| pubmed-article:14647039 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14647039 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:14647039 | lifeskim:mentions | umls-concept:C0221908 | lld:lifeskim |
| pubmed-article:14647039 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:14647039 | lifeskim:mentions | umls-concept:C0002716 | lld:lifeskim |
| pubmed-article:14647039 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:14647039 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:14647039 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:14647039 | pubmed:dateCreated | 2003-12-3 | lld:pubmed |
| pubmed-article:14647039 | pubmed:abstractText | Calcifying epithelial odontogenic tumors (CEOTs), also known as Pindborg tumors, are characterized by the presence of squamous-cell proliferation, calcification, and, notably, amyloid deposits. On the basis of immunohistochemical analyses, the amyloidogenic component had heretofore been deemed to consist of cytokeratin-related or other molecules; however, its chemical composition had never been elucidated. We have used our microanalytic techniques to characterize the protein nature of CEOT-associated amyloid isolated from specimens obtained from 3 patients. As evidenced by the results of amino-acid sequencing and mass spectrometry, the fibrils were found to be composed of a polypeptide of approximately 46 mer. This component was identical in sequence to the N-terminal portion of a hypothetical 153-residue protein encoded by the FLJ20513 gene cloned from the human KATO III cell line. That the amyloid protein was derived from this larger molecule was demonstrated by reverse transcription-polymerase chain reaction amplification of tumor-cell RNA where a full-length FLJ20513 transcript was found. Furthermore, immunohistochemical analyses revealed that the amyloid within the CEOTs immunostained with antibodies prepared against a synthetic FLJ20513-related dodecapeptide. Our studies provide unequivocal evidence that CEOT-associated amyloid consists of a unique and previously undescribed protein that we provisionally designate APin. | lld:pubmed |
| pubmed-article:14647039 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14647039 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14647039 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14647039 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:14647039 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14647039 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14647039 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14647039 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14647039 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:14647039 | pubmed:issn | 0022-2143 | lld:pubmed |
| pubmed-article:14647039 | pubmed:author | pubmed-author:WestermarkPer... | lld:pubmed |
| pubmed-article:14647039 | pubmed:author | pubmed-author:EulitzManfred... | lld:pubmed |
| pubmed-article:14647039 | pubmed:author | pubmed-author:SlettenKnutK | lld:pubmed |
| pubmed-article:14647039 | pubmed:author | pubmed-author:MurphyCharles... | lld:pubmed |
| pubmed-article:14647039 | pubmed:author | pubmed-author:SolomonAlanA | lld:pubmed |
| pubmed-article:14647039 | pubmed:author | pubmed-author:DonnellRobert... | lld:pubmed |
| pubmed-article:14647039 | pubmed:author | pubmed-author:WestermarkGun... | lld:pubmed |
| pubmed-article:14647039 | pubmed:author | pubmed-author:WeissDeborah... | lld:pubmed |
| pubmed-article:14647039 | pubmed:author | pubmed-author:WeaverKristal... | lld:pubmed |
| pubmed-article:14647039 | pubmed:author | pubmed-author:HrncicRudiR | lld:pubmed |
| pubmed-article:14647039 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14647039 | pubmed:volume | 142 | lld:pubmed |
| pubmed-article:14647039 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14647039 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14647039 | pubmed:pagination | 348-55 | lld:pubmed |
| pubmed-article:14647039 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:14647039 | pubmed:meshHeading | pubmed-meshheading:14647039... | lld:pubmed |
| pubmed-article:14647039 | pubmed:meshHeading | pubmed-meshheading:14647039... | lld:pubmed |
| pubmed-article:14647039 | pubmed:meshHeading | pubmed-meshheading:14647039... | lld:pubmed |
| pubmed-article:14647039 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14647039 | pubmed:articleTitle | Calcifying epithelial odontogenic (Pindborg) tumor-associated amyloid consists of a novel human protein. | lld:pubmed |
| pubmed-article:14647039 | pubmed:affiliation | Human Immunology and Cancer Program, Department of Medicine, University of Tennessee Graduate School of Medicine, Knoxville 37920, USA. asolomon@mc.utmck.edu | lld:pubmed |
| pubmed-article:14647039 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14647039 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:14647039 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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