Evidence map›Paper›PMID 30012886›Full record

ArticleThe Journal of biological chemistry2018

Functional proteasome complex is required for turnover of islet amyloid polypeptide in pancreatic β-cells.

Diti Chatterjee Bhowmick, Aleksandar Jeremic

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

13 citing papers in PubMed, 27 citations in OpenAlex.

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  4. Proteotoxic stress and the ubiquitin proteasome system.Seminars in cell & developmental biology · 2024
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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

2 authors at 1 institution in 1 country.

Diti Chatterjee BhowmickFrom the Departments of Biological Sciences and Biomedical Sciences, George Washington University, Washington, D. C. 20052.
Aleksandar JeremicFrom the Departments of Biological Sciences and Biomedical Sciences, George Washington University, Washington, D. C. 20052 jerema@gwu.edu.
George Washington University · US

Funding

Molecular Mechanisims of Amylin Trafficking and Toxicity in Human Pancreatic IsleR01DK091845 · NIDDK · GEORGE WASHINGTON UNIVERSITY · PI JEREMIC, ALEKSANDAR MILORAD · 2013 to 2017
$1.4M
NIDDK NIH HHS R01 DK091845
6 · The paper itself

Abstract

Human islet amyloid polypeptide (hIAPP) is the principal constituent of amyloid deposits and toxic oligomers in the pancreatic islets. Together with hyperglycemia, hIAPP-derived oligomers and aggregates are important culprits in type 2 diabetes mellitus (T2DM). Here, we explored the role of the cell's main proteolytic complex, the proteasome, in hIAPP turnover in normal and stressed β-cells evoked by chronic hyperglycemia. Moderate inhibition (10-35%) of proteasome activity/function in cultured human islets by the proteasome inhibitor lactacystin enhanced intracellular accumulation of hIAPP. Unexpectedly, prolonged (>1 h) and marked (>50%) impairment of proteasome activity/function had a strong inhibitory effect on hIAPP transcription and secretion from normal and stressed β-cells. This negative compensatory feedback mechanism for controlling IAPP turnover was also observed in the lactacystin-treated rat insulinoma β-cell line (INS 832/13), demonstrating the presence of an evolutionarily conserved mechanism for IAPP production. In line with these

Indexed as

AcetylcysteineAnimalsCell Line, TumorDiabetes Mellitus, Type 2Down-RegulationHepatocyte Nuclear Factor 3-betaHumansInsulinomaInsulin-Secreting CellsIslet Amyloid PolypeptideLeupeptinsMiceOligopeptidesPromoter Regions, GeneticProteasome Endopeptidase ComplexProteasome InhibitorsAcetylcysteinebenzyloxycarbonylleucyl-leucyl-leucine aldehydeepoxomicinFOXA2 protein, humanHepatocyte Nuclear Factor 3-betaIslet Amyloid PolypeptidelactacystinLeupeptinsOligopeptidesProteasome Endopeptidase ComplexProteasome InhibitorsamyloidFoxA2hyperglycemiainsulinIslet amyloid polypeptideproteasomesecretiontranscriptiontype 2 diabetes

Identifiers

PMID30012886
PMCPMC6139561
OpenAlexW2884213510

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.