{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T17:23:55Z","timestamp":1787073835627,"version":"build-2736575974"},"reference-count":54,"publisher":"American Chemical Society (ACS)","issue":"12","license":[{"start":{"date-parts":[[2016,9,5]],"date-time":"2016-09-05T00:00:00Z","timestamp":1473033600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2016,9,5]],"date-time":"2016-09-05T00:00:00Z","timestamp":1473033600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2016,9,5]],"date-time":"2016-09-05T00:00:00Z","timestamp":1473033600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/501100000265","name":"Medical Research Council","doi-asserted-by":"publisher","award":["G0900580"],"award-info":[{"award-number":["G0900580"]}],"id":[{"id":"10.13039\/501100000265","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003621","name":"Ministry of Science, ICT and Future Planning","doi-asserted-by":"publisher","award":["2231-415"],"award-info":[{"award-number":["2231-415"]}],"id":[{"id":"10.13039\/501100003621","id-type":"DOI","asserted-by":"publisher"}]},{"name":"National Institute of Allergy & Infectious Disease, National Institutes of Health","award":["1-Z01-AI000752-12"],"award-info":[{"award-number":["1-Z01-AI000752-12"]}]},{"name":"National Institute of Allergy & Infectious Disease, National Institutes of Health","award":["1-Z01-AI001105-07"],"award-info":[{"award-number":["1-Z01-AI001105-07"]}]},{"name":"Fondation Alliance Biosecure"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2016,12,2]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Aggregated and protease-resistant mammalian prion protein (PrPSc) is the primary protein component of infectious prions. Enriched PrPSc preparations are often used to study the mechanisms that underly prion disease. However, most enrichment procedures are relatively nonspecific and tend to yield significant amounts of non-PrPSc components including various proteins that could confound functional and structural studies. It is thus important to identify these proteins and assess their potential relevance to prion pathogenesis. Following proteinase K treatment and phosphotungstic acid precipitation of brain homogenate, we have used mass spectrometry to analyze the protein content of PrPSc isolated from prion-infected mice, multiple cases of sporadic Creutzfeldt-Jakob disease (sCJD), and human growth hormone associated cases of iatrogenic CJD (iCJD). Creatine kinase was the primary protein contaminant in all PrPSc samples, while many of the other proteins identified were also found in non-CJD controls, which suggests that they are not CJD specific. Interestingly, the Alzheimer\u2019s disease associated peptide amyloid \u03b2 1\u201342 (A\u03b21\u201342) was identified in the majority of the sCJD cases as well as non-CJD age-matched controls, while apoliprotein E was found in greater abundance in the sCJD cases. By contrast, while some of the iCJD cases showed evidence of higher molecular weight A\u03b2 oligomers, monomeric A\u03b21\u201342 peptide was not detected by immunoblot, and only one case had significant levels of apolipoprotein E. Our data are consistent with the age-associated deposition of A\u03b21\u201342 in older sporadic CJD and non-CJD patients and suggest that both apolipoprotein E and A\u03b21\u201342 abundance can differ depending upon the type of CJD.<\/jats:p>","DOI":"10.1021\/acs.jproteome.6b00633","type":"journal-article","created":{"date-parts":[[2016,9,5]],"date-time":"2016-09-05T21:48:07Z","timestamp":1473112087000},"page":"4518-4531","source":"Crossref","is-referenced-by-count":3,"title":["Relative Abundance\nof apoE and A\u03b21\u201342\nAssociated with Abnormal Prion Protein Differs between Creutzfeldt-Jakob\nDisease Subtypes"],"prefix":"10.1021","volume":"15","author":[{"given":"Roger\nA.","family":"Moore","sequence":"first","affiliation":[{"name":"National Institutes of Health , , , ,","place":["Hamilton, Montana, United States, 59840"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Young Pyo","family":"Choi","sequence":"additional","affiliation":[{"name":"Korea Brain