Bradykinin-related peptides from Phyllomedusa hypochondrialis

被引：53

作者：

Brand, G. D.

Krause, F. C.

Silva, L. P.

Leite, J. R. S. A.

Melo, J. A. T.

Prates, M. V.

Pesquero, J. B.

Santos, E. L.

Nakaie, C. R.

Costa-Neto, C. M.

Bloch, C., Jr.

机构：

[1] EMBRAPA, Lab Espectrometria Massa, Recursos Genet & Biotecnol, Estacao Parque Biol, BR-70770900 Brasilia, DF, Brazil

[2] Univ Brasilia, Programa Posgrad Biol Anim, IB, BR-70910900 Brasilia, DF, Brazil

[3] Univ Fed Sao Paulo, Escola Paulista Med, Dept Biofis, BR-04023062 Sao Paulo, Brazil

[4] Univ Sao Paulo, Fac Med Ribeirao Preto, Dept Bioquim & Imunol, BR-14049900 Ribeirao Preto, Brazil

来源：

PEPTIDES | 2006年 / 27卷 / 09期

关键词：

imaging mass spectrometry; frog skin; BRP; Phyllomedusa;

D O I：

10.1016/j.peptides.2006.04.020

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：2137 / 2146

页数：10

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