Return to search

Pathological and immunochemical characterization of secondary amyloidosis in chronic murine alveolar hydatidosis

Induction of amyloid and associated pathological changes induced by alveolar hydatid cysts (AHC), the larval stage of Echinococcus multilocularis, were studied in Balb/c, C57BL/6J, CBA and A/JAX strains of mice. The onset and incidence of amyloidosis in these four strains corresponded with the intensity of hepatic inflammation and not with the load of parasite biomass. The spleens of AHC-infected mice were more sensitive to amyloid deposition than livers or kidneys. Rabbit antisera raised against mouse AA-amyloid protein (Azocasein induced) was shown to cross-react with AHC-induced amyloid (AHCA). The immunological cross-reactivity was determined by three different assays: immunoperoxidase, indirect immunofluorescence and Ouchterlony tests. In order to determine the chemical nature of AHCA, it was extracted from the tissues of C57BL/6J mice at 12 weeks p.i., either in water or 6 M acid-urea buffer. The AHCA protein showed a molecular weight (Mw) of 8,000 daltons and a pI value of 5.3. Azocasein-induced and purified amyloid protein from C57BL/6J mice had a similar MW but a pI value of 5.8. The amino acid composition of purified AHCA presented a closer relationship of AHCA to senescence-induced (age associated) amyloid protein than to AA-amyloid. The role of AHC-derived factors in the pathogenesis of secondary amyloidosis was studied in vitro and in vivo. AHC-antigens were purified by affinity chromatography and by gel filtration on Sephacryl S-300. Purified AHC-antigens were cytotoxic and chemotactic when tested in vivo and phlogistic when introduced intradermally or intraperitoneally in mice. Furthermore, AHC-antigens were amyloidogenic. The injection of 1 mg i.p. in mice induced amyloid deposition after 96 hours in their spleens. In Balb/c, C57BL/6J and A/JAX mice, amyloid deposition was correlated with the appearance of an amyloid enhancing-like factor (AHC-AEF) in the spleens. AHC-AEF appeared just prior to amyloid deposition. The passive transfer of AHC-AEF t

Identiferoai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.72751
Date January 1985
CreatorsKarmi, Tarif Osama.
PublisherMcGill University
Source SetsLibrary and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada
LanguageEnglish
Detected LanguageEnglish
TypeElectronic Thesis or Dissertation
Formatapplication/pdf
CoverageDoctor of Philosophy (Department of Microbiology and Immunology.)
RightsAll items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated.
Relationalephsysno: 000213704, proquestno: AAINL20848, Theses scanned by UMI/ProQuest.

Page generated in 0.002 seconds