1. Bradykinin-related peptides from Phyllomedusa hypochondrialis.
- Author
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Brand GD, Krause FC, Silva LP, Leite JR, Melo JA, Prates MV, Pesquero JB, Santos EL, Nakaie CR, Costa-Neto CM, and Bloch C Jr
- Subjects
- Amino Acid Sequence, Animals, CHO Cells, Cricetinae, Cricetulus, Female, Guinea Pigs, Humans, Hydroxyproline chemistry, Mass Spectrometry, Molecular Sequence Data, Muscle, Smooth cytology, Muscle, Smooth metabolism, Ranidae classification, Receptor, Bradykinin B2 chemistry, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Transfection, Bradykinin analogs & derivatives, Bradykinin chemistry, Ranidae metabolism
- 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.
- Published
- 2006
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