ArticleJournal of lipid research2022
KIAA1363 affects retinyl ester turnover in cultured murine and human hepatic stellate cells.
Article in Journal of lipid research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- Decreased Endothelial Cell Retinoic Acid Signaling Accelerates Progression of Single Ventricle Pulmonary Vascular Malformations.JACC. Basic to translational science · 2026Article
- The application of neutrophil extracellular traps to thrombus age Estimation in rat deep vein thrombosis model.Forensic science, medicine, and pathology · 2025Article
- Reduced Esterification Rather Than Increased Hydrolysis Is Causative for Loss of Hepatic Retinoids Upon CClLiver international : official journal of the International Association for the Study of the Liver · 2025Article
- Immunometabolic effects ofImmunometabolism (Cobham, Surrey) · 2024Review
- Adipocyte HSL is required for maintaining circulating vitamin A and RBP4 levels during fasting.EMBO reports · 2024Article
- Forward genetic screening using fundus spot scale identifies an essential role for Lipe in murine retinal homeostasis.Communications biology · 2023Article
- KIAA1363-A Multifunctional Enzyme in Xenobiotic Detoxification and Lipid Ester Hydrolysis.Metabolites · 2022Review
- Mechanisms of Feedback Regulation of Vitamin A Metabolism.Nutrients · 2022Review
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
Large quantities of vitamin A are stored as retinyl esters (REs) in specialized liver cells, the hepatic stellate cells (HSCs). To date, the enzymes controlling RE degradation in HSCs are poorly understood. In this study, we identified KIAA1363 (also annotated as arylacetamide deacetylase 1 or neutral cholesterol ester hydrolase 1) as a novel RE hydrolase. We show that KIAA1363 is expressed in the liver, mainly in HSCs, and exhibits RE hydrolase activity at neutral pH. Accordingly, addition of the KIAA1363-specific inhibitor JW480 largely reduced RE hydrolase activity in lysates of cultured murine and human HSCs. Furthermore, cell fractionation experiments and confocal microscopy studies showed that KIAA1363 localizes to the endoplasmic reticulum. We demonstrate that overexpression of KIAA1363 in cells led to lower cellular RE content after a retinol loading period. Conversely, pharmacological inhibition or shRNA-mediated silencing of KIAA1363 expression in cultured murine and human HSCs attenuated RE degradation. Together, our data suggest that KIAA1363 affects vitamin A metabolism of HSCs by hydrolyzing REs at the endoplasmic reticulum, thereby counteracting retinol esterification and RE storage in lipid droplets.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.