Two novel rat guanylin molecules, guanylin-94 and guanylin-16, do not increase cyclic GMP production in T84 cells

Biochem Biophys Res Commun. 1995 Sep 25;214(3):1204-10. doi: 10.1006/bbrc.1995.2414.

Abstract

Guanylin, a 15-amino acid peptide homologue of bacterial heat-stable enterotoxins, is an endogenous activator of guanylate cyclase C (GC-C). We isolated two novel guanylin molecules from rat intestinal mucosa. They contained guanylin-15 at their C-termini and were identified as guanylin-94 and guanylin-16 by amino acid sequencing and mass spectrometry. Guanylin-94 and guanylin-16 in total account for 85% of guanylin molecules in both the small and large intestine, guanylin-15 being a minor component. Rat guanylin-94 and guanylin-16 did not increase cyclic GMP production in T84 cells. Identification of the post-translational processing products of guanylin should provide a better understanding of the biosynthesis of the peptide.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 1-Methyl-3-isobutylxanthine / pharmacology
  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Chromatography, Gel
  • Chromatography, High Pressure Liquid
  • Colon
  • Cyclic GMP / metabolism*
  • Gastrointestinal Hormones*
  • Ileum
  • Intercellular Signaling Peptides and Proteins
  • Intestinal Mucosa / chemistry
  • Kinetics
  • Male
  • Mass Spectrometry
  • Molecular Sequence Data
  • Natriuretic Peptides
  • Peptides / chemistry
  • Peptides / isolation & purification
  • Peptides / metabolism
  • Peptides / pharmacology*
  • Protein Processing, Post-Translational
  • Rats
  • Rats, Sprague-Dawley

Substances

  • Gastrointestinal Hormones
  • Intercellular Signaling Peptides and Proteins
  • Natriuretic Peptides
  • Peptides
  • guanylin 16
  • guanylin 94
  • guanylin
  • Cyclic GMP
  • 1-Methyl-3-isobutylxanthine