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Hemorphin and hemorphin-like peptides isolated from dog pancreas and sheep brain are able to potentiate bradykinin activity in vivo.
Ianzer, Danielle; Konno, Katsuhiro; Xavier, Carlos Henrique; Stöcklin, Reto; Santos, Robson Augusto S; de Camargo, Antônio Carlos Martins; Pimenta, Daniel Carvalho.
Afiliação
  • Ianzer D; Center for Applied Toxinology, CAT-CEPID, Laboratório Especial de Toxinologia Aplicada, Instituto Butantan, Av. Vital Brasil 1500, Sao Paulo, SP 05503-900, Brazil.
Peptides ; 27(11): 2957-66, 2006 Nov.
Article em En | MEDLINE | ID: mdl-16904236
Hemorphins are biologically active peptides, derived from hemoglobin, which presents a number of physiological activities. Proteolytic generation of these peptides is not fully understood; however, among their roles, is to provoke reduction on blood pressure. In this work, this particular biological effect was chosen as the monitor for the selection of mammalian vasoactive peptides. By combining high-performance liquid chromatography and mass spectrometry, including 'de novo' sequencing, several hemorphin-like peptides were identified presenting bradykinin potentiating activity. Moreover, taking LVV-hemorphin-7 as model compound, we evaluated its biological effect on blood pressure of anaesthetized rats. By summarizing all the results, it is possible to present the hemorphins as a family of proteolytically generated peptides that are able to potentiate bradykinin activity in vivo.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Pâncreas / Fragmentos de Peptídeos / Peptídeos / Química Encefálica / Hemoglobinas / Bradicinina Limite: Animals Idioma: En Revista: Peptides Ano de publicação: 2006 Tipo de documento: Article País de afiliação: Brasil País de publicação: Estados Unidos
Buscar no Google
Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Pâncreas / Fragmentos de Peptídeos / Peptídeos / Química Encefálica / Hemoglobinas / Bradicinina Limite: Animals Idioma: En Revista: Peptides Ano de publicação: 2006 Tipo de documento: Article País de afiliação: Brasil País de publicação: Estados Unidos