Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2007-10-1
pubmed:abstractText
Aiming to extend the knowledge about the diversity of bradykinin-potentiating peptides (BPPs) and their precursor proteins, a venom gland cDNA library from the South American rattlesnake (Crotalus dursissus terrificus, Cdt) was screened. Two novel homologous cDNAs encoding the BPPs precursor protein were cloned. Their sequence contain only one single longer BPP sequence with the typical IPP-tripeptide, and two short potential BPP-like molecules, revealing a unique structural organization. Several peptide sequences structurally similar to the BPPs identified in the precursor protein from Cdt and also from others snakes, were chemically synthesized and were bioassayed both in vitro and in vivo, by means of isolated smooth muscle preparations and by measurements of blood pressure in anaesthetized rats, respectively. We demonstrate here that a pyroglutamyl residue at the N-terminus with a high content of proline residues, even with the presence of a IPP moiety characteristic of typical BPPs, are not enough to determine a bradykinin-potentiating activity to these peptides. Taken together, our results indicate that the characterization of the BPPs precursor proteins and identification of characteristic glutamine residues followed by proline-rich peptide sequences are not enough to predict if these peptides, even with a pyroglutamyl residue at the N-terminus, will present the typical pharmacological activities described for the BPPs.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-2952
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
74
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1350-60
pubmed:meshHeading
pubmed-meshheading:17714693-Amino Acid Sequence, pubmed-meshheading:17714693-Animals, pubmed-meshheading:17714693-Antihypertensive Agents, pubmed-meshheading:17714693-Base Sequence, pubmed-meshheading:17714693-Blood Pressure, pubmed-meshheading:17714693-Cloning, Molecular, pubmed-meshheading:17714693-Crotalid Venoms, pubmed-meshheading:17714693-Crotalus, pubmed-meshheading:17714693-Guinea Pigs, pubmed-meshheading:17714693-Ileum, pubmed-meshheading:17714693-Male, pubmed-meshheading:17714693-Molecular Sequence Data, pubmed-meshheading:17714693-Muscle, Smooth, pubmed-meshheading:17714693-Muscle Contraction, pubmed-meshheading:17714693-Oligopeptides, pubmed-meshheading:17714693-Protein Precursors, pubmed-meshheading:17714693-Rats, pubmed-meshheading:17714693-Rats, Wistar, pubmed-meshheading:17714693-Salivary Glands, pubmed-meshheading:17714693-Sequence Alignment, pubmed-meshheading:17714693-Sequence Homology, Nucleic Acid, pubmed-meshheading:17714693-Structure-Activity Relationship
pubmed:year
2007
pubmed:articleTitle
Identification of novel bradykinin-potentiating peptides (BPPs) in the venom gland of a rattlesnake allowed the evaluation of the structure-function relationship of BPPs.
pubmed:affiliation
Center for Applied Toxinology, Instituto Butantan, São Paulo, SP, Brazil.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't