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Characterization of canine intestinal cholecystokinin-58 lacking its carboxyl-terminal nonapeptide. Evidence for similar post-translational processing in brain and gut.

Publication ,  Journal Article
Reeve, JR; Eysselein, V; Eberlein, GA; Chew, P; Ho, FJ; Huebner, VD; Shively, JE; Lee, TD; Liddle, RA
Published in: J Biol Chem
July 25, 1991

An antibody raised against a synthetic cholecystokinin (CCK) analog, (1-27)-(CCK)-33, corresponding to the midregion of CCK-58, detected immunoreactivity in intestinal extracts which eluted between the positions of CCK-33/39 and CCK-58 on high performance liquid chromatography. This peak, lacking carboxyl-terminal cholecystokinin immunoreactivity, was purified by reverse phase and cation-exchange chromatographies. Amino acid, mass spectral, and microsequence analysis established that it was the amino-terminal desnonapeptide fragment of cholecystokinin-58, (1-49)-CCK-58. It was demonstrated further that CCK-58 has less biological activity than CCK-8, suggesting that the amino terminus either sterically hindered the ability of CCK-58 to exert its biological activity or that its amino terminus acted at another site to inhibit release of amylase from rat pancreatic acini. The desnonapeptide of CCK-58 by itself had no biological activity, nor did it affect CCK-8-stimulated amylase release from isolated rat pancreatic acini, suggesting that the amino terminus shields the carboxyl terminus from expressing its biological activity. Its presence in intestine suggests that it is released into the circulation where it could be detected by midregion antibodies. The presence of high proportions of (1-49)-CCK-58 indicates that most CCK-8 is directly derived from CCK-58. Its occurrence in brain and intestine indicates similar processing for procholecystokinin in both tissues.

Duke Scholars

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

July 25, 1991

Volume

266

Issue

21

Start / End Page

13770 / 13776

Location

United States

Related Subject Headings

  • Structure-Activity Relationship
  • Secretory Rate
  • Rats
  • Protein Processing, Post-Translational
  • Peptide Fragments
  • Molecular Sequence Data
  • Mass Spectrometry
  • Intestinal Mucosa
  • In Vitro Techniques
  • Dogs
 

Citation

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Reeve, J. R., Eysselein, V., Eberlein, G. A., Chew, P., Ho, F. J., Huebner, V. D., … Liddle, R. A. (1991). Characterization of canine intestinal cholecystokinin-58 lacking its carboxyl-terminal nonapeptide. Evidence for similar post-translational processing in brain and gut. J Biol Chem, 266(21), 13770–13776.
Reeve, J. R., V. Eysselein, G. A. Eberlein, P. Chew, F. J. Ho, V. D. Huebner, J. E. Shively, T. D. Lee, and R. A. Liddle. “Characterization of canine intestinal cholecystokinin-58 lacking its carboxyl-terminal nonapeptide. Evidence for similar post-translational processing in brain and gut.J Biol Chem 266, no. 21 (July 25, 1991): 13770–76.
Reeve JR, Eysselein V, Eberlein GA, Chew P, Ho FJ, Huebner VD, et al. Characterization of canine intestinal cholecystokinin-58 lacking its carboxyl-terminal nonapeptide. Evidence for similar post-translational processing in brain and gut. J Biol Chem. 1991 Jul 25;266(21):13770–6.
Reeve JR, Eysselein V, Eberlein GA, Chew P, Ho FJ, Huebner VD, Shively JE, Lee TD, Liddle RA. Characterization of canine intestinal cholecystokinin-58 lacking its carboxyl-terminal nonapeptide. Evidence for similar post-translational processing in brain and gut. J Biol Chem. 1991 Jul 25;266(21):13770–13776.

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

July 25, 1991

Volume

266

Issue

21

Start / End Page

13770 / 13776

Location

United States

Related Subject Headings

  • Structure-Activity Relationship
  • Secretory Rate
  • Rats
  • Protein Processing, Post-Translational
  • Peptide Fragments
  • Molecular Sequence Data
  • Mass Spectrometry
  • Intestinal Mucosa
  • In Vitro Techniques
  • Dogs