A Receptor of the Immunoglobulin Superfamily Regulates Adaptive Thermogenesis

  1. Hurtado del Pozo, Carmen 3
  2. Ruiz, Henry H. 3
  3. Arivazhagan, Lakshmi 3
  4. Aranda, Juan Francisco 3
  5. Shim, Cynthia 3
  6. Daya, Peter 3
  7. Derk, Julia 3
  8. MacLean, Michael 3
  9. He, Meilun 3
  10. Frye, Laura 3
  11. Friedline, Randall H. 12
  12. Noh, Hye Lim 12
  13. Kim, Jason K. 145
  14. Friedman, Richard A. 67
  15. Ramasamy, Ravichandran 3
  16. Schmidt, Ann Marie 3
  1. 1 Program in Molecular Medicine, Department of Medicine, University of Massachusetts Medical School, Albert
  2. 2 Sherman Center, Worcester, MA 01605, USA
  3. 3 Diabetes Research Program, Division of Endocrinology, Diabetes and Metabolism, Department of Medicine, NYU School of Medicine, New York, NY 10016, USA
  4. 4 Sherman Center, Worcester, MA 01605, USA.
  5. 5 Division of Endocrinology, Metabolism and Diabetes, Department of Medicine, University of Massachusetts Medical School, Albert Sherman Center, Worcester, MA 01605, USA
  6. 6 Biomedical Informatics Shared Resource, Herbert Irving Comprehensive Cancer Center, and Department of Biomedical Informatics,
  7. 7 Columbia University Irving Medical Center, New York, NY 10032, USA
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Revista:
Cell Reports

ISSN: 2211-1247

Año de publicación: 2019

Volumen: 28

Número: 3

Páginas: 773-791.e7

Tipo: Artículo

DOI: 10.1016/J.CELREP.2019.06.061 GOOGLE SCHOLAR lock_openAcceso abierto editor

Otras publicaciones en: Cell Reports

Resumen

Exquisite regulation of energy homeostasis protects from nutrient deprivation but causes metabolic dysfunction upon nutrient excess. In human and murine adipose tissue, the accumulation of ligands of the receptor for advanced glycation end products (RAGE) accompanies obesity, implicating this receptor in energy metabolism. Here, we demonstrate that mice bearing global- or adipocyte-specific deletion of Ager, the gene encoding RAGE, display superior metabolic recovery after fasting, a cold challenge, or high-fat feeding. The RAGE-dependent mechanisms were traced to suppression of protein kinase A (PKA)-mediated phosphorylation of its key targets,hormone-sensitive lipase and p38 mitogen-activated protein kinase, upon b-adrenergic receptor stimulation—processes that dampen the expression andactivity of uncoupling protein 1 (UCP1) and thermogenic programs. This work identifies the innate role of RAGE as a key node in the immunometabolic networks that control responses to nutrient supply and cold challenges, and it unveils opportunities to harness energy expenditure in environmental and metabolic stress.

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