{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,9]],"date-time":"2026-01-09T17:09:18Z","timestamp":1767978558318,"version":"3.49.0"},"reference-count":0,"publisher":"Rockefeller University Press","issue":"6","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1995,6,1]]},"abstract":"<jats:p>Inbred strains of mice provide a model for studies of the pathogenesis of amyloid A (AA) amyloidosis. All susceptible strains of mice described to date codominantly express two serum amyloid A (apoSAA) isoforms, apoSAA1 and apoSAA2, of which only apoSAA2 serves as a precursor for amyloid fibrils. In previous studies, we have shown that the CE\/J strain, which produces a single, novel apoSAA isoform, apoSAACE\/J, is amyloid resistant. In the present study amyloid-resistant CE\/J females were mated with amyloid-susceptible CBA\/J males to produce F1 hybrid offspring which were then backcrossed to the parental CBA\/J mouse strain. Amyloid susceptibility was determined in 30 backcrossed mice 72 h after injection of murine amyloid enhancing factor and silver nitrate. ApoSAA isoforms in plasma were separated by isoelectric focusing gel electrophoresis and visualized after immunoblotting with anti-AA antiserum. Amyloid A fibrils in spleen homogenates were denatured by formic acid and AA protein was quantified by ELISA using anti-mouse apoSAA antibodies. Values &amp;lt; 5 apoSAA equivalent units were considered negative. 13 mice expressed an apoSAA1 and apoSAA2 doublet characteristic of CBA\/J mice, whereas 17 mice, expressed the apoSAACE\/J isoform codominantly with apoSAA1 and apoSAA2. The correlation of amyloid resistance to expression of the apoSAACE\/J isoform was absolute (17\/17 were negative; mean score 2.6 +\/- 0.17 [standard error of the mean] apoSAA equivalent units) and the correlation between amyloid susceptibility and the expression of apoSAA2\/apoSAA1 was also striking (12\/13 were amyloid positive; mean score 47.9 +\/- 9.0 [standard error of the mean] apoSAA equivalent units (P &amp;lt; 0.001). This is not significantly different from the 50% segregation of apoSAA phenotypes expected for linkage to a single gene. These results indicate that a single gene governs apoSAACE\/J expression and thus confers protection against amyloid deposition even in the presence of apoSAA1 and apoSAA2 isoforms and show for the first time that resistance to AA amyloidosis is a dominant trait governed by a single gene.<\/jats:p>","DOI":"10.1084\/jem.181.6.2249","type":"journal-article","created":{"date-parts":[[2004,6,24]],"date-time":"2004-06-24T07:56:10Z","timestamp":1088063770000},"page":"2249-2252","update-policy":"https:\/\/doi.org\/10.1084\/jem.crossmarkpolicy","source":"Crossref","is-referenced-by-count":14,"title":["Linkage of protection against amyloid fibril formation in the mouse to a single, autosomal dominant gene."],"prefix":"10.1084","volume":"181","author":[{"given":"W A","family":"Gonnerman","sequence":"first","affiliation":[{"name":"E. N. Rogers Memorial Veterans Affairs Hospital, Bedford, Massachusetts 01730, USA."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R","family":"Elliott-Bryant","sequence":"additional","affiliation":[{"name":"E. N. Rogers Memorial Veterans Affairs Hospital, Bedford, Massachusetts 01730, USA."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"I","family":"Carreras","sequence":"additional","affiliation":[{"name":"E. N. Rogers Memorial Veterans Affairs Hospital, Bedford, Massachusetts 01730, USA."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J D","family":"Sipe","sequence":"additional","affiliation":[{"name":"E. N. Rogers Memorial Veterans Affairs Hospital, Bedford, Massachusetts 01730, USA."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"E S","family":"Cathcart","sequence":"additional","affiliation":[{"name":"E. N. Rogers Memorial Veterans Affairs Hospital, Bedford, Massachusetts 01730, USA."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"291","published-online":{"date-parts":[[1995,6,1]]},"container-title":["The Journal of experimental medicine"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/rupress.org\/jem\/article-pdf\/181\/6\/2249\/1677520\/2249.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/rupress.org\/jem\/article-pdf\/181\/6\/2249\/1677520\/2249.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,7,25]],"date-time":"2023-07-25T06:56:27Z","timestamp":1690268187000},"score":1,"resource":{"primary":{"URL":"https:\/\/rupress.org\/jem\/article\/181\/6\/2249\/57607\/Linkage-of-protection-against-amyloid-fibril"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1995,6,1]]},"references-count":0,"journal-issue":{"issue":"6","published-print":{"date-parts":[[1995,6,1]]}},"URL":"https:\/\/doi.org\/10.1084\/jem.181.6.2249","relation":{},"ISSN":["0022-1007","1540-9538"],"issn-type":[{"value":"0022-1007","type":"print"},{"value":"1540-9538","type":"electronic"}],"subject":[],"published":{"date-parts":[[1995,6,1]]}}}