The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Adiponutrin Functions as a Nutritionally Regulated Lysophosphatidic Acid Acyltransferase
Open accessAbstract
SUMMARY Numerous studies in humans link a nonsynonymous genetic polymorphism (I148M) in adiponutrin (ADPN) to various forms of fatty liver disease and liver cirrhosis. Despite its high clinical relevance, the molecular function of ADPN and the mechanism by which I148M variant affects hepatic metabolism are unclear. Here we show that ADPN promotes cellular lipid synthesis by converting lysophosphatidic acid (LPA) into phosphatidic acid. The ADPN-catalyzed LPA acyltransferase (LPAAT) reaction is specific for LPA and long-chain acyl-CoAs. Wild-type mice receiving a high-sucrose diet exhibit substantial upregulation of Adpn in the liver and a concomitant increase in LPAAT activity. In Adpn-deficient mice, this diet-induced increase in hepatic LPAAT activity is reduced. Notably, the I148M variant of human ADPN exhibits increased LPAAT activity leading to increased cellular lipid accumulation. This gain of function provides a plausible biochemical mechanism for the development of liver steatosis in subjects carrying the I148M variant.
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A RAPID METHOD OF TOTAL LIPID EXTRACTION AND PURIFICATION
Bligh, E. G., & Dyer, W. J. (1959) · Canadian Journal of Biochemistry and Physiology · doi:10.1139/o59-099 · Cited by 54,751
Nonalcoholic Fatty Liver Disease
Marchesini, G., Brizi, M., Bianchi, G., Tomassetti, S., Bugianesi, E., Lenzi, M., McCullough, A. J., Natale, S., Forlani, G., & Melchionda, N. (2001) · Diabetes · doi:10.2337/diabetes.50.8.1844 · Cited by 2,581
Thematic review series: Glycerolipids. DGAT enzymes and triacylglycerol biosynthesis
Yen, C.-L. E., Stone, S. J., Koliwad, S., Harris, C., & Farese, R. V. (2008) · Journal of Lipid Research · doi:10.1194/jlr.r800018-jlr200 · Cited by 1,105
Signaling functions of phosphatidic acid
WANG, X., DEVAIAH, S., ZHANG, W., & WELTI, R. (2006) · Progress in Lipid Research · doi:10.1016/j.plipres.2006.01.005 · Cited by 757
Stone, S. J., Levin, M. C., Zhou, P., Han, J., Walther, T. C., & Farese, R. V. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m805768200 · Cited by 390
A feed-forward loop amplifies nutritional regulation of PNPLA3
Huang, Y., He, S., Li, J. Z., Seo, Y.-K., Osborne, T. F., Cohen, J. C., & Hobbs, H. H. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003585107 · Cited by 386 · cited 5×
“…Obregon, 2009; Kershaw et al., 2006; Moldes et al., 2006), and pharmacological factors (e.g., troglitazone, lipoic acid, liver X receptor [LXR] agonists) (Huang et al., 2010; Huong and Ide, 2008; Polson and Thompson, 2003a) regulateADPN andATGL expression, but in most cases in opposite directions.”
InfluentialHoekstra, M., Li, Z., Kruijt, J. K., Eck, M. V., Berkel, T. J. C. V., & Kuiper, J. (2010) · Journal of Hepatology · doi:10.1016/j.jhep.2009.11.004 · Cited by 108
Cited by
Mechanisms and disease consequences of nonalcoholic fatty liver disease
Loomba, R., Friedman, S. L., & Shulman, G. I. (2021) · Cell · doi:10.1016/j.cell.2021.04.015 · Cited by 2,002
Non-alcoholic fatty liver disease as a cause and a consequence of metabolic syndrome
Yki-Järvinen, H. (2014) · The Lancet Diabetes & Endocrinology · doi:10.1016/s2213-8587(14)70032-4 · Cited by 1,259
Genetics and epigenetics of NAFLD and NASH: Clinical impact
Eslam, M., Valenti, L., & Romeo, S. (2018) · Journal of Hepatology · doi:10.1016/j.jhep.2017.09.003 · Cited by 971
Nonalcoholic fatty liver disease as a nexus of metabolic and hepatic diseases
Samuel, V. T., & Shulman, G. I. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2017.08.002 · Cited by 745
“PNPLA3 has dual functions as a triacylglycerol hydrolase and as an acylglycerol transacylase (Kumari et al., 2012), but the mechanism by which this polymorphism—which attenuates the hydrolase activity (Pingitore et al., 2014)—increases liver fat is still unclear.”
Luukkonen, P. K., Zhou, Y., Sädevirta, S., Leivonen, M., Arola, J., Orešič, M., Hyötyläinen, T., & Yki-Järvinen, H. (2016) · Journal of Hepatology · doi:10.1016/j.jhep.2016.01.002 · Cited by 461
Metadata
- Authors
- Kumari, M., Schoiswohl, G., Chitraju, C., Paar, M., Cornaciu, I., Rangrez, A. Y., Wongsiriroj, N., Nagy, H. M., Ivanova, P. T., Scott, S. A., Knittelfelder, O., Rechberger, G. N., Birner-Gruenberger, R., Eder, S., Brown, H. A., Haemmerle, G., Oberer, M., Lass, A., Kershaw, E. E., Zimmermann, R., & Zechner, R.
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2012-05
- Volume
- 15
- Issue
- 5
- Pages
- 691-702
- ISSN
- 1550-4131 (ISSN-L)
- OpenAlex
- W2093976705
- Cited by
- 316
- References
- 7
- FWCI
- 13.38
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Kumari, M., Schoiswohl, G., Chitraju, C., Paar, M., Cornaciu, I., Rangrez, A. Y., Wongsiriroj, N., Nagy, H. M., Ivanova, P. T., Scott, S. A., Knittelfelder, O., Rechberger, G. N., Birner-Gruenberger, R., Eder, S., Brown, H. A., Haemmerle, G., Oberer, M., Lass, A., Kershaw, E. E., . . . Zechner, R. (2012). Adiponutrin Functions as a Nutritionally Regulated Lysophosphatidic Acid Acyltransferase. Cell Metabolism. https://doi.org/10.1016/j.cmet.2012.04.008
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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