Binding sites for peptide-histidine-isoleucine (PHI) on rat insulinoma-derived RINm5F cells

Rüdiger Göke; J. Michael Conlon

doi:10.1016/0303-7207(88)90180-3

Binding sites for peptide-histidine-isoleucine (PHI) on rat insulinoma-derived RINm5F cells

Rüdiger Göke, J. Michael Conlon

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

6 Citations (Scopus)

Abstract

Specific binding sites for ¹²⁵I-labelled rat peptide-histidine-isoleucine (PHI) were identified on rat insulinoma-derived RINm5F cells. The concentrations of peptides producing half-maximal displacement of label were rat PHI, 0.36 ± 0.14 nM, vasoactive intestinal polypeptide (VIP), 0.38 ± 0.13 nM and secretin, approximately 0.2 μM. Glucagon and glucagon-like peptide-1(7-36)amide were without effect on binding. PHI and VIP produced dose-dependent increases in cAMP production in the cells that were significantly (P < 0.05) above unstimulated rates for ligand concentrations between 10^-8 and 10 ^-6 M. Both PHI and VIP produced a small but significant (P < 0.05) enhancement in the rate of release of immunoreactive insulin from the cells but the effect was not dose dependent.

Original language	English
Pages (from-to)	211-215
Number of pages	5
Journal	Molecular and Cellular Endocrinology
Volume	60
Issue number	2-3
DOIs	https://doi.org/10.1016/0303-7207(88)90180-3
Publication status	Published - Dec 1988
Externally published	Yes

Keywords

Cyclic AMP
Insulin release
Vasoactive intestinal polypeptide

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Endocrinology

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10.1016/0303-7207(88)90180-3

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@article{c6a5651fde414f65bbde82833b5c2472,

title = "Binding sites for peptide-histidine-isoleucine (PHI) on rat insulinoma-derived RINm5F cells",

abstract = "Specific binding sites for 125I-labelled rat peptide-histidine-isoleucine (PHI) were identified on rat insulinoma-derived RINm5F cells. The concentrations of peptides producing half-maximal displacement of label were rat PHI, 0.36 ± 0.14 nM, vasoactive intestinal polypeptide (VIP), 0.38 ± 0.13 nM and secretin, approximately 0.2 μM. Glucagon and glucagon-like peptide-1(7-36)amide were without effect on binding. PHI and VIP produced dose-dependent increases in cAMP production in the cells that were significantly (P < 0.05) above unstimulated rates for ligand concentrations between 10-8 and 10 -6 M. Both PHI and VIP produced a small but significant (P < 0.05) enhancement in the rate of release of immunoreactive insulin from the cells but the effect was not dose dependent.",

keywords = "Cyclic AMP, Insulin release, Vasoactive intestinal polypeptide",

author = "R{\"u}diger G{\"o}ke and Conlon, {J. Michael}",

note = "Funding Information: This work was supported by the Stiftung Volkswagenwerk. The authors thank Dr. Peter Flat& University of Surrey, U.K. for his gift of cells and for his help in establishing the cells in culture.",

year = "1988",

month = dec,

doi = "10.1016/0303-7207(88)90180-3",

language = "English",

volume = "60",

pages = "211--215",

journal = "Molecular and Cellular Endocrinology",

issn = "0303-7207",

publisher = "Elsevier Ireland Ltd",

number = "2-3",

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TY - JOUR

T1 - Binding sites for peptide-histidine-isoleucine (PHI) on rat insulinoma-derived RINm5F cells

AU - Göke, Rüdiger

AU - Conlon, J. Michael

N1 - Funding Information: This work was supported by the Stiftung Volkswagenwerk. The authors thank Dr. Peter Flat& University of Surrey, U.K. for his gift of cells and for his help in establishing the cells in culture.

PY - 1988/12

Y1 - 1988/12

N2 - Specific binding sites for 125I-labelled rat peptide-histidine-isoleucine (PHI) were identified on rat insulinoma-derived RINm5F cells. The concentrations of peptides producing half-maximal displacement of label were rat PHI, 0.36 ± 0.14 nM, vasoactive intestinal polypeptide (VIP), 0.38 ± 0.13 nM and secretin, approximately 0.2 μM. Glucagon and glucagon-like peptide-1(7-36)amide were without effect on binding. PHI and VIP produced dose-dependent increases in cAMP production in the cells that were significantly (P < 0.05) above unstimulated rates for ligand concentrations between 10-8 and 10 -6 M. Both PHI and VIP produced a small but significant (P < 0.05) enhancement in the rate of release of immunoreactive insulin from the cells but the effect was not dose dependent.

AB - Specific binding sites for 125I-labelled rat peptide-histidine-isoleucine (PHI) were identified on rat insulinoma-derived RINm5F cells. The concentrations of peptides producing half-maximal displacement of label were rat PHI, 0.36 ± 0.14 nM, vasoactive intestinal polypeptide (VIP), 0.38 ± 0.13 nM and secretin, approximately 0.2 μM. Glucagon and glucagon-like peptide-1(7-36)amide were without effect on binding. PHI and VIP produced dose-dependent increases in cAMP production in the cells that were significantly (P < 0.05) above unstimulated rates for ligand concentrations between 10-8 and 10 -6 M. Both PHI and VIP produced a small but significant (P < 0.05) enhancement in the rate of release of immunoreactive insulin from the cells but the effect was not dose dependent.

KW - Cyclic AMP

KW - Insulin release

KW - Vasoactive intestinal polypeptide

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U2 - 10.1016/0303-7207(88)90180-3

DO - 10.1016/0303-7207(88)90180-3

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AN - SCOPUS:0024226728

SN - 0303-7207

VL - 60

SP - 211

EP - 215

JO - Molecular and Cellular Endocrinology

JF - Molecular and Cellular Endocrinology

IS - 2-3

ER -

Binding sites for peptide-histidine-isoleucine (PHI) on rat insulinoma-derived RINm5F cells

Abstract

Keywords

ASJC Scopus subject areas

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