<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Del Castillo-Izquierdo A</submitter><funding>Instituto de Salud Carlos III</funding><funding>Girona Biomedical Research Institute</funding><funding>Marie Skłodowska-Curie Innovative Training Network</funding><funding>Fundació Marató de TV3</funding><funding>European Regional Development Fund</funding><pagination>2177</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9686780</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>11(11)</volume><pubmed_abstract>Dipeptidyl peptidase 9 (DPP9) is a member of the dipeptidyl peptidase IV family. Inhibition of DPP9 has recently been shown to activate the nucleotide-binding domain leucine-rich repeat 1 (NLRP1) inflammasome. NLRP1 is known to bind nucleic acids with high affinity and directly interact with double stranded RNA, which plays a key role in viral replication. &lt;i>DPP9&lt;/i> has also recently emerged as a key gene related to lung-inflammation in critical SARS-CoV-2 infection. Importantly, DPP9 activity is strongly dependent on the oxidative status. Here, we explored the potential role of &lt;i>DPP9&lt;/i> in the gastrointestinal tract. We performed transcriptomics analyses of colon (microarray, &lt;i>n&lt;/i> = 37) and jejunal (RNA sequencing, &lt;i>n&lt;/i> = 31) biopsies from two independent cohorts as well as p</pubmed_abstract><journal>Antioxidants (Basel, Switzerland)</journal><pubmed_title>DPP9 as a Potential Novel Mediator in Gastrointestinal Virus Infection.</pubmed_title><pmcid>PMC9686780</pmcid><funding_grant_id>201612-31</funding_grant_id><funding_grant_id>PI20/01090</funding_grant_id><funding_grant_id>CM19/00190</funding_grant_id><funding_grant_id>859890</funding_grant_id><funding_grant_id>CP18/00009</funding_grant_id><pubmed_authors>Mayneris-Perxachs J</pubmed_authors><pubmed_authors>Latorre J</pubmed_authors><pubmed_authors>Lefebvre P</pubmed_authors><pubmed_authors>Puig J</pubmed_authors><pubmed_authors>Ballanti M</pubmed_authors><pubmed_authors>Pamplona R</pubmed_authors><pubmed_authors>Ramos R</pubmed_authors><pubmed_authors>Portero-Otin M</pubmed_authors><pubmed_authors>Arnoriaga-Rodriguez M</pubmed_authors><pubmed_authors>Moreno-Navarrete JM</pubmed_authors><pubmed_authors>Staels B</pubmed_authors><pubmed_authors>Mingrone G</pubmed_authors><pubmed_authors>Alessandro Paoluzi O</pubmed_authors><pubmed_authors>Federici M</pubmed_authors><pubmed_authors>Fernandez-Real JM</pubmed_authors><pubmed_authors>Garre-Olmo J</pubmed_authors><pubmed_authors>Del Castillo-Izquierdo A</pubmed_authors><pubmed_authors>Jove M</pubmed_authors><pubmed_authors>Monteleone G</pubmed_authors><pubmed_authors>Sol J</pubmed_authors></additional><is_claimable>false</is_claimable><name>DPP9 as a Potential Novel Mediator in Gastrointestinal Virus Infection.</name><description>Dipeptidyl peptidase 9 (DPP9) is a member of the dipeptidyl peptidase IV family. Inhibition of DPP9 has recently been shown to activate the nucleotide-binding domain leucine-rich repeat 1 (NLRP1) inflammasome. NLRP1 is known to bind nucleic acids with high affinity and directly interact with double stranded RNA, which plays a key role in viral replication. &lt;i>DPP9&lt;/i> has also recently emerged as a key gene related to lung-inflammation in critical SARS-CoV-2 infection. Importantly, DPP9 activity is strongly dependent on the oxidative status. Here, we explored the potential role of &lt;i>DPP9&lt;/i> in the gastrointestinal tract. We performed transcriptomics analyses of colon (microarray, &lt;i>n&lt;/i> = 37) and jejunal (RNA sequencing, &lt;i>n&lt;/i> = 31) biopsies from two independent cohorts as well as p</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Nov</publication><modification>2026-04-08T11:01:50.224Z</modification><creation>2024-11-20T11:17:16.938Z</creation></dates><accession>S-EPMC9686780</accession><cross_references><pubmed>36358551</pubmed><doi>10.3390/antiox11112177</doi></cross_references></HashMap>