Cysteamine selectively enhances neuropeptide Y2 receptor binding activity

Wei Li; Terry D. Hexum

doi:10.1016/0006-291X(92)91204-4

Cysteamine selectively enhances neuropeptide Y₂ receptor binding activity

Wei Li, Terry D. Hexum

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

Abstract

Affinity labeling of [¹²⁵I]NPY to the bovine hippocampal NPY receptor has revealed a 50 kDa specific binding protein, the Y₂ receptor. Cysteamine (10 μM - 10 mM) specifically enhanced NPY specific labeling of the Y₂ receptor without affecting crosslinking effeiciency. Several structurally related agents, including reduced glutathione, cysteine, β-mercaptoethanol and ethanolamine, were without effect on receptor binding. The enhancement of binding by cysteamine could be reversed by washing the membranes. These studies suggest that cysteamine may change the conformation of the NPY Y₂ receptor and increase its binding activity.

Original language	English (US)
Pages (from-to)	380-386
Number of pages	7
Journal	Biochemical and biophysical research communications
Volume	184
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(92)91204-4
State	Published - Apr 15 1992
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "Cysteamine selectively enhances neuropeptide Y2 receptor binding activity",

abstract = "Affinity labeling of [125I]NPY to the bovine hippocampal NPY receptor has revealed a 50 kDa specific binding protein, the Y2 receptor. Cysteamine (10 μM - 10 mM) specifically enhanced NPY specific labeling of the Y2 receptor without affