| First Author | Bell AW | Year | 1996 |
| Journal | Scand J Immunol | Volume | 43 |
| Issue | 2 | Pages | 173-80 |
| PubMed ID | 8633197 | Mgi Jnum | J:34855 |
| Mgi Id | MGI:82312 | Doi | 10.1046/j.1365-3083.1996.d01-26.x |
| Citation | Bell AW, et al. (1996) Both murine SAA1 and SAA2 yield AA amyloid in alveolar hydatid cyst-infected mice. Scand J Immunol 43(2):173-80 |
| abstractText | Amyloid susceptible C57BL/6 and partially amyloid resistant A/J mice, infected intraperitoneally with 250 alveolar hydatid cyst (AHC), the larval stage of a cestode parasite Echinococcus multilocularis, develop multiple organ amyloid deposits at approximately 1 and 4 weeks post infection (p.i.), respectively. Pooled spleens and livers from each mouse strain, at 8 and 10 weeks p.i., were used for the purification of protein AA utilizing a HiLoad Superdex 200 column equilibrated with 5 M 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 mouse strain. The results show a mixture of serum amyloid A1 (SAA1) and (SAA2)-derived AA protein from each mouse strain; SAA1-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 SAA1 to AA. This conversion could be detected by amino acid sequencing of electrophoretically separated AA subspecies. |
