, Volume 58, Issue 1, pp 3–13 | Cite as

Role of calcitonin gene-related peptide in energy metabolism

  • William Gustavo Lima
  • Gleuber Henrique Marques-Oliveira
  • Thaís Marques da Silva
  • Valéria Ernestânia Chaves



Calcitonin gene-related peptide (CGRP) is a neuropeptide produced by alternative tissue-specific splicing of the primary transcript of the CALC genes. CGRP is widely distributed in the central and peripheral nervous system, as well as in several organs and tissues. The presence of CGRP in the liver and brown and white adipose tissue suggests an effect of this neuropeptide on regulation of energy homeostasis.


In this review, we summarize the current knowledge of the effect of CGRP on the control of energy metabolism, primarily focusing on food intake, thermoregulation and lipid metabolism in adipose tissue, liver and muscle.


CGRP induces anorexia, stimulating anorexigenic neuropeptide and/or inhibiting orexigenic neuropeptide expression, through cAMP/PKA pathway activation. CGRP also induces energy expenditure, increasing the skin temperature and brown adipose tissue thermogenesis. It has been also suggested that information related to peripheral lipid stores may be conveyed to the brain via CGRP-sensory innervation from adipose tissue. More recently, it was demonstrated that mice lacking αCGRP are protected from obesity induced by high-fat diet and that CGRP regulates the content of lipid in liver, muscle and adipose tissue.


It is unclear the receptor responsible by CGRP effects, as well as whether this neuropeptide acts directly or indirectly in liver, muscle and adipose tissue.


Food intake Thermoregulation Lipid metabolism Obesity Hypothalamus TRPV1 



Acetyl-CoA carboxylase






AMP-dependent protein kinase


Body mass index


Calcitonin gene-related peptide


3′,5′-Cyclic adenosine monophosphate


Calcitonin receptor-like receptor


calcitonin receptor




Half-maximal effect


Free fatty acid


haematoxylin and eosin


Interscapular brown adipose tissue


Receptor activity-modifying proteins




transient receptor potential cation channel subfamily V member 1


Uncoupling protein



The authors would like to thank Renato Helios Migliorini (in memoriam) for being an exemplary scientist and professor.


This work was supported through funding from the Federal University of São João del-Rei. W.G.L. received a fellowship from the Fundação de Amparo à Pesquisa do Estado de Minas Gerais (FAPEMIG). T.M.S. received a fellowship from the Federal University of São João del-Rei.

Author contributions

All authors contributed to the development, analysis and drafting of this article.

Compliance with ethical standards

Conflicts of interest

The authors declare that they have no competing interests.


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© Springer Science+Business Media, LLC 2017

Authors and Affiliations

  1. 1.Laboratory of PhysiologyFederal University of São João del-ReiDivinópolisBrazil

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