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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1992-4-20
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pubmed:abstractText |
Crude amyloid enhancing factor (AEF) drastically reduces the pre-amyloid phase on passive transfer and induces amyloid deposition in the recipient mice in 48-120 h. We attempted to purify AEF from murine amyloidotic liver and spleen extracts by using gel filtration, preparative sodium dodecyl sulphate-polyacrylamide gel electrophoresis and ion exchange chromatography and isolated a 5.5 kDa peptide. In the mouse bioassay, this peptide induced accelerated splenic AA deposition in a dose-dependent manner. Based on structural, electrophoretic and immunochemical criteria the peptide was identified as ubiquitin. A polyclonal rabbit anti-bovine ubiquitin IgG antibody (RABU) abolished the in vivo AEF activity of crude murine AEF in a dose-dependent manner. Monomeric ubiquitin and its large molecular weight adducts were isolated from crude AEF using cyanogen bromide-activated sepharose conjugated to RABU and size exclusion chromatography methods. These were assayed and were found to possess AEF activity. Furthermore, increased levels of ubiquitin, a phenomenon similar to that of AEF, were detected by immunocytochemistry in mouse peritoneal leucocytes prior to and during amyloid deposition. Since AEF shares a number of biological and functional properties with ubiquitin, we suggest a possible role of ubiquitin as an AEF, and that serum amyloid protein A and ubiquitin, the two reactants generated during inflammatory stress conditions, may converge to induce AA amyloid deposition.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Caseins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins,
http://linkedlifedata.com/resource/pubmed/chemical/amyloid enhancing factor,
http://linkedlifedata.com/resource/pubmed/chemical/proteose-peptone
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pubmed:status |
MEDLINE
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pubmed:issn |
0174-7398
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
420
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
139-48
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1312754-Acute-Phase Reaction,
pubmed-meshheading:1312754-Amino Acid Sequence,
pubmed-meshheading:1312754-Amyloidosis,
pubmed-meshheading:1312754-Animals,
pubmed-meshheading:1312754-Caseins,
pubmed-meshheading:1312754-Disease Models, Animal,
pubmed-meshheading:1312754-Glycoproteins,
pubmed-meshheading:1312754-Macrophages,
pubmed-meshheading:1312754-Male,
pubmed-meshheading:1312754-Mice,
pubmed-meshheading:1312754-Mice, Inbred C57BL,
pubmed-meshheading:1312754-Molecular Sequence Data,
pubmed-meshheading:1312754-Neutrophils,
pubmed-meshheading:1312754-Peptide Fragments,
pubmed-meshheading:1312754-Ubiquitins
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pubmed:year |
1992
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pubmed:articleTitle |
Amyloid enhancing factor activity is associated with ubiquitin.
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pubmed:affiliation |
Department of Microbiology and Immunology, McGill University, Montreal, Quebec, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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