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Titolo:
Design and synthesis of sensitive fluorogenic substrates specific for Lys-gingipain
Autore:
Abe, N; Baba, A; Kadowaki, T; Okamoto, K; Okazaki, S; Asao, T; Yamamoto, K;
Indirizzi:
Kyushu Univ, Grad Sch Dent Sci, Dept Pharmacol, Higashi Ku, Fukuoka 8128582, Japan Kyushu Univ Fukuoka Japan 8128582 ol, Higashi Ku, Fukuoka 8128582, Japan Taiho Pharmaceut Co Ltd, Res Ctr, Hanno, Saitama 3578527, Japan Taiho Pharmaceut Co Ltd Hanno Saitama Japan 3578527 aitama 3578527, Japan
Titolo Testata:
JOURNAL OF BIOCHEMISTRY
fascicolo: 5, volume: 128, anno: 2000,
pagine: 877 - 881
SICI:
0021-924X(200011)128:5<877:DASOSF>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
HISTIDINE-RICH POLYPEPTIDES; PORPHYROMONAS-GINGIVALIS; CYSTEINE PROTEINASE; ARG-GINGIPAIN; PERIODONTAL-DISEASE; CATHEPSIN-H; PURIFICATION; FORMS; INVOLVEMENT; VIRULENCE;
Keywords:
cysteine proteinase; fluorogenic substrate; Lys-gingipain; periodontitis; Porphyromonas gingivalis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
20
Recensione:
Indirizzi per estratti:
Indirizzo: Yamamoto, K Kyushu Univ, Grad Sch Dent Sci, Dept Pharmacol, Higashi Ku, Fukuoka 8128582, Japan Kyushu Univ Fukuoka Japan 8128582 Ku, Fukuoka 8128582, Japan
Citazione:
N. Abe et al., "Design and synthesis of sensitive fluorogenic substrates specific for Lys-gingipain", J BIOCHEM, 128(5), 2000, pp. 877-881

Abstract

Lys-gingipain (Kgp) is a major cysteine proteinase produced by the oral anaerobic bacterium Porphyromonas gingivalis, and has been implicated as a major pathogen in the development and progression of advanced adult periodontitis, This enzyme is believed to act as a major virulence factor of the disease, yet there exist no convenient and sensitive substrates for analyzing its biological activity. For a better understanding of the importance of this enzyme in the organism, there is an urgent need for specific substrates,Here we designed and synthesized two peptide 4-methyl-coumaryl-7-amides (RICA), carbobenzoxy (Z)-His-Glu-Lys-MCA, and Z-Glu-Lys-MCA, and tested theirpossible use as sensitive substrates for Kgp with limited specificity. Both substrates exhibited greater k(cat)/K-m values than the best known Kgp substrates described so far. Both substrates were resistant to Arg-gingipain,another pathogenic cysteine proteinase from P, gingivalis, as well as trypsin and cathepsins B, L, and a The levels of Kgp in various microorganisms and human cells were determined with Z-His-Glu-Lys-MCA Little or no Kgp-like activity was detected in either other microorganisms or human cells tested. These results indicate that the present substrates are a valuable and fast tool for routine assays and for mechanistic studies on Kgp.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 07:02:25