| Literature DB >> 16797783 |
G D Brand1, F C Krause, L P Silva, J R S A Leite, J A T Melo, M V Prates, J B Pesquero, E L Santos, C R Nakaie, C M Costa-Neto, C Bloch.
Abstract
Bradykinin related peptides (BRPs) present in the water-soluble secretion and freshly dissected skin fragments of Phyllomedusa hypochondrialis were investigated by mass spectrometry techniques. Eighteen BRPs, along with their post-translational modifications, were characterized in the secretion by de novo MS/MS sequencing and direct MALDI imaging experiments of the frog skin. These molecules revealed strong sequence similarities to the main plasma kinin of some mammals and reptiles. Such a diversity of molecules, within the same peptide family, belonging to a single amphibian species may be related to functional specializations of these peptides and a variety of corresponding receptors that might be present in a number of different predators. Also, a novel analog, [Val]1,[Thr]6-bradykinyl-Gln,Ser had its biological activity positively detected in cell culture expressing the human bradykinin B2 receptor and in guinea pig ileum preparations.Entities:
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Year: 2006 PMID： 16797783 DOI： 10.1016/j.peptides.2006.04.020
Source DB: PubMed Journal: Peptides ISSN： 0196-9781 Impact factor: 3.750