Bradykinin-related peptides from Phyllomedusa hypochondrialis

Bradykinin-related peptides from Phyllomedusa hypochondrialis

Author Brand, G. D. Google Scholar
Krause, F. C. Google Scholar
Silva, L. P. Google Scholar
Leite, J. R. S. A. Google Scholar
Melo, J. A. T. Google Scholar
Prates, M. V. Google Scholar
Pesquero, J. B. Google Scholar
Santos, E. L. Google Scholar
Nakaie, C. R. Google Scholar
Costa-Neto, C. M. Google Scholar
Bloch, C. Google Scholar
Institution Empresa Brasileira de Pesquisa Agropecuária (EMBRAPA)
Universidade de Brasília (UnB)
Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
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 B-2 receptor and in guinea pig ileum preparations. (c) 2006 Elsevier Inc. All rights reserved.
Keywords imaging mass spectrometry
frog skin
Language English
Date 2006-09-01
Published in Peptides. New York: Elsevier B.V., v. 27, n. 9, p. 2137-2146, 2006.
ISSN 0196-9781 (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 2137-2146
Access rights Closed access
Type Article
Web of Science ID WOS:000240379800013

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