Sauvagine is a protein that functions as a neuropeptide. It is 40 amino acids in length, and has sequence XGPPISIDLSLELLRKMIEIEKQEKEKQQAANNRLLLDTI-NH2, with a pyrrolidone carboxylic acid modification at the N-terminal and amidation of the C-terminal isoleucine residue. It was originally isolated from the skin of the frog Phyllomedusa sauvagei, but has been hypothesised to be produced endogenously by mammals, as it produces similar physiological effects to endogenous neuropeptides such as Corticotropin-releasing hormone.
- Montecucchi PC, Henschen A. Amino acid composition and sequence analysis of sauvagine, a new active peptide from the skin of Phyllomedusa sauvagei. International Journal of Peptide and Protein Research. 1981 Aug;18(2):113-20. PMID 7309372
- Falaschi P, D'Urso R, Negri L, Rocco A, Montecucchi PC, Henschen A, Melchiorri P, Erspamer V. Potent in vivo and in vitro prolactin inhibiting activity of sauvagine, a frog skin peptide. Endocrinology. 1982 Aug;111(2):693-5. PMID 7094889
- Brown MR, Fisher LA, Spiess J, Rivier J, Rivier C, Vale W. Comparison of the biologic actions of corticotropin-releasing factor and sauvagine. Regulatory Peptides. 1982; 4(2):107–114. DOI 10.1016/0167-0115(82)90101-X
- Fekete E. Physiology, pharmacology, and therapeutic relevance of urocortins in mammals: ancient CRF paralogs. Frontiers in Neuroendocrinology 2007; 28(1):1-27. DOI: 10.1016/j.yfrne.2006.09.002
- Lovejoy DA, de Lannoy L. Evolution and phylogeny of the corticotropin-releasing factor (CRF) family of peptides: expansion and specialization in the vertebrates. Journal of Chemical Neuroanatomy. 2013 Dec;54:50-6. doi: 10.1016/j.jchemneu.2013.09.006 PMID 24076419
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