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Titolo:
Temperature elevation regulates iron protoporphyrin IX and hemoglobin binding by Porphyromonas gingivalis
Autore:
Smalley, JW; Birss, AJ; Percival, R; Marsh, PD;
Indirizzi:
Univ Liverpool, Dept Clin Dent Sci, Oral Biol Unit, Liverpool L69 3GN, Merseyside, England Univ Liverpool Liverpool Merseyside England L69 3GN , Merseyside, England Univ Leeds, Leeds Dent Inst, Div Oral Biol, Unit Oral Microbiol, Leeds LS29LU, W Yorkshire, England Univ Leeds Leeds W Yorkshire England LS2 9LU LS29LU, W Yorkshire, England
Titolo Testata:
CURRENT MICROBIOLOGY
fascicolo: 5, volume: 41, anno: 2000,
pagine: 328 - 335
SICI:
0343-8651(200011)41:5<328:TERIPI>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEMIN-BINDING; PROTEASE ACTIVITY; W50; HEMAGGLUTINATION; VIRULENCE; MOSSBAUER; DISEASE; CLONING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Smalley, JW Univ Liverpool, Dept Clin Dent Sci, Oral Biol Unit, Edwards Bldg, Liverpool L69 3GN, Merseyside, England Univ Liverpool Edwards Bldg Liverpool Merseyside England L69 3GN
Citazione:
J.W. Smalley et al., "Temperature elevation regulates iron protoporphyrin IX and hemoglobin binding by Porphyromonas gingivalis", CURR MICROB, 41(5), 2000, pp. 328-335

Abstract

Porphyromonas gingivalis, an obligate anerobe with a growth requirement for iron protoporphyrin IX (FePPIX), is exposed to increased temperatures in the inflamed periodontal pocket. In this study, P. gingivalis was grown in a chemostat at 37 degreesC (control), 39 degreesC, and 41 degreesC, and examined for hemagglutinating (HA) activity, hemoglobin binding and degrading activity, and iron protoporphyrin IX binding. HA activity decreased in cells as the growth temperature increased. Binding of mu -oxo bishaem (dimeric haem), and Fe(II)- and Fe(III)-monomeric forms was increased in 39 degreesC-grown cells but decreased in 41 degreesC-grown cells compared with controls. Cellular hemoglobin binding and degradation decreased with increased growth temperature. The decrease in cellular hemagglutination and hemoglobin degradation occurring with increased growth temperature would limit the potential overproduction of toxic monomeric haem molecules. The increased binding of mu -oxo bishaem and monomeric forms of FePPIX at 39 degreesC may reflect a defense strategy against reactive oxidants and a mechanism of dampening down the inflammatory response to maintain an ecological balance.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 11:00:26