Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2003-10-15
pubmed:abstractText
Lys49 phospholipase A2 homologues constitute a group of catalytically-inactive proteins, present in the venoms of many crotalid snakes, which induce myonecrosis. Current evidence supports the mapping of their toxic site to the C-terminal region, where amino acids comprised within the sequence 115-129 appear to play a central role in toxicity. This study evaluated the possible toxic effects of several synthetic peptides corresponding to the sequence 115-129 of different Lys49 myotoxins, using in vitro cytotoxicity and in vivo myotoxicity assays. Peptides varied widely in their activities, ranging from fully toxic to harmless. Thus, the toxic actions of Lys49 myotoxins cannot always be reproduced by their free peptides 115-129. Peptides from Agkistrodon p. piscivorus (AppK) and A. contortrix laticinctus Lys49 myotoxins exerted both cytotoxicity and myotoxicity. Random scrambling of peptide AppK resulted in complete loss of toxicity, demonstrating that its specific sequence of residues, rather than their simple presence or frequency, confers its ability to damage muscle. Peptide AppK synthesized with D-amino acids retained both activities of the natural L-enantiomer, suggesting that its mechanism of action does not involve the recognition of a proteic receptor/acceptor site on muscle cells, but possibly the binding to other structures, such as negatively-charged membrane phospholipids.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0041-0101
pubmed:author
pubmed:issnType
Print
pubmed:volume
42
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
307-12
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Comparative study of synthetic peptides corresponding to region 115-129 in Lys49 myotoxic phospholipases A2 from snake venoms.
pubmed:affiliation
Facultad de Microbiología, Instituto Clodomiro Picado, Universidad de Costa Rica, San José, Costa Rica. blomonte@cariari.ucr.ac.cr
pubmed:publicationType
Journal Article, Comparative Study