Evidence map›Paper›PMID 27804051›Full record

ArticleMolecular and cellular biochemistry2017

Receptor-mediated toxicity of human amylin fragment aggregated by short- and long-term incubations with copper ions.

Giuseppe Caruso, Donatella A Distefano, Paolo Parlascino, Claudia G Fresta, Giuseppe Lazzarino, Susan M Lunte, Vincenzo G Nicoletti

Abstract read
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In one paragraph

Article in Molecular and cellular biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.5field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

31 citing papers in PubMed, 41 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Giuseppe CarusoDepartment of Chemistry and Pharmaceutical Chemistry, University of Kansas, Lawrence, KS, USA.
Donatella A DistefanoDivision of Medical Biochemistry, Department of Biomedical and Biotechnological Sciences, University of Catania, Catania, Italy.
Paolo ParlascinoDivision of Medical Biochemistry, Department of Biomedical and Biotechnological Sciences, University of Catania, Catania, Italy.
Claudia G FrestaDepartment of Chemistry and Pharmaceutical Chemistry, University of Kansas, Lawrence, KS, USA.
Giuseppe LazzarinoDivision of Medical Biochemistry, Department of Biomedical and Biotechnological Sciences, University of Catania, Catania, Italy. lazzarig@unict.it.ORCID http://orcid.org/0000-0002-5917-7279
Susan M LunteDepartment of Chemistry and Pharmaceutical Chemistry, University of Kansas, Lawrence, KS, USA.
Vincenzo G NicolettiDivision of Medical Biochemistry, Department of Biomedical and Biotechnological Sciences, University of Catania, Catania, Italy.
University of Catania · ITUniversity of Kansas · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

AmyloidAnimalsCell LineCopperHumansIslet Amyloid PolypeptideNerve Tissue ProteinsRatsReceptor for Advanced Glycation End ProductsReceptors, Nerve Growth FactorAGER protein, humanAmyloidCopperIslet Amyloid PolypeptideNerve Tissue ProteinsNGFR protein, humanReceptor for Advanced Glycation End ProductsReceptors, Nerve Growth FactorAggregationAmylinCell viability Copper Receptor-mediated cell toxicityOligomers

Identifiers

PMID27804051
OpenAlexW2546921692

What OpenQuestion holds

Textmetadata
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.