Research Institute , , ,","place":["Daegu, Republic of Korea, 41068"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark W.","family":"Head","sequence":"additional","affiliation":[{"name":"University of Edinburgh , , ,","place":["Edinburgh, U.K., EH8 9YL"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James W.","family":"Ironside","sequence":"additional","affiliation":[{"name":"University of Edinburgh , , ,","place":["Edinburgh, U.K., EH8 9YL"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert","family":"Faris","sequence":"additional","affiliation":[{"name":"National Institutes of Health , , , ,","place":["Hamilton, Montana, United States, 59840"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Diane L.","family":"Ritchie","sequence":"additional","affiliation":[{"name":"University of Edinburgh , , ,","place":["Edinburgh, U.K., EH8 9YL"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gianluigi","family":"Zanusso","sequence":"additional","affiliation":[{"name":"University of Verona , , ,","place":["Verona, Italy, 37129"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Suzette A.","family":"Priola","sequence":"additional","affiliation":[{"name":"National Institutes of Health , , , ,","place":["Hamilton, Montana, United States, 59840"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2016,9,5]]},"reference":[{"key":"2026081810433558500_cit1","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1093\/bmb\/66.1.1","article-title":"Introduction\nto the transmissible spongiform encephalopathies or prion diseases","volume":"66","author":"Chesebro","year":"2003","journal-title":"Br. Med. Bull."},{"key":"2026081810433558500_cit2","doi-asserted-by":"publisher","first-page":"14","DOI":"10.1016\/j.sbi.2008.12.007","article-title":"Prion protein misfolding and disease","volume":"19","author":"Moore","year":"2009","journal-title":"Curr. Opin. Struct. Biol."},{"key":"2026081810433558500_cit3","doi-asserted-by":"publisher","first-page":"177","DOI":"10.1146\/annurev.biochem.78.082907.145410","article-title":"Getting a\ngrip on prions:\noligomers, amyloids, and pathological membrane interactions","volume":"78","author":"Caughey","year":"2009","journal-title":"Annu. Rev. Biochem."},{"key":"2026081810433558500_cit4","doi-asserted-by":"publisher","first-page":"296","DOI":"10.1111\/j.1365-2990.2012.01265.x","article-title":"Review: Creutzfeldt-Jakob\ndisease: prion protein type,\ndisease phenotype and agent strain","volume":"38","author":"Head","year":"2012","journal-title":"Neuropathol.\nAppl. Neurobiol."},{"key":"2026081810433558500_cit5","doi-asserted-by":"publisher","first-page":"457","DOI":"10.1007\/978-94-007-5416-4_17","article-title":"Human prion diseases:\nfrom Kuru to variant Creutzfeldt-Jakob\ndisease","volume":"65","author":"Sikorska","year":"2012","journal-title":"Subcell. Biochem."},{"key":"2026081810433558500_cit6","doi-asserted-by":"publisher","first-page":"214","DOI":"10.1002\/rmv.725","article-title":"The contribution\nof different prion protein types and\nhost polymorphisms to clinicopathological variations in Creutzfeldt-Jakob\ndisease","volume":"22","author":"Head","year":"2012","journal-title":"Rev. Med. Virol."},{"key":"2026081810433558500_cit7","doi-asserted-by":"publisher","first-page":"618","DOI":"10.1016\/S1474-4422(12)70063-7","article-title":"Sporadic human prion\ndiseases: molecular insights and\ndiagnosis","volume":"11","author":"Puoti","year":"2012","journal-title":"Lancet Neurol."},{"key":"2026081810433558500_cit8","doi-asserted-by":"publisher","first-page":"286","DOI":"10.4161\/pri.29237","article-title":"Variant CJD: 18\nyears of research and surveillance","volume":"8","author":"Diack","year":"2014","journal-title":"Prion"},{"key":"2026081810433558500_cit9","doi-asserted-by":"publisher","first-page":"901","DOI":"10.3201\/eid1806.120116","article-title":"Iatrogenic\nCreutzfeldt-Jakob disease,\nfinal assessment","volume":"18","author":"Brown","year":"2012","journal-title":"Emerging Infect. 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Sci."