Faculty Profiles - OKAMOTO Kuniaki

MISC - OKAMOTO Kuniaki

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歯周病原性細菌のヘムおよびアミノ酸獲得機構

山本健二, 岡元邦彰, 門脇知子, 安部直子, 馬場貴代, 中山浩次

生化学 72 ( 8 ) 2000

カテプシンDおよびEの性状解析に有用な新しい合成基質の作製

安田善之, 岡元邦彰, 岡本美子, 景山節, 内山安男, 木南英紀, 山本健二

生化学 71 ( 8 ) 867 - 867 1999.8

Arginine- and lysine-specific gingipains from Porphyromonas gingivalis as major virulence factors of progressive periodontal disease.

山本健二, 門脇知子, 岡元邦彰, 安部直子, 中山浩次

炎症 18 ( 4 ) 259 - 264 1998

Structural and functional characterization of periodontal pathogenic cysteine proteinases from Porphyromonas gingivalis

K. Yamamoto, T. Kadowaki, K. Okamoto, K. Nakayama

Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme 42 ( 14 Suppl ) 2425 - 2432 1997.10

Biological roles of a novel class of cysteine proteinases from Porphyromonas gingivalis in periodontal disease progression

K Yamamoto, T Kadowaki, K Okamoto, N Abe, K Nakayama

MEDICAL ASPECTS OF PROTEASES AND PROTEASE INHIBITORS 15 139 - 149 1997

Language：English Publisher：I O S PRESS

We have studied the role of a novel class of cysteine proteinases from the oral anaerobic bacterium Porphyromonas gingivalis in periodontal disease progression. Two unique cysteine proteinases, so termed Arg-gingipain (RGP) and Lys-gingipain (KGP) due to their peptide cleavage specificity at arginine and lysine residues, respectively, have been implicated as major virulence factors in periodontal disease. Both enzymes are shown to be involved in the direct destruction of periodontal tissues and the disruption of normal host defense mechanisms. These enzymes have also been implicated in the hemagglutinating activity of the organism. To determine the structuraI, genetic, and functional relationships between the two enzymes, we have cloned the RGP- and KGP-encoding genes and ultimately constructed the rgp- or kgp-deficient mutants from the organism. In the course of this study, RGP has been shown to be encoded by two separate genes (rgpA and rgpB) on the chromosome of the organism. Deduced amino acid sequences of both RGP- and KGP-encoding genes revealed that the precursors of both enzymes were composed of at least four domains: the signal peptide, the NH2-terminal prosequence, the proteinase domain, and the COOH-terminal hemagglutinin domain. Although both enzymes were apparently different in the amino acid sequences of the NH2-terminal prosequences and the proteinase domains, their COOH-terminal hemagglutinin domains exhibited significant similarity. Analysis of the rgpA rgpB double mutant confirmed that RGP was a major virulence factor of the organism. However, the disruption of the KGP gene did not affect either the bactericidal activity of polymorphonucler cells or the hemagglutinin activity of the organism.

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ラットカテプシンE分子のN-結合型糖鎖の役割

池田仁子, 西下一久, 坂井英昭, 岡元邦彰, 筑波隆幸, 加藤有三, 山本健二

日本分子生物学会年会プログラム・講演要旨集 19 255 - 255 1996.8

Processing of exine protein and secretion protein by Porphyromonas gingivalis arginine peculiar cysteine proteinase (Arg-gingipain).

門脇知子, 中山浩次, 吉村文信, 岡元邦彰, 山本健二

日本分子生物学会年会プログラム・講演要旨集 19th 1996

Periodontal disease and pathogenic protease.

山本健二, 門脇知子, 岡元邦彰

モダンフィジシャン 16 ( 12 ) 1996

Structural comparison of the pathogenicity protease gene of Porphyromonas gingivalis.

岡元邦彰, 門脇知子, 中山浩次, 山本健二

日本分子生物学会年会プログラム・講演要旨集 19th 1996

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