic peptides.2011
Author(s)
Zervoudi E, Papakyriakou A, Georgiadou D, Evnouchidou I, Gajda A, Poreba M, Salvesen GS, Drag M, Hattori A, Swevers L, Vourloumis D, Stratikos E.
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Journal Title
Biochem J 435
Pages: 411-420
Peer Reviewed
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[Presentation] Histidine-379 of human laeverin/aminopeptidase Q, a non-conserved residue within the exopeptidase motif, defines its distinctive enzymatic properties2009
Author(s)
Hattori A, Maruyama M, Arisaka Y, Goto Y, Ohsawa Y, Inoue H, Fujiwara H, Tsujimoto M
Organizer
6th General meeting of the International Proteolytic Society
Place of Presentation
Gold Coast, Australia.
Year and Date
2009-10-27
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