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

Publication ,  Journal Article
Spannagel, AW; Reeve, JR; Liddle, RA; Guan, D; Green, GM
Published in: Am J Physiol
September 1997

A cholecystokinin (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 amino-terminal 41 residues. To determine the biologically active region of the molecule, a peptide was synthesized consisting of the amino-terminal 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.

Duke Scholars

Published In

Am J Physiol

DOI

ISSN

0002-9513

Publication Date

September 1997

Volume

273

Issue

3 Pt 1

Start / End Page

G754 / G758

Location

United States

Related Subject Headings

  • Trypsin Inhibitor, Kazal Pancreatic
  • Sincalide
  • Rats, Wistar
  • Rats
  • Peptide Fragments
  • Pancreatic Juice
  • Pancreas
  • Molecular Weight
  • Male
  • Intercellular Signaling Peptides and Proteins
 

Citation

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Spannagel, A. W., Reeve, J. R., Liddle, R. A., Guan, D., & Green, G. M. (1997). An amino-terminal fragment of LCRF, LCRF-(1-35), has the same activity as the natural peptide. Am J Physiol, 273(3 Pt 1), G754–G758. https://doi.org/10.1152/ajpgi.1997.273.3.G754
Spannagel, A. W., J. R. Reeve, R. A. Liddle, D. Guan, and G. M. Green. “An amino-terminal fragment of LCRF, LCRF-(1-35), has the same activity as the natural peptide.Am J Physiol 273, no. 3 Pt 1 (September 1997): G754–58. https://doi.org/10.1152/ajpgi.1997.273.3.G754.
Spannagel AW, Reeve JR, Liddle RA, Guan D, Green GM. An amino-terminal fragment of LCRF, LCRF-(1-35), has the same activity as the natural peptide. Am J Physiol. 1997 Sep;273(3 Pt 1):G754–8.
Spannagel, A. W., et al. “An amino-terminal fragment of LCRF, LCRF-(1-35), has the same activity as the natural peptide.Am J Physiol, vol. 273, no. 3 Pt 1, Sept. 1997, pp. G754–58. Pubmed, doi:10.1152/ajpgi.1997.273.3.G754.
Spannagel AW, Reeve JR, Liddle RA, Guan D, Green GM. An amino-terminal fragment of LCRF, LCRF-(1-35), has the same activity as the natural peptide. Am J Physiol. 1997 Sep;273(3 Pt 1):G754–G758.

Published In

Am J Physiol

DOI

ISSN

0002-9513

Publication Date

September 1997

Volume

273

Issue

3 Pt 1

Start / End Page

G754 / G758

Location

United States

Related Subject Headings

  • Trypsin Inhibitor, Kazal Pancreatic
  • Sincalide
  • Rats, Wistar
  • Rats
  • Peptide Fragments
  • Pancreatic Juice
  • Pancreas
  • Molecular Weight
  • Male
  • Intercellular Signaling Peptides and Proteins