{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,7]],"date-time":"2026-02-07T13:51:36Z","timestamp":1770472296571,"version":"3.49.0"},"reference-count":34,"publisher":"Proceedings of the National Academy of Sciences","issue":"5","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1998,3,3]]},"abstract":"<jats:p>\n            Amyloid protein A (AA) amyloidosis is a consequence of some long-standing inflammatory conditions, and subsequently, an N-terminal fragment of the acute phase protein serum AA forms \u03b2-sheet fibrils that are deposited in different tissues. It is unknown why only some individuals develop AA amyloidosis. In the mouse model, AA amyloidosis develops after \u224825 days of inflammatory challenge. This lag phase can be shortened dramatically by administration of a small amount of amyloid extract containing an as yet undefined amyloid-enhancing factor. In the present study, we show that preformed amyloid-like fibrils made from short synthetic peptides corresponding to parts of several different amyloid fibril proteins exert amyloidogenic enhancing activity when given i.v. to mice at the induction of inflammation. We followed i.v. administered, radiolabeled, heterologous, synthetic fibrils to the lung and to the perifollicular area in the spleen and found that new AA\u2013amyloid fibrils developed on these preformed fibrils. Our findings thus show that preformed, synthetic, amyloid-like fibrils have an\n            <jats:italic>in vivo<\/jats:italic>\n            nidus activity and that amyloid-enhancing activity may occur, at least in part, through this mechanism. Our findings also show that fibrils of a heterologous chemical nature exert amyloid-enhancing activity.\n          <\/jats:p>","DOI":"10.1073\/pnas.95.5.2558","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T14:40:11Z","timestamp":1027694411000},"page":"2558-2563","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":121,"title":["Acceleration of amyloid protein A amyloidosis by amyloid-like synthetic fibrils"],"prefix":"10.1073","volume":"95","author":[{"given":"Katarzyna","family":"Johan","sequence":"first","affiliation":[{"name":"Division of Molecular and Immunological Pathology, University Hospital, S-581 85 Link\u00f6ping, Sweden; and Ludwig Institute for Cancer Research, Uppsala Branch, S-751 24 Uppsala, Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gunilla","family":"Westermark","sequence":"additional","affiliation":[{"name":"Division of Molecular and Immunological Pathology, University Hospital, S-581 85 Link\u00f6ping, Sweden; and Ludwig Institute for Cancer Research, Uppsala Branch, S-751 24 Uppsala, Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ulla","family":"Engstr\u00f6m","sequence":"additional","affiliation":[{"name":"Division of Molecular and Immunological Pathology, University Hospital, S-581 85 Link\u00f6ping, Sweden; and Ludwig Institute for Cancer Research, Uppsala Branch, S-751 24 Uppsala, Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"\u212bsa","family":"Gustavsson","sequence":"additional","affiliation":[{"name":"Division of Molecular and Immunological Pathology, University Hospital, S-581 85 Link\u00f6ping, Sweden; and Ludwig Institute for Cancer Research, Uppsala Branch, S-751 24 Uppsala, Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Per","family":"Hultman","sequence":"additional","affiliation":[{"name":"Division of Molecular and Immunological Pathology, University Hospital, S-581 85 Link\u00f6ping, Sweden; and Ludwig Institute for Cancer Research, Uppsala Branch, S-751 24 Uppsala, Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Per","family":"Westermark","sequence":"additional","affiliation":[{"name":"Division of Molecular and Immunological Pathology, University Hospital, S-581 85 Link\u00f6ping, Sweden; and Ludwig Institute for Cancer Research, Uppsala Branch, S-751 24 Uppsala, Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"341","published-online":{"date-parts":[[1998,3,3]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.3109\/13506129409148635"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)50605-6"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.169.5.1841"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.91.8.3186"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/0163-7258(89)90102-2"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.3109\/13506129609014375"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.159.2.641"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-3083.1987.tb02307.x"},{"key":"e_1_3_3_9_2","unstructured":"McAdam K. 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