An amino-terminal fragment of LCRF, LCRF-(1-35), has the same activity as the natural peptide

Published

Journal Article

A cholecystoki nin (CCK)-releasing peptide, luminal CCK-releasing factor (LCRF), has been purified from rat jejunal secretion. Amino acid analysis and mass spectral analysis showed that the purified peptide is composed of 70-75 amino acid residues and has a mass of 8, 136 Da. Microsequence analysis of LCRF yielded an amino acid sequence for the ammo-terminal 41 residues. To determine the biologically active region of the molecule, a peptide was synthesized consisting of the aminoterminal 35 amino acids of LCRF. In this study, intraduodenal infusion of LCRF-(1-35) significantly stimulated pancreatic secretion in conscious rats. The dose-response curves to LCRF-(1-35) and to monitor peptide were similar and biphasic, with higher doses producing submaximal pancreatic secretory responses. The CCK-A receptor antagonist MK-329 abolished the pancreatic secretory response to intraduodenally infused LCRF-(1-35). These results demonstrate that LCRF biological activity is contained within the amino-terminal 35-amino acid portion of LCRF, and this fragment may be useful for investigating the role of LCRF in gastrointestinal function. Copyright © 1997 the American Physiological Society.

Duke Authors

Cited Authors

  • Spannagel, AW; Reeve, JR; Liddle, RA; Guan, D; Green, GM

Published Date

  • December 1, 1997

Published In

Volume / Issue

  • 273 / 3 PART 1

International Standard Serial Number (ISSN)

  • 0002-9513

Citation Source

  • Scopus