T-cadherin is a receptor for hexameric and high-molecular-weight forms of Acrp30/adiponectin
| العنوان: | T-cadherin is a receptor for hexameric and high-molecular-weight forms of Acrp30/adiponectin |
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| المؤلفون: | Harvey F. Lodish, Tsu-Shuen Tsao, Jonathan S. Bogan, Naina Shehzeen Ahmad, Christopher Hug, Jin Wang |
| المصدر: | Proceedings of the National Academy of Sciences. 101:10308-10313 |
| بيانات النشر: | Proceedings of the National Academy of Sciences, 2004. |
| سنة النشر: | 2004 |
| مصطلحات موضوعية: | medicine.medical_specialty, Gene Expression, CHO Cells, Plasma protein binding, Biology, Kidney, Ligands, law.invention, Myoblasts, Magnetics, Mice, chemistry.chemical_compound, law, Cricetinae, Internal medicine, medicine, Animals, Humans, Receptor, Multidisciplinary, Adiponectin, Proteins, nutritional and metabolic diseases, Biological Sciences, Cadherins, Flow Cytometry, Cell biology, AdipoRon, Molecular Weight, T-cadherin, Endocrinology, Adipose Tissue, chemistry, Recombinant DNA, Intercellular Signaling Peptides and Proteins, Adiponectin binding, Signal transduction, hormones, hormone substitutes, and hormone antagonists, Plasmids, Protein Binding, Signal Transduction |
| الوصف: | Acrp30/adiponectin is reduced in the serum of obese and diabetic individuals, and the genetic locus of adiponectin is linked to the metabolic syndrome. Recombinant adiponectin, administered to diet-induced obese mice, induced weight loss and improved insulin sensitivity. In muscle and liver, adiponectin stimulates AMP-activated protein kinase activation and fatty acid oxidation. To expression-clone molecules capable of binding adiponectin, we transduced a C2C12 myoblast cDNA retroviral expression library into Ba/F3 cells and panned infected cells on recombinant adiponectin linked to magnetic beads. We identified T-cadherin as a receptor for the hexameric and high-molecular-weight species of adiponectin but not for the trimeric or globular species. Only eukaryotically expressed adiponectin bound to T-cadherin, implying that posttranslational modifications of adiponectin are critical for binding. An adiponectin mutant lacking a conserved N-terminal cysteine residue required for formation of hexamer and high-molecular-weight species did not bind T-cadherin in coimmunoprecipitation studies. Although lacking known cellular functions, T-cadherin is expressed in endothelial and smooth muscle cells, where it is positioned to interact with adiponectin. Because T-cadherin is a glycosylphosphatidylinositol-anchored extracellular protein, it may act as a coreceptor for an as-yet-unidentified signaling receptor through which adiponectin transmits metabolic signals. |
| تدمد: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.0403382101 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3960f7ae0155e499ad5d33798c8bc936 https://doi.org/10.1073/pnas.0403382101 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....3960f7ae0155e499ad5d33798c8bc936 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 10916490 00278424 |
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| DOI: | 10.1073/pnas.0403382101 |