},{"key":"2026081810433558500_cit45","doi-asserted-by":"publisher","first-page":"116","DOI":"10.1007\/s004010050870","article-title":"Coexistence\nof Alzheimer-type neuropathology in Creutzfeldt-Jakob\ndisease","volume":"96","author":"Hainfellner","year":"1998","journal-title":"Acta Neuropathol."},{"key":"2026081810433558500_cit46","doi-asserted-by":"publisher","first-page":"347","DOI":"10.1159\/000121389","article-title":"Association between\ndeposition of beta-amyloid and\npathological prion protein in sporadic Creutzfeldt-Jakob disease","volume":"5","author":"Debatin","year":"2008","journal-title":"Neurodegener. Dis."},{"key":"2026081810433558500_cit47","doi-asserted-by":"publisher","first-page":"413","DOI":"10.1136\/jnnp.2005.070805","article-title":"Alzheimer-type neuropathology in\na 28 year old patient with iatrogenic Creutzfeldt-Jakob disease after\ndural grafting","volume":"77","author":"Preusser","year":"2005","journal-title":"J. Neurol., Neurosurg. 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Wkly."},{"key":"2026081810433558500_cit49","doi-asserted-by":"publisher","first-page":"911","DOI":"10.1007\/s00401-016-1565-x","article-title":"Dura mater\nis a potential source of Abeta seeds","volume":"131","author":"Kovacs","year":"2016","journal-title":"Acta Neuropathol."},{"key":"2026081810433558500_cit50","doi-asserted-by":"publisher","first-page":"128","DOI":"10.1016\/S0140-6736(03)13867-6","article-title":"Distribution\nof codon 129 genotype in human growth hormone-treated CJD patients\nin France and the UK","volume":"362","author":"Brandel","year":"2003","journal-title":"Lancet"},{"key":"2026081810433558500_cit51","doi-asserted-by":"publisher","first-page":"3386","DOI":"10.1093\/brain\/awv235","article-title":"Iatrogenic\nCJD due to pituitary-derived growth hormone with genetically determined\nincubation times of up to 40 years","volume":"138","author":"Rudge","year":"2015","journal-title":"Brain"},{"key":"2026081810433558500_cit52","doi-asserted-by":"publisher","first-page":"613504","DOI":"10.1155\/2010\/613504","article-title":"Application\nof \u2033omics\u2033\nto prion biomarker discovery","volume":"2010","author":"Huzarewich","year":"2010","journal-title":"J. Biomed. Biotechnol."},{"key":"2026081810433558500_cit53","doi-asserted-by":"publisher","first-page":"365","DOI":"10.1007\/s004010000200","article-title":"Immunohistochemical detection of apolipoprotein E within\nprion-associated lesions in squirrel monkey brains","volume":"100","author":"Nakamura","year":"2000","journal-title":"Acta Neuropathol."},{"key":"2026081810433558500_cit54","doi-asserted-by":"publisher","first-page":"95","DOI":"10.1515\/BC.2006.013","article-title":"Detection of prion\nparticles in samples of BSE and scrapie by fluorescence correlation\nspectroscopy without proteinase K digestion","volume":"387","author":"Birkmann","year":"2006","journal-title":"Biol. Chem."},{"key":"2026081810433558500_cit55","doi-asserted-by":"publisher","first-page":"328","DOI":"10.1038\/ncb1841","article-title":"Prions hijack tunnelling nanotubes\nfor intercellular spread","volume":"11","author":"Gousset","year":"2009","journal-title":"Nat. Cell Biol."}],"container-title":["Journal of Proteome Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acs.jproteome.6b00633","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/jprobs\/article-pdf\/15\/12\/4518\/15514159\/pr6b00633.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/jprobs\/article-pdf\/15\/12\/4518\/15514159\/pr6b00633.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T16:24:05Z","timestamp":1787070245000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/jprobs\/article\/15\/12\/4518\/1464742\/Relative-Abundance-of-apoE-and-A-1-42-Associated"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,9,5]]},"references-count":54,"journal-issue":{"issue":"12","published-online":{"date-parts":[[2016,9,5]]},"published-print":{"date-parts":[[2016,12,2]]}},"URL":"https:\/\/doi.org\/10.1021\/acs.jproteome.6b00633","relation":{},"ISSN":["1535-3893","1535-3907"],"issn-type":[{"value":"1535-3893","type":"print"},{"value":"1535-3907","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,9,5]]}}}