Bioactivity of intraduodenally and intravenously infused fragments of luminal cholecystokinin releasing factor (LCRF)

Alan W. Spannagel; Joseph R. Reeve; George H. Greeley; Noboro Yanaihara; Rodger A. Liddle; Gary M. Green

doi:10.1016/S0167-0115(97)01074-4

Bioactivity of intraduodenally and intravenously infused fragments of luminal cholecystokinin releasing factor (LCRF)

Alan W. Spannagel, Joseph R. Reeve, George H. Greeley, Noboro Yanaihara, Rodger A. Liddle, Gary M. Green

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

Abstract

A luminal cholecystokinin releasing factor (LCRF), has been purified from intestinal secretion and found to have a mass of 8136 daltons. The amino-terminal 41 residues have been sequenced. Previous studies showed that intraduodenal infusion of the synthetic amino-terminal 35 amino acid peptide, LCRF_1-35 significantly stimulated pancreatic protein and fluid secretion in conscious rats, but the peptide did not stimulate amylase release from isolated, dispersed pancreatic acini. In the present study, several fragments of LCRF were synthesized and tested for CCK-releasing activity (pancreatic protein secretion) to determine whether shorter fragments of LCRF exhibit the characteristic biological activity of native LCRF and synthetic LCRF_1-35. Compounds tested were LCRF_1-41, LCRF_1-35, LCRF_1-6, and LCRF_11-25. Of the fragments shorter than LCRF_1-35, only LCRF_11-25 but not LCRF_1-6 had significant CCK releasing activity. LCRF_1-41 was equivalent to LCRF_1-35 in potency and efficacy. Intravenous and intraduodenal infusion of LCRF_1-35 elicited nearly identical dose-response curves. Copyright (C) 1998 Elsevier Science B.V.

Original language	English (US)
Pages (from-to)	161-164
Number of pages	4
Journal	Regulatory Peptides
Volume	73
Issue number	3
DOIs	https://doi.org/10.1016/S0167-0115(97)01074-4
State	Published - Feb 27 1998
Externally published	Yes

Keywords

CCK
Exocrine pancreas
Feedback regulation

ASJC Scopus subject areas

Biochemistry
Physiology
Endocrinology
Clinical Biochemistry
Cellular and Molecular Neuroscience

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10.1016/S0167-0115(97)01074-4

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title = "Bioactivity of intraduodenally and intravenously infused fragments of luminal cholecystokinin releasing factor (LCRF)",

abstract = "A luminal cholecystokinin releasing factor (LCRF), has been purified from intestinal secretion and found to have a mass of 8136 daltons. The amino-terminal 41 residues have been sequenced. Previous studies showed that intraduodenal infusion of the synthetic amino-terminal 35 amino acid peptide, LCRF1-35 significantly stimulated pancreatic protein and fluid secretion in conscious rats, but the peptide did not stimulate amylase release from isolated, dispersed pancreatic acini. In the present study, several fragments of LCRF were synthesized and tested for CCK-releasing activity (pancreatic protein secretion) to determine whether shorter fragments of LCRF exhibit the characteristic biological activity of native LCRF and synthetic LCRF1-35. Compounds tested were LCRF1-41, LCRF1-35, LCRF1-6, and LCRF11-25. Of the fragments shorter than LCRF1-35, only LCRF11-25 but not LCRF1-6 had significant CCK releasing activity. LCRF1-41 was equivalent to LCRF1-35 in potency and efficacy. Intravenous and intraduodenal infusion of LCRF1-35 elicited nearly identical dose-response curves. Copyright (C) 1998 Elsevier Science B.V.",

keywords = "CCK, Exocrine pancreas, Feedback regulation",

author = "Spannagel, {Alan W.} and Reeve, {Joseph R.} and Greeley, {George H.} and Noboro Yanaihara and Liddle, {Rodger A.} and Green, {Gary M.}",

note = "Funding Information: This study was supported by NIH grants DK37482 (GMG), IBN-9506305 (GHG), DK38626 (RAL), and DK33850 (JRR). The excellent technical assistance of Kristen Xu is gratefully acknowledged.",

year = "1998",

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doi = "10.1016/S0167-0115(97)01074-4",

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T1 - Bioactivity of intraduodenally and intravenously infused fragments of luminal cholecystokinin releasing factor (LCRF)

AU - Spannagel, Alan W.

AU - Reeve, Joseph R.

AU - Greeley, George H.

AU - Yanaihara, Noboro

AU - Liddle, Rodger A.

AU - Green, Gary M.

N1 - Funding Information: This study was supported by NIH grants DK37482 (GMG), IBN-9506305 (GHG), DK38626 (RAL), and DK33850 (JRR). The excellent technical assistance of Kristen Xu is gratefully acknowledged.

PY - 1998/2/27

Y1 - 1998/2/27

N2 - A luminal cholecystokinin releasing factor (LCRF), has been purified from intestinal secretion and found to have a mass of 8136 daltons. The amino-terminal 41 residues have been sequenced. Previous studies showed that intraduodenal infusion of the synthetic amino-terminal 35 amino acid peptide, LCRF1-35 significantly stimulated pancreatic protein and fluid secretion in conscious rats, but the peptide did not stimulate amylase release from isolated, dispersed pancreatic acini. In the present study, several fragments of LCRF were synthesized and tested for CCK-releasing activity (pancreatic protein secretion) to determine whether shorter fragments of LCRF exhibit the characteristic biological activity of native LCRF and synthetic LCRF1-35. Compounds tested were LCRF1-41, LCRF1-35, LCRF1-6, and LCRF11-25. Of the fragments shorter than LCRF1-35, only LCRF11-25 but not LCRF1-6 had significant CCK releasing activity. LCRF1-41 was equivalent to LCRF1-35 in potency and efficacy. Intravenous and intraduodenal infusion of LCRF1-35 elicited nearly identical dose-response curves. Copyright (C) 1998 Elsevier Science B.V.

AB - A luminal cholecystokinin releasing factor (LCRF), has been purified from intestinal secretion and found to have a mass of 8136 daltons. The amino-terminal 41 residues have been sequenced. Previous studies showed that intraduodenal infusion of the synthetic amino-terminal 35 amino acid peptide, LCRF1-35 significantly stimulated pancreatic protein and fluid secretion in conscious rats, but the peptide did not stimulate amylase release from isolated, dispersed pancreatic acini. In the present study, several fragments of LCRF were synthesized and tested for CCK-releasing activity (pancreatic protein secretion) to determine whether shorter fragments of LCRF exhibit the characteristic biological activity of native LCRF and synthetic LCRF1-35. Compounds tested were LCRF1-41, LCRF1-35, LCRF1-6, and LCRF11-25. Of the fragments shorter than LCRF1-35, only LCRF11-25 but not LCRF1-6 had significant CCK releasing activity. LCRF1-41 was equivalent to LCRF1-35 in potency and efficacy. Intravenous and intraduodenal infusion of LCRF1-35 elicited nearly identical dose-response curves. Copyright (C) 1998 Elsevier Science B.V.

KW - CCK

KW - Exocrine pancreas

KW - Feedback regulation

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Bioactivity of intraduodenally and intravenously infused fragments of luminal cholecystokinin releasing factor (LCRF)

Abstract

Keywords

ASJC Scopus subject areas

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