Physiological importance and control of non-shivering facultative thermogenesis

Front Biosci (Schol Ed). 2011 Jan 1;3(1):352-71. doi: 10.2741/s156.


This review examines general and evolutionary aspects of temperature homeostasis, focusing on mammalian facultative or adaptive thermogenesis and its control by the sympathetic nervous system and hormones. Thyroid hormone acquired a new role with the advent of homeothermy enhancing facultative thermogenesis by interacting synergistically with the sympathetic nervous system, and directly increasing basal metabolic rate (obligatory thermogenesis). Facultative thermogenesis is triggered by cold. The major site of facultative thermogenesis in mammals is brown adipose tissue, endowed with abundant mitochondria rich in a protein called uncoupling protein-1. This protein can uncouple phosphorylation in a controlled manner, releasing the energy of the proton-motive force as heat. Its synthesis and function are regulated synergistically by the sympathetic nervous system and thyroid hormone and modulated by other hormones directly, or indirectly, modulating sympathetic activity as well as thyroid hormone secretion and activation in brown adipose tissue. Alternate, evolutionary older forms of facultative thermogenesis activated in transgenic mice with disabled brown adipose tissue thermogenesis reveal this latter as the culmination of energy-efficient facultative thermogenesis.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adaptation, Biological / physiology*
  • Adipose Tissue, Brown / metabolism*
  • Animals
  • Basal Metabolism / physiology
  • Biological Evolution*
  • Ion Channels / metabolism*
  • Mice
  • Mitochondrial Proteins / metabolism*
  • Shivering / physiology
  • Sympathetic Nervous System / physiology*
  • Thermogenesis / physiology*
  • Thyroid Hormones / metabolism*
  • Uncoupling Protein 1


  • Ion Channels
  • Mitochondrial Proteins
  • Thyroid Hormones
  • Ucp1 protein, mouse
  • Uncoupling Protein 1