Sauvagine

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Sauvagine
Identifiers
Organism Phyllomedusa sauvagei
SymbolN/A
CAS number 74434-59-6
UniProt P01144
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Structures Swiss-model
Domains InterPro

Sauvagine is a neuropeptide from the corticotropin-releasing factor (CRF) family of peptides and is orthologous to the mammalian hormone, urocortin 1, and the teleost fish hormone, urotensin 1. [1] It is 40 amino acids in length, [2] and has the 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 sauvagii. Given its relation to other CRF-related peptides, it exerts similar physiological effects as corticotropin-releasing hormone. [3] [4]

Sauvagine belongs to the corticotropin-releasing factor (CRF) family that also includes CRF, urocortin l/urotensin l, urocortin II and urocortin III. [5] [1]

Interactions

Sauvagine has been shown to interact with corticotropin releasing factor receptors 1 and 2, and (as with other CRF-related peptides) is also bound by the corticotropin-releasing factor binding protein. [6]

Related Research Articles

Peptides are short chains of amino acids linked by peptide bonds. A polypeptide is a longer, continuous, unbranched peptide chain. Polypeptides which have a molecular mass of 10,000 Da or more are called proteins. Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides.

<span class="mw-page-title-main">Proopiomelanocortin</span> Mammalian protein found in Homo sapiens

Pro-opiomelanocortin (POMC) is a precursor polypeptide with 241 amino acid residues. POMC is synthesized in corticotrophs of the anterior pituitary from the 267-amino-acid-long polypeptide precursor pre-pro-opiomelanocortin (pre-POMC), by the removal of a 26-amino-acid-long signal peptide sequence during translation. POMC is part of the central melanocortin system.

<span class="mw-page-title-main">Corticotropin-releasing hormone</span> Mammalian protein found in humans

Corticotropin-releasing hormone (CRH) is a peptide hormone involved in stress responses. It is a releasing hormone that belongs to corticotropin-releasing factor family. In humans, it is encoded by the CRH gene. Its main function is the stimulation of the pituitary synthesis of adrenocorticotropic hormone (ACTH), as part of the hypothalamic–pituitary–adrenal axis.

Corticotropin-releasing factor family, CRF family is a family of related neuropeptides in vertebrates. This family includes corticotropin-releasing hormone, urotensin-I, urocortin, and sauvagine. The family can be grouped into 2 separate paralogous lineages, with urotensin-I, urocortin and sauvagine in one group and CRH forming the other group. Urocortin and sauvagine appear to represent orthologues of fish urotensin-I in mammals and amphibians, respectively. The peptides have a variety of physiological effects on stress and anxiety, vasoregulation, thermoregulation, growth and metabolism, metamorphosis and reproduction in various species, and are all released as prohormones.

Corticotropes are basophilic cells in the anterior pituitary that produce pro-opiomelanocortin (POMC) which undergoes cleavage to adrenocorticotropin (ACTH), β-lipotropin (β-LPH), and melanocyte-stimulating hormone (MSH). These cells are stimulated by corticotropin releasing hormone (CRH) and make up 15–20% of the cells in the anterior pituitary. The release of ACTH from the corticotropic cells is controlled by CRH, which is formed in the cell bodies of parvocellular neurosecretory cells within the paraventricular nucleus of the hypothalamus and passes to the corticotropes in the anterior pituitary via the hypophyseal portal system. Adrenocorticotropin hormone stimulates the adrenal cortex to release glucocorticoids and plays an important role in the stress response.

<span class="mw-page-title-main">Dermorphin</span> Chemical compound

Dermorphin is a hepta-peptide first isolated from the skin of South American frogs belonging to the genus Phyllomedusa. The peptide is a natural opioid that binds as an agonist with high potency and selectivity to mu opioid receptors. Dermorphin is about 30–40 times more potent than morphine, but theoretically may be less likely to produce drug tolerance and addiction due to its high potency. The amino acid sequence of dermorphin is H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2.

Insect diuretic hormones are hormones that regulate water balance through diuretic action.

<span class="mw-page-title-main">Urocortin</span>

Urocortin is a protein that in humans is encoded by the UCN gene. Urocortin belongs to the corticotropin-releasing factor (CRF) family of proteins which includes CRF, urotensin I, sauvagine, urocortin II and urocortin III. Urocortin is involved in the mammalian stress response, and regulates aspects of appetite and stress response.

Urocortin 2 (Ucn2) is an endogenous peptide in the corticotrophin-releasing factor (CRF) family.

<span class="mw-page-title-main">Urotensin-II</span> Chemical compound

Urotensin-II (U-II) is a peptide ligand that is the strongest known vasoconstrictor. Because of the involvement of the UII system in multiple biological systems such as the cardiovascular, nervous, endocrine, and renal, it represents a promising target for the development of new drugs.

<span class="mw-page-title-main">Urotensin-II receptor</span> Protein-coding gene in the species Homo sapiens

The urotensin-2 receptor (UR-II-R) also known as GPR14 is a class A rhodopsin family G protein coupled-receptor (GPCR) that is 386 amino acids long which binds primarily to the neuropeptide urotensin II.[1] The receptor quickly rose to prominence when it was found that when activated by urotensin II it induced the most potent vasoconstriction effect ever seen. While the precise function of the urotensin II receptor is not fully known it has been linked to cardiovascular effects, stress, and REM sleep.

<span class="mw-page-title-main">Corticotropin-releasing hormone receptor 1</span> Protein and coding gene in humans

Corticotropin-releasing hormone receptor 1 (CRHR1) is a protein, also known as CRF1, with the latter (CRF1) now being the IUPHAR-recommended name. In humans, CRF1 is encoded by the CRHR1 gene at region 17q21.31, beside micrototubule-associated protein tau MAPT.

<span class="mw-page-title-main">Corticotropin-releasing hormone receptor 2</span> Protein found in humans

Corticotropin-releasing hormone receptor 2 (CRHR2) is a protein, also known by the IUPHAR-recommended name CRF2, that is encoded by the CRHR2 gene and occurs on the surfaces of some mammalian cells. CRF2 receptors are type 2 G protein-coupled receptors for corticotropin-releasing hormone (CRH) that are resident in the plasma membranes of hormone-sensitive cells. CRH, a peptide of 41 amino acids synthesized in the hypothalamus, is the principal neuroregulator of the hypothalamic-pituitary-adrenal axis, signaling via guanine nucleotide-binding proteins (G proteins) and downstream effectors such as adenylate cyclase. The CRF2 receptor is a multi-pass membrane protein with a transmembrane domain composed of seven helices arranged in a V-shape. CRF2 receptors are activated by two structurally similar peptides, urocortin II, and urocortin III, as well as CRH.

<span class="mw-page-title-main">CRHBP</span> Protein-coding gene in the species Homo sapiens

Corticotropin-releasing factor-binding protein is a protein that in humans is encoded by the CRHBP gene. It belongs to corticotropin-releasing hormone binding protein family.

<span class="mw-page-title-main">UCN2</span> Protein-coding gene in the species Homo sapiens

Urocortin-2 is a protein that in humans is encoded by the UCN2 gene.

<span class="mw-page-title-main">UCN3</span> Protein-coding gene in the species Homo sapiens

Urocortin-3 is a protein that, in humans, is encoded by the UCN3 gene. It belongs to the corticotropin-releasing hormone family.

<span class="mw-page-title-main">Antalarmin</span> Chemical compound

Antalarmin (CP-156,181) is a drug that acts as a CRH1 antagonist.

A Corticotropin-releasing hormone antagonist is a specific type of receptor antagonist that blocks the receptor sites for corticotropin-releasing hormone, also known as corticotropin-releasing factor (CRF), which synchronizes the behavioral, endocrine, autonomic, and immune responses to stress by controlling the hypothalamic-pituitary-adrenal axis. CRH antagonists thereby block the consequent secretions of ACTH and cortisol due to stress, among other effects.

Corticotropin-releasing hormone binding protein (CRH-BP) binds corticotropin-releasing hormone (CRH) and several related peptide hormones. It is an ancient, highly conserved protein whose origin predates the divergence of protostomes and deuterostomes.

<span class="mw-page-title-main">Urotensin II–related peptide</span>

Urotensin II-related peptide (URP) is a cyclic neuropeptide that is found in all vertebrates that have been genome sequenced so far. It has a long lasting hypotensive effect and may also regulate reproduction. It is part of the Urotensin II system and is one of the two endogenous ligands for rats, mice, and possibly humans.

References

  1. 1 2 Lovejoy DA, de Lannoy L (December 2013). "Evolution and phylogeny of the corticotropin-releasing factor (CRF) family of peptides: expansion and specialization in the vertebrates". Journal of Chemical Neuroanatomy. 54: 50–6. doi:10.1016/j.jchemneu.2013.09.006. PMID   24076419. S2CID   24576375.
  2. Montecucchi PC, Henschen A (August 1981). "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. 18 (2): 113–20. doi:10.1111/j.1399-3011.1981.tb02047.x. PMID   7309372.
  3. Falaschi P, D'Urso R, Negri L, Rocco A, Montecucchi PC, Henschen A, Melchiorri P, Erspamer V (August 1982). "Potent in vivo and in vitro prolactin inhibiting activity of sauvagine, a frog skin peptide". Endocrinology. 111 (2): 693–5. doi:10.1210/endo-111-2-693. PMID   7094889.
  4. Brown MR, Fisher LA, Spiess J, Rivier J, Rivier C, Vale W (July 1982). "Comparison of the biologic actions of corticotropin-releasing factor and sauvagine". Regulatory Peptides. 4 (2): 107–14. doi:10.1016/0167-0115(82)90101-X. PMID   6289384. S2CID   22063430.
  5. Fekete EM, Zorrilla EP (April 2007). "Physiology, pharmacology, and therapeutic relevance of urocortins in mammals: ancient CRF paralogs". Frontiers in Neuroendocrinology. 28 (1): 1–27. doi:10.1016/j.yfrne.2006.09.002. PMC   2730896 . PMID   17083971.
  6. Jahn O, Eckart K, Sydow S, Hofmann BA, Spiess J (January 2001). "Pharmacological characterization of recombinant rat corticotropin releasing factor binding protein using different sauvagine analogs". Peptides. 22 (1): 47–56. doi:10.1016/S0196-9781(00)00356-9. PMID   11179597. S2CID   45722298.