Document Detail

Purification of peptides with differential cytolytic activities from the skin secretions of the Central American frog, Lithobates vaillanti (Ranidae).
MedLine Citation:
PMID:  19379837     Owner:  NLM     Status:  MEDLINE    
Peptide-based defenses of ranid frogs from Mexico and Central America have been studied in much less detail than those from North America. Peptides belonging to the brevinin-1 (5 peptides), palustrin-2 (1 peptide), and ranatuerin-2 (3 peptides) families were isolated from norepinephrine-stimulated skin secretions of the Costa Rican frog, Lithobates vaillanti (Ranidae) and characterized structurally. Brevinin-1VLa (FLGAIAGVAAKFLPKVFCFITKKC) and brevinin-1VLc (FLPVIASVAAKVLPK VFCFITKKC) showed particularly high growth-inhibitory potency (MIC < or =3 microM) against a Gram-positive microorganism Staphylococcus aureus and the opportunistic yeast pathogen Candida albicans and potent cytolytic activity (LC(50)< or =8 microM) against both human erythrocytes and HepG2 hepatoma-derived cells. The peptides were also active against a Gram-negative microorganism Escherichia coli (MIC< or =50 microM). Substitutions in brevinin-1VLd (Lys(11) --> Asn) and brevinin-1VLe (Lys(11) --> Ser) that decrease cationicity result in loss of activity against E. coli. Ranatuerin-2VLb (GIMDTIKGAAKDLAGQLLDKLKCKITKC) showed relatively weak antimicrobial activity (MIC> or =75 microM) but selective cytolytic activity against HepG2 tumor cells (LC(50)=30 microM) compared with erythrocytes (LC(50)>200 microM). In addition, a dodecapeptide (RICYAMWIPYPC) were isolated from the secretions that were devoid of antimicrobial activity. This component contains an Ala-Met bond that constitutes the scissile bond in the selective elastase inhibitor, elafin but the peptide did not inhibit pancreatic elastase at concentrations up to 100 microM.
J Michael Conlon; Haider Raza; Laurent Coquet; Thierry Jouenne; Jérôme Leprince; Hubert Vaudry; Jay D King
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-04-18
Journal Detail:
Title:  Comparative biochemistry and physiology. Toxicology & pharmacology : CBP     Volume:  150     ISSN:  1532-0456     ISO Abbreviation:  Comp. Biochem. Physiol. C Toxicol. Pharmacol.     Publication Date:  2009 Aug 
Date Detail:
Created Date:  2009-07-07     Completed Date:  2009-09-30     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100959500     Medline TA:  Comp Biochem Physiol C Toxicol Pharmacol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  150-4     Citation Subset:  IM    
Department of Biochemistry, Faculty of Medicine and Health Sciences, United Arab Emirates University, 17666 Al-Ain, United Arab Emirates.
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MeSH Terms
Amino Acid Sequence
Amphibian Proteins / chemistry,  isolation & purification*,  pharmacology
Antimicrobial Cationic Peptides / chemistry,  isolation & purification*,  pharmacology
Bodily Secretions / chemistry*,  secretion
Candida albicans / drug effects,  growth & development
Cell Line, Tumor
Cell Survival / drug effects
Costa Rica
Cytotoxins / chemistry,  isolation & purification*,  pharmacology
Dose-Response Relationship, Drug
Erythrocytes / drug effects
Escherichia coli / drug effects,  growth & development
Hemolysis / drug effects
Liver Neoplasms / pathology
Microbial Sensitivity Tests
Molecular Sequence Data
Molecular Structure
Norepinephrine / pharmacology
Peptides / chemistry,  isolation & purification*,  pharmacology
Ranidae / metabolism*
Skin / drug effects,  secretion*
Staphylococcus aureus / drug effects,  growth & development
Reg. No./Substance:
0/Amphibian Proteins; 0/Antimicrobial Cationic Peptides; 0/Cytotoxins; 0/Peptides; 51-41-2/Norepinephrine

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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