{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Del Castillo-Izquierdo A"],"funding":["Instituto de Salud Carlos III","Girona Biomedical Research Institute","Marie Skłodowska-Curie Innovative Training Network","Fundació Marató de TV3","European Regional Development Fund"],"pagination":["2177"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9686780"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(11)"],"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. <i>DPP9</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 <i>DPP9</i> in the gastrointestinal tract. We performed transcriptomics analyses of colon (microarray, <i>n</i> = 37) and jejunal (RNA sequencing, <i>n</i> = 31) biopsies from two independent cohorts as well as p"],"journal":["Antioxidants (Basel, Switzerland)"],"pubmed_title":["DPP9 as a Potential Novel Mediator in Gastrointestinal Virus Infection."],"pmcid":["PMC9686780"],"funding_grant_id":["201612-31","PI20/01090","CM19/00190","859890","CP18/00009"],"pubmed_authors":["Mayneris-Perxachs J","Latorre J","Lefebvre P","Puig J","Ballanti M","Pamplona R","Ramos R","Portero-Otin M","Arnoriaga-Rodriguez M","Moreno-Navarrete JM","Staels B","Mingrone G","Alessandro Paoluzi O","Federici M","Fernandez-Real JM","Garre-Olmo J","Del Castillo-Izquierdo A","Jove M","Monteleone G","Sol J"],"additional_accession":[]},"is_claimable":false,"name":"DPP9 as a Potential Novel Mediator in Gastrointestinal Virus Infection.","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. <i>DPP9</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 <i>DPP9</i> in the gastrointestinal tract. We performed transcriptomics analyses of colon (microarray, <i>n</i> = 37) and jejunal (RNA sequencing, <i>n</i> = 31) biopsies from two independent cohorts as well as p","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Nov","modification":"2026-04-08T11:01:50.224Z","creation":"2024-11-20T11:17:16.938Z"},"accession":"S-EPMC9686780","cross_references":{"pubmed":["36358551"],"doi":["10.3390/antiox11112177"]}}