<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>5</volume><submitter>Sklirou AD</submitter><funding>EU COST</funding><pubmed_abstract>Despite the fact that several natural products (e.g. crude extracts or purified compounds) have been found to activate cell antioxidant responses and/or delay cellular senescence the effect(s) of small peptides on cell viability and/or modulation of protective mechanisms (e.g. the proteostasis network) remain largely elusive. We have thus studied a hexapeptide (Hexapeptide-11) of structure Phe-Val-Ala-Pro-Phe-Pro (FVAPFP) originally isolated from yeast extracts and later synthesized by solid state synthesis to high purity. We show herein that Hexapeptide-11 exhibits no significant toxicity in normal human diploid lung or skin fibroblasts. Exposure of fibroblasts to Hexapeptide-11 promoted dose and time-dependent activation of proteasome, autophagy, chaperones and antioxidant responses rela</pubmed_abstract><journal>Redox biology</journal><pagination>205-215</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4434199</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Hexapeptide-11 is a novel modulator of the proteostasis network in human diploid fibroblasts.</pubmed_title><pmcid>PMC4434199</pmcid><pubmed_authors>Dominguez M</pubmed_authors><pubmed_authors>Sklirou AD</pubmed_authors><pubmed_authors>Skaltsounis AL</pubmed_authors><pubmed_authors>Papassideri I</pubmed_authors><pubmed_authors>Trougakos IP</pubmed_authors><pubmed_authors>Ralli M</pubmed_authors></additional><is_claimable>false</is_claimable><name>Hexapeptide-11 is a novel modulator of the proteostasis network in human diploid fibroblasts.</name><description>Despite the fact that several natural products (e.g. crude extracts or purified compounds) have been found to activate cell antioxidant responses and/or delay cellular senescence the effect(s) of small peptides on cell viability and/or modulation of protective mechanisms (e.g. the proteostasis network) remain largely elusive. We have thus studied a hexapeptide (Hexapeptide-11) of structure Phe-Val-Ala-Pro-Phe-Pro (FVAPFP) originally isolated from yeast extracts and later synthesized by solid state synthesis to high purity. We show herein that Hexapeptide-11 exhibits no significant toxicity in normal human diploid lung or skin fibroblasts. Exposure of fibroblasts to Hexapeptide-11 promoted dose and time-dependent activation of proteasome, autophagy, chaperones and antioxidant responses rela</description><dates><release>2015-01-01T00:00:00Z</release><publication>2015 Aug</publication><modification>2025-06-01T01:01:44.87Z</modification><creation>2025-06-01T01:01:44.87Z</creation></dates><accession>S-EPMC4434199</accession><cross_references><pubmed>25974626</pubmed><doi>10.1016/j.redox.2015.04.010</doi></cross_references></HashMap>