<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Hahn KR</submitter><funding>Ministry of Science, ICT and Future Planning</funding><pagination>20659</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9712579</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>12(1)</volume><pubmed_abstract>Carboxyl terminus of Hsc70-interacting protein (CHIP) is highly conserved and is linked to the connection between molecular chaperones and proteasomes to degrade chaperone-bound proteins. In this study, we synthesized the transactivator of transcription (Tat)-CHIP fusion protein for effective delivery into the brain and examined the effects of CHIP against oxidative stress in HT22 cells induced by hydrogen peroxide (H&lt;sub>2&lt;/sub>O&lt;sub>2&lt;/sub>) treatment and ischemic damage in gerbils by 5 min of occlusion of both common carotid arteries, to elucidate the possibility of using Tat-CHIP as a therapeutic agent against ischemic damage. Tat-CHIP was effectively delivered to HT22 hippocampal cells in a concentration- and time-dependent manner, and protein degradation was confirmed in HT22 cells. </pubmed_abstract><journal>Scientific reports</journal><pubmed_title>CHIP ameliorates neuronal damage in H&lt;sub>2&lt;/sub>O&lt;sub>2&lt;/sub>-induced oxidative stress in HT22 cells and gerbil ischemia.</pubmed_title><pmcid>PMC9712579</pmcid><funding_grant_id>NRF-2021R1F1A1048079</funding_grant_id><funding_grant_id>NRF-2022R1A2B5B01002280</funding_grant_id><pubmed_authors>Kim DW</pubmed_authors><pubmed_authors>Kwon HJ</pubmed_authors><pubmed_authors>Yoon YS</pubmed_authors><pubmed_authors>Hahn KR</pubmed_authors><pubmed_authors>Hwang IK</pubmed_authors></additional><is_claimable>false</is_claimable><name>CHIP ameliorates neuronal damage in H&lt;sub>2&lt;/sub>O&lt;sub>2&lt;/sub>-induced oxidative stress in HT22 cells and gerbil ischemia.</name><description>Carboxyl terminus of Hsc70-interacting protein (CHIP) is highly conserved and is linked to the connection between molecular chaperones and proteasomes to degrade chaperone-bound proteins. In this study, we synthesized the transactivator of transcription (Tat)-CHIP fusion protein for effective delivery into the brain and examined the effects of CHIP against oxidative stress in HT22 cells induced by hydrogen peroxide (H&lt;sub>2&lt;/sub>O&lt;sub>2&lt;/sub>) treatment and ischemic damage in gerbils by 5 min of occlusion of both common carotid arteries, to elucidate the possibility of using Tat-CHIP as a therapeutic agent against ischemic damage. Tat-CHIP was effectively delivered to HT22 hippocampal cells in a concentration- and time-dependent manner, and protein degradation was confirmed in HT22 cells. </description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Nov</publication><modification>2026-05-27T11:53:52.799Z</modification><creation>2024-11-21T00:16:00.677Z</creation></dates><accession>S-EPMC9712579</accession><cross_references><pubmed>36450819</pubmed><doi>10.1038/s41598-022-22766-0</doi></cross_references></HashMap>