Isolation, localization, and cardiovascular activity of tachykinins from the stomach of the bowfin Amia calva

D. Waugh, K. E. Groff, B. Platzack, J. H. Youson, K. R. Olson, J. M. Conlon

Research output: Contribution to journalArticle

16 Scopus citations

Abstract

The bowfin is an extant representative of an ancient group of ray-tinned fish with evolutionary connections to modern teleosts. A peptide with substance P-like immunoreactivity was isolated from an extract of bowfin stomach and its primary structure was established as Ser-Lys-Ser-His-Gln- Phe-Tyr-Gly-Leu-Met-NH2. This amino acid sequence resembles mammalian substance P only in the COOH-terminal region of the peptide. A second tachykinin with neurokinin A-like immunoreactivity isolated from the extract comprises 23 amino acid residues and shows limited structural similarity to mammalian neuropeptide-γ. A randomly distributed population of cells in the gastric glands of the bowfin were immunostained with an antiserum raised against substance P, but no immunopositive structures were identified in the surface epithelium, lamina propria, or the nerve plexuses of the submucosa. Bolus injections of synthetic bowfin substance P (0.1-10 nmol/kg) into the bulbus arteriosus of unanesthetized bowfin resulted in a significant and dose-dependent rise in vascular resistance and arterial blood pressure (P < 0.01) and a fall in cardiac output (P < 0.05) without change in heart rate. After 5-10 min, arterial pressure and vascular resistance returned to preinjection levels, but cardiac output significantly (P < 0.05) increased over baseline values. The response to the peptide was unaffected by pretreatment of the animals with phentolamine. The study has shown that the stomach of the bowfin synthesizes tachykinins with novel structural features that display cardiovascular activity in this species.

Original languageEnglish (US)
Pages (from-to)R565-R571
JournalAmerican Journal of Physiology - Regulatory Integrative and Comparative Physiology
Volume269
Issue number3 38-3
StatePublished - Jan 1 1995
Externally publishedYes

Keywords

  • Amiiformes
  • neuropeptide-γ
  • substance P

ASJC Scopus subject areas

  • Physiology
  • Physiology (medical)

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