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http://purl.uniprot.org/citations/20536400http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20536400http://www.w3.org/2000/01/rdf-schema#comment"AA amyloidosis invariably has been associated with fibrillar deposits of the acute phase high-density lipoprotein serum amyloid A isotypes SAA1 and SAA2. We now report the first case in a patient with no antecedent history of a chronic inflammatory or neoplastic process whose pathologic renal deposits were comprised of a mutated form of the constitutively expressed serum amyloid A4 (SAA4) protein. Analyses by tandem mass spectrometry of amyloid extracted from kidney biopsies revealed a component identical in sequence to the N-terminal portion of SAA4, except for the substitution of glycine for tryptophan at position 22 (W22G). Sequencing of genomic DNA using SAA4-specific primers showed a TGG to GGG transversion in codon 22 that accounted for the observed modification. Confirmation of the SAA4 nature of the amyloid was obtained immunohistochemically. Notably, only wild-type SAA4 was detected by mass spectrometry in the patient's serum and its concentration was within normal limits. Given the substitution of an amino acid lacking a side chain for a bulky residue, we posit that the W22G alteration would profoundly affect SAA4 stability, rendering it amyloidogenic. Our studies provide the first evidence for a novel type of AA amyloidosis in which the fibrils were formed from a mutated SAA4 protein."xsd:string
http://purl.uniprot.org/citations/20536400http://purl.org/dc/terms/identifier"doi:10.1080/13506120902879905"xsd:string
http://purl.uniprot.org/citations/20536400http://purl.uniprot.org/core/author"Wang S."xsd:string
http://purl.uniprot.org/citations/20536400http://purl.uniprot.org/core/author"Murphy C.L."xsd:string
http://purl.uniprot.org/citations/20536400http://purl.uniprot.org/core/author"Solomon A."xsd:string
http://purl.uniprot.org/citations/20536400http://purl.uniprot.org/core/author"Weiss D.T."xsd:string
http://purl.uniprot.org/citations/20536400http://purl.uniprot.org/core/author"Kestler D.P."xsd:string
http://purl.uniprot.org/citations/20536400http://purl.uniprot.org/core/author"Stevens F.A."xsd:string
http://purl.uniprot.org/citations/20536400http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/20536400http://purl.uniprot.org/core/name"Amyloid"xsd:string
http://purl.uniprot.org/citations/20536400http://purl.uniprot.org/core/pages"84-88"xsd:string
http://purl.uniprot.org/citations/20536400http://purl.uniprot.org/core/title"AA amyloidosis associated with a mutated serum amyloid A4 protein."xsd:string
http://purl.uniprot.org/citations/20536400http://purl.uniprot.org/core/volume"16"xsd:string
http://purl.uniprot.org/citations/20536400http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20536400
http://purl.uniprot.org/citations/20536400http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20536400
http://purl.uniprot.org/uniprot/#_B2R5G8-mappedCitation-20536400http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20536400
http://purl.uniprot.org/uniprot/#_P35542-mappedCitation-20536400http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20536400
http://purl.uniprot.org/uniprot/P35542http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/20536400
http://purl.uniprot.org/uniprot/B2R5G8http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/20536400