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Titolo:
BOTH MURINE SAA(1) AND SAA(2) YIELD AA AMYLOID IN ALVEOLAR HYDATID CYST-INFECTED MICE
Autore:
BELL AW; CHAN SL; MARCANTONIO D; ALIKHAN Z;
Indirizzi:
MCGILL UNIV,DEPT MICROBIOL & IMMUNOL,3775 UNIV ST MONTREAL PQ H3A 2B4CANADA MCGILL UNIV,DEPT MICROBIOL & IMMUNOL MONTREAL PQ H3A 2B4 CANADA MCGILL UNIV,DEPT ANAT & CELL BIOL MONTREAL PQ H3A 2B4 CANADA
Titolo Testata:
Scandinavian journal of immunology
fascicolo: 2, volume: 43, anno: 1996,
pagine: 173 - 180
SICI:
0300-9475(1996)43:2<173:BMSASY>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
SERUM-PROTEIN SAA; SECONDARY AMYLOIDOSIS; MOUSE; AMYLOIDOGENESIS; DEPOSITS; DEGRADATION; UBIQUITIN; PROTEASES; SEQUENCE; APOSAA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
52
Recensione:
Indirizzi per estratti:
Citazione:
A.W. Bell et al., "BOTH MURINE SAA(1) AND SAA(2) YIELD AA AMYLOID IN ALVEOLAR HYDATID CYST-INFECTED MICE", Scandinavian journal of immunology, 43(2), 1996, pp. 173-180

Abstract

Amyloid susceptible C57BL/6 and partially amyloid resistant A/J mice,infected intraperitoneally with 250 alveolar hydatid cyst (AHC), the larval stage of ii cestode parasite Echinococcus multilocularis, develop multiple organ amyloid deposits at approximately 1 and 4 weeks postinfection (p.i.), respectively. Pooled spleens and livers from each mouse strain, at 8 and 10 weeks p.i., were used for the purification ofprotein AA utilizing a HiLoad Superdex 200 column equilibrated with 5M guanidine-HCl. Protein AA from each mouse strain was separated on 16% Tris-tricine SDS-PAGE gels and immunoblotted with monospecific rabbit anti-mouse AA IgG; five and six immunoreactive AA subspecies were detected in the C57BL/6 and A/J materials, respectively. N-Terminal amino acid sequence analysis was performed on the bulk column-purified protein AA as well as on the electroblotted AA subspecies from each mousestrain. The results show a mixture of serum amyloid A(1) (SAA(1)) and(SAA(2))-derived AA protein from each mouse strain; SAA(1)-derived AA, although alluded to, has never been demonstrated as tissue deposits in mice. These findings suggest that the intense and persistent inflammatory processes in AHC-infected mice may have induced conversion of weakly amyloidogenic SAA(1) to AA. This conversion could be detected byamino acid sequencing of electrophoretically separated AA subspecies.

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Documento generato il 21/09/20 alle ore 19:17:23