<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Caruso G</submitter><funding>American Heart Association</funding><funding>National Institutes of Health</funding><funding>Neuropsychopharmacology Research Program 2017</funding><funding>NIGMS NIH HHS</funding><funding>National Science Foundation</funding><pagination>E3659</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6274958</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>19(11)</volume><pubmed_abstract>Human amylin is a 37-residue peptide hormone (hA1-37) secreted by β-cells of the pancreas and, along with insulin, is directly associated with type 2 diabetes mellitus (T2DM). Amyloid deposits within the islets of the pancreas represent a hallmark of T2DM. Additionally, amylin aggregates have been found in blood vessels and/or brain of patients with Alzheimer's disease, alone or co-deposited with β-amyloid. The purpose of this study was to investigate the neuroprotective potential of human amylin in the context of endothelial-neuronal "cross-talk". We initially performed dose-response experiments to examine cellular toxicity (quantified by the [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide] MTT assay) of different hA17⁻29 concentrations in endothelial cells (RBE4). In the cu</pubmed_abstract><journal>International journal of molecular sciences</journal><pubmed_title>Sub-Toxic Human Amylin Fragment Concentrations Promote the Survival and Proliferation of SH-SY5Y Cells via the Release of VEGF and HspB5 from Endothelial RBE4 Cells.</pubmed_title><pmcid>PMC6274958</pmcid><funding_grant_id>P20 GM103638</funding_grant_id><funding_grant_id>CHE-1411993</funding_grant_id><funding_grant_id>RC-06-05</funding_grant_id><funding_grant_id>P20GM103638</funding_grant_id><funding_grant_id>NFP0075515</funding_grant_id><pubmed_authors>Caraci F</pubmed_authors><pubmed_authors>Fresta CG</pubmed_authors><pubmed_authors>Distefano DA</pubmed_authors><pubmed_authors>Parlascino P</pubmed_authors><pubmed_authors>Lunte SM</pubmed_authors><pubmed_authors>Caruso G</pubmed_authors><pubmed_authors>Lazzarino G</pubmed_authors></additional><is_claimable>false</is_claimable><name>Sub-Toxic Human Amylin Fragment Concentrations Promote the Survival and Proliferation of SH-SY5Y Cells via the Release of VEGF and HspB5 from Endothelial RBE4 Cells.</name><description>Human amylin is a 37-residue peptide hormone (hA1-37) secreted by β-cells of the pancreas and, along with insulin, is directly associated with type 2 diabetes mellitus (T2DM). Amyloid deposits within the islets of the pancreas represent a hallmark of T2DM. Additionally, amylin aggregates have been found in blood vessels and/or brain of patients with Alzheimer's disease, alone or co-deposited with β-amyloid. The purpose of this study was to investigate the neuroprotective potential of human amylin in the context of endothelial-neuronal "cross-talk". We initially performed dose-response experiments to examine cellular toxicity (quantified by the [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide] MTT assay) of different hA17⁻29 concentrations in endothelial cells (RBE4). In the cu</description><dates><release>2018-01-01T00:00:00Z</release><publication>2018 Nov</publication><modification>2026-07-16T17:25:05.376Z</modification><creation>2019-03-27T00:11:38Z</creation></dates><accession>S-EPMC6274958</accession><cross_references><pubmed>30463298</pubmed><doi>10.3390/ijms19113659</doi></cross_references></HashMap>