<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Tse CM</submitter><funding>Cystic Fibrosis Foundation grant</funding><funding>nih ro1</funding><funding>National Institutes of Health grants</funding><pagination>8273</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10179158</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>24(9)</volume><pubmed_abstract>Cholesterol-rich membrane domains, also called lipid rafts (LRs), are specialized membrane domains that provide a platform for intracellular signal transduction. Membrane proteins often cluster in LRs that further aggregate into larger platform-like structures that are enriched in ceramides and are called ceramide-rich platforms (CRPs). The role of CRPs in the regulation of intestinal epithelial functions remains unknown. Down-regulated in adenoma (DRA) is an intestinal Cl&lt;sup>-&lt;/sup>/HCO&lt;sub>3&lt;/sub>&lt;sup>-&lt;/sup> antiporter that is enriched in LRs. However, little is known regarding the mechanisms involved in the regulation of DRA activity. The air-liquid interface (ALI) was created by removing apical media for a specified number of days; from 12-14 days post-confluency, Caco-2/BBe cells or</pubmed_abstract><journal>International journal of molecular sciences</journal><pubmed_title>The Air-Liquid Interface Reorganizes Membrane Lipids and Enhances the Recruitment of Slc26a3 to Lipid-Rich Domains in Human Colonoid Monolayers.</pubmed_title><pmcid>PMC10179158</pmcid><funding_grant_id>UO1-DK-10316</funding_grant_id><funding_grant_id>CF-SINGH20G0</funding_grant_id><funding_grant_id>R01-DK-116352</funding_grant_id><funding_grant_id>P30-DK-89502</funding_grant_id><pubmed_authors>Lin R</pubmed_authors><pubmed_authors>Donowitz M</pubmed_authors><pubmed_authors>Zhang Z</pubmed_authors><pubmed_authors>Tse CM</pubmed_authors><pubmed_authors>Sarker R</pubmed_authors><pubmed_authors>Singh V</pubmed_authors></additional><is_claimable>false</is_claimable><name>The Air-Liquid Interface Reorganizes Membrane Lipids and Enhances the Recruitment of Slc26a3 to Lipid-Rich Domains in Human Colonoid Monolayers.</name><description>Cholesterol-rich membrane domains, also called lipid rafts (LRs), are specialized membrane domains that provide a platform for intracellular signal transduction. Membrane proteins often cluster in LRs that further aggregate into larger platform-like structures that are enriched in ceramides and are called ceramide-rich platforms (CRPs). The role of CRPs in the regulation of intestinal epithelial functions remains unknown. Down-regulated in adenoma (DRA) is an intestinal Cl&lt;sup>-&lt;/sup>/HCO&lt;sub>3&lt;/sub>&lt;sup>-&lt;/sup> antiporter that is enriched in LRs. However, little is known regarding the mechanisms involved in the regulation of DRA activity. The air-liquid interface (ALI) was created by removing apical media for a specified number of days; from 12-14 days post-confluency, Caco-2/BBe cells or</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 May</publication><modification>2025-04-26T01:39:07.792Z</modification><creation>2025-04-06T10:13:29.888Z</creation></dates><accession>S-EPMC10179158</accession><cross_references><pubmed>37175979</pubmed><doi>10.3390/ijms24098273</doi></cross_references></HashMap>