Isolation and biological activity of [Trp5]bradykinin from the plasma of the phylogenetically ancient fish, the bowfin and the longnosed gar

J. Michael Conlon, Bjorn Platzack, Luciano E. Marra, John H. Youson, Kenneth Olson

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

The holostean fish occupy an important position in vertebrate phylogeny as extant representatives of a ancient group of ray-finned fish with evolutionary connections to present-day teleosts. Incubation of heat-denatured plasma from the bowfin Amia calva with trypsin generated bradykinin-like immunoreactivity. The primary structure of bowfin bradykinin was established as Ala-Pro-Pro-Gly-Trp-Ser-Pro-Phe-Arg. This amino acid sequence contains one amino acid substitution (Phe5 → Trp) compared with mammalian bradykinin. The same peptide was generated in heat-denatured plasma from the longnosed gar Lepisosteus osseus. Treatment of plasma from either the bowfin or gar with glass beads under conditions previously shown to activate Factor XII in the plasma of mammals and reptiles did not generate bradykinin. Bolus injections of synthetic bowfin bradykinin (0.1, 0.3, and 1.0 nmol/kg) into the bulbus arteriosus of unanesthetized bowfin resulted in an immediate fall in arterial blood pressure of 5-10 min duration that was followed by a dose-dependent rise in pressure that was sustained for 30-60 min. There was no change in heart rate following bradykinin administration. The data suggest that the kallikrein-kinin system may predate the appearance of teleosts and may play a role in cardiovascular regulation in holosteans.

Original languageEnglish
Pages (from-to)485-489
Number of pages5
JournalPeptides
Volume16
Issue number3
DOIs
StatePublished - 1995

Fingerprint

Bradykinin
Bioactivity
Fish
Fishes
Plasmas
Hot Temperature
Skates (Fish)
Kallikrein-Kinin System
Factor XII
Amino Acids
Kinins
Kallikreins
Mammals
Reptiles
Blood pressure
Amino Acid Substitution
Phylogeny
Prednisolone
Trypsin
Glass

Keywords

  • Arterial blood pressure
  • Bradykinin
  • Holostean

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Physiology
  • Cellular and Molecular Neuroscience

Cite this

Isolation and biological activity of [Trp5]bradykinin from the plasma of the phylogenetically ancient fish, the bowfin and the longnosed gar. / Conlon, J. Michael; Platzack, Bjorn; Marra, Luciano E.; Youson, John H.; Olson, Kenneth.

In: Peptides, Vol. 16, No. 3, 1995, p. 485-489.

Research output: Contribution to journalArticle

Conlon, J. Michael ; Platzack, Bjorn ; Marra, Luciano E. ; Youson, John H. ; Olson, Kenneth. / Isolation and biological activity of [Trp5]bradykinin from the plasma of the phylogenetically ancient fish, the bowfin and the longnosed gar. In: Peptides. 1995 ; Vol. 16, No. 3. pp. 485-489.
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