| Title: | Major urinary protein regulation of chemical communication and nutrient metabolism |
| Address: | "Department of Molecular & Integrative Physiology, University of Michigan Medical School, Ann Arbor, Michigan, USA" |
| DOI: | 10.1016/S0083-6729(10)83006-7 |
| ISSN/ISBN: | 0083-6729 (Print) 0083-6729 (Linking) |
| Abstract: | "The major urinary protein (MUP) family members contain a conserved beta-barrel structure with a characteristic central hydrophobic pocket. They are secreted by the liver and excreted into the urine. MUPs bind via their central pockets to volatile pheromones or other lipophilic molecules, and regulate pheromone transportation in the circulation, excretion in the kidney, and release into the air from urine marks. MUPs are highly polymorphic, and the MUP profiles in urine function as individual identity signatures of the owners. The MUP signatures are detected by the main and accessory olfactory systems and trigger adaptive behavioral responses and/or developmental processes. Circulating MUPs serve as a metabolic signal to regulate glucose and lipid metabolism. Recombinant MUP1 markedly ameliorates hyperglycemia and glucose intolerance in mice with type 2 diabetes. MUP1 suppresses hepatic gluconeogenesis and promotes energy expenditure in skeletal muscle by stimulating mitochondrial biogenesis and function. MUPs are unique members of the lipocalin superfamily that mediate both chemical and metabolic signaling" |
| Keywords: | "Animals Behavior/physiology Behavior, Animal/physiology Energy Metabolism/*physiology Humans Pheromones/*metabolism Proteins/chemistry/genetics/*physiology;" |
| Notes: | "MedlineZhou, Yingjiang Rui, Liangyou eng R01 DK065122/DK/NIDDK NIH HHS/ R01 DK073601/DK/NIDDK NIH HHS/ R01 DK 065122/DK/NIDDK NIH HHS/ Research Support, N.I.H., Extramural Review 2010/09/14 Vitam Horm. 2010; 83:151-63. doi: 10.1016/S0083-6729(10)83006-7" |
