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http://purl.uniprot.org/citations/27804051http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27804051http://www.w3.org/2000/01/rdf-schema#comment"Human amylin (hA1-37) is a polypeptide hormone secreted in conjunction with insulin from the pancreatic β-cells involved in the pathogenesis of type 2 diabetes mellitus (T2DM). The shorter fragment hA17-29 than full-length peptide is capable to form amyloids "in vitro". Here, we monitored the time course of hA17-29 β-amyloid fibril and oligomer formation [without and with copper(II)], cellular toxicity of different amyloid aggregates, and involvement of specific receptors (receptor for advanced glycation end-products, RAGE; low-affinity nerve growth factor receptor, p75-NGFR) in aggregate toxicity. Fibril and oligomer formation of hA17-29 incubated at 37 °C for 0, 48, and 120 h, without or with copper(II), were measured by the thioflavin T fluorescence assay and ELISA, respectively. Toxicity of hA17-29 aggregates and effects of anti-RAGE and anti-p75-NGFR antibodies were evaluated on neuroblastoma SH-SY5Y viability. Fluorescence assay of hA17-29 indicates an initial slow rate of soluble fibril formation (48 h), followed by a slower rate of insoluble aggregate formation (120 h). The highest quantity of oligomers was recorded when hA17-29 was pre-aggregated for 48 h in the presence of copper(II) showing also the maximal cell toxicity (-44% of cell viability, p < 0.01 compared to controls). Anti-RAGE or anti-p75-NGFR antibodies almost abolished cell toxicity of hA17-29 aggregates. These results indicate that copper(II) influences the aggregation process and hA17-29 toxicities are especially attributable to oligomeric aggregates. hA17-29 aggregate toxicity seems to be mediated by RAGE and p75-NGFR receptors which might be potential targets for new drugs in T2DM treatment."xsd:string
http://purl.uniprot.org/citations/27804051http://purl.org/dc/terms/identifier"doi:10.1007/s11010-016-2864-1"xsd:string
http://purl.uniprot.org/citations/27804051http://purl.uniprot.org/core/author"Lazzarino G."xsd:string
http://purl.uniprot.org/citations/27804051http://purl.uniprot.org/core/author"Nicoletti V.G."xsd:string
http://purl.uniprot.org/citations/27804051http://purl.uniprot.org/core/author"Caruso G."xsd:string
http://purl.uniprot.org/citations/27804051http://purl.uniprot.org/core/author"Lunte S.M."xsd:string
http://purl.uniprot.org/citations/27804051http://purl.uniprot.org/core/author"Distefano D.A."xsd:string
http://purl.uniprot.org/citations/27804051http://purl.uniprot.org/core/author"Fresta C.G."xsd:string
http://purl.uniprot.org/citations/27804051http://purl.uniprot.org/core/author"Parlascino P."xsd:string
http://purl.uniprot.org/citations/27804051http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/27804051http://purl.uniprot.org/core/name"Mol Cell Biochem"xsd:string
http://purl.uniprot.org/citations/27804051http://purl.uniprot.org/core/pages"85-93"xsd:string
http://purl.uniprot.org/citations/27804051http://purl.uniprot.org/core/title"Receptor-mediated toxicity of human amylin fragment aggregated by short- and long-term incubations with copper ions."xsd:string
http://purl.uniprot.org/citations/27804051http://purl.uniprot.org/core/volume"425"xsd:string
http://purl.uniprot.org/citations/27804051http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/27804051
http://purl.uniprot.org/citations/27804051http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/27804051
http://purl.uniprot.org/uniprot/#_E9LVY5-mappedCitation-27804051http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27804051
http://purl.uniprot.org/uniprot/#_E9LVY6-mappedCitation-27804051http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27804051
http://purl.uniprot.org/uniprot/#_E9LVY7-mappedCitation-27804051http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27804051
http://purl.uniprot.org/uniprot/#_F1ABM9-mappedCitation-27804051http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27804051
http://purl.uniprot.org/uniprot/#_F1ABN0-mappedCitation-27804051http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27804051
http://purl.uniprot.org/uniprot/#_F1ABN1-mappedCitation-27804051http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27804051
http://purl.uniprot.org/uniprot/#_Q15109-mappedCitation-27804051http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27804051
http://purl.uniprot.org/uniprot/#_A0A1U9X782-mappedCitation-27804051http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27804051