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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Schreiber, Renate Taschler, Ulrike Wolinski, Heimo Seper, Andrea Tamegger, Stefanie N. Graf, Maria Kohlwein, Sepp D. Haemmerle, Guenter Zimmermann, Robert Zechner, Rudolf Lass, Achim |
| Description | Country affiliation: Austria Author Affiliation: Schreiber R ( Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria.) |
| Abstract | Excess dietary vitamin A is esterified with fatty acids and stored in the form of retinyl ester (RE) predominantly in the liver. According to the requirements of the body, liver RE stores are hydrolyzed and retinol is delivered to peripheral tissues. The controlled mobilization of retinol ensures a constant supply of the body with the vitamin. Currently, the enzymes catalyzing liver RE hydrolysis are unknown. In this study, we identified mouse esterase 22 (Es22) as potent RE hydrolase highly expressed in the liver, particularly in hepatocytes. The enzyme is located exclusively at the endoplasmic reticulum (ER), implying that it is not involved in the mobilization of RE present in cytosolic lipid droplets. Nevertheless, cell culture experiments revealed that overexpression of Es22 attenuated the formation of cellular RE stores, presumably by counteracting retinol esterification at the ER. Es22 was previously shown to form a complex with beta-glucuronidase (Gus). Our studies revealed that Gus colocalizes with Es22 at the ER but does not affect its RE hydrolase activity. Interestingly, however, Gus was capable of hydrolyzing the naturally occurring vitamin A metabolite retinoyl beta-glucuronide. In conclusion, our observations implicate that both Es22 and Gus play a role in liver retinoid metabolism. |
| File Format | HTM / HTML |
| ISSN | 00222275 |
| e-ISSN | 15397262 |
| DOI | 10.1194/jlr.M000950 |
| Journal | The Journal of Lipid Research |
| Issue Number | 12 |
| Volume Number | 50 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology |
| Publisher Date | 2009-12-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Discipline Biochemistry Carboxylic Ester Hydrolases Metabolism Glucuronidase Liver Retinoids Animals Cos Cells Cercopithecus Aethiops Hydrolysis Enzymology Mice Mice, Inbred C57bl Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Endocrinology |
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