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Ranachensinin: A Novel Aliphatic Tachykinin from the Skin Secretion of the Chinese Brown Frog, Rana chensinensis.
MedLine Citation:
PMID:  24073664     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Amphibian skin secretions contain a plethora of pharmacologically-active substances and represent established sources of bioactive peptides, including tachykinins. Tachykinins are one of the most widely-studied peptide families in animals and are found in neuroendocrine tissues from the lowest vertebrates to mammals. They are characterized by the presence of a highly-conserved C-terminal pentapeptide amide sequence motif (-FXGLM-amide) that also constitutes the bioactive core of the peptide. Amidation of the C-terminal methioninyl residue appears to be mandatory in the expression of biological activity. Here, we describe the isolation, characterization and molecular cloning of a novel tachykinin named ranachensinin, from the skin secretion of the Chinese brown frog, Rana chensinensis. This peptide, DDTSDRSN QFIGLM-amide, contains the classical C-terminal pentapeptide amide motif in its primary structure and an Ile (I) residue in the variable X position. A synthetic replicate of ranachensinin, synthesized by solid-phase Fmoc chemistry, was found to contract the smooth muscle of rat urinary bladder with an EC50 of 20.46 nM. However, in contrast, it was found to be of low potency in contraction of rat ileum smooth muscle with an EC50 of 2.98 µM. These data illustrate that amphibian skin secretions continue to provide novel bioactive peptides with selective effects on functional targets in mammalian tissues.
Authors:
Yuxin Wu; Renjie Li; Jie Ma; Mei Zhou; Lei Wang; Timothy I McClure; Jiqun Cai; Tianbao Chen; Chris Shaw
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Publication Detail:
Type:  JOURNAL ARTICLE    
Journal Detail:
Title:  Protein and peptide letters     Volume:  20     ISSN:  1875-5305     ISO Abbreviation:  Protein Pept. Lett.     Publication Date:  2013 Nov 
Date Detail:
Created Date:  2013-9-30     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9441434     Medline TA:  Protein Pept Lett     Country:  -    
Other Details:
Languages:  ENG     Pagination:  1217-1224     Citation Subset:  -    
Affiliation:
Natural Drug Discovery Research Group, School of Pharmacy, Medical Biology Centre, Queen's University, 97 Lisburn Road, Belfast BT9 7BL, Northern Ireland, UK. l.wang@qub.ac.uk.
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