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Titolo:
Consumption of peptide-derived arginine by a periodontopathogenic bacterium, Porphyromonas gingivalis
Autore:
Masuda, K; Tomita, K; Hayashi, H; Yoshioka, M; Hinode, D; Nakamura, R;
Indirizzi:
Univ Tokushima, Sch Dent, Dept Prevent Dent, Tokushima 7708504, Japan UnivTokushima Tokushima Japan 7708504 nt Dent, Tokushima 7708504, Japan
Titolo Testata:
ANAEROBE
fascicolo: 4, volume: 7, anno: 2001,
pagine: 209 - 217
SICI:
1075-9964(200108)7:4<209:COPABA>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
BACTEROIDES-GINGIVALIS; COLLAGENOLYTIC ACTIVITY; CULTURE SUPERNATANT; DEGRADATION; CATABOLISM; PROTEASE; ENZYME; ASACCHAROLYTICUS; DEIMINASE; STRAINS;
Keywords:
Porphyromonas gingivalis; amino acid consumption; arginine deiminase pathway; adenosine triphosphate production; periodontal disease;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Nakamura, R Univ Tokushima, Sch Dent, Dept Prevent Dent, 18-15 Kuramotocho3 Chome, Tokushima 7708504, Japan Univ Tokushima 18-15 Kuramotocho 3 ChomeTokushima Japan 7708504
Citazione:
K. Masuda et al., "Consumption of peptide-derived arginine by a periodontopathogenic bacterium, Porphyromonas gingivalis", ANAEROBE, 7(4), 2001, pp. 209-217

Abstract

The specificity of amino acid consumption by Porphyromonas gingivalis, well known as an important pathogen of adult periodontitis, is described. P. gingivalis is an asaccharolytic, black-pigmented and gram-negative anaerobe and produces several types of proteases including cysteine proteases. such as arg-gingipain and trypsin-like enzyme. This suggests that arginine is a possible energy source for its growth. When P. gingivalis was grown anaerobically in brain-heart infusion broth, several free amino acids such as lysine, glycine and glutamic acid increased in the culture supernatant with thebacterial growth; but free arginine increased first and then started to decrease after the early log phase. Citrulline and ornithine increased to late log phase in contrast to the decrease of arginine. The total arginine in the medium decreased steadily with the growth of P. gingivalis. In relationto the arginine consumption, cell extracts of P. gingivalis clearly demonstrated enzyme activities for the arginine deiminase pathway and adenosine triphosphate production. The arginine deiminase pathway was also presumed from the presence of putative homologue corresponding to the other bacterial arginine deiminase pathway relating enzymes in the unfinished P. gingivalisW83 genome. These results suggest that P. gingivalis catabolizes arginine which is released from proteins and/or peptides. by several types of proteases, and obtains energy through the arginine deiminase pathway. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/10/20 alle ore 08:29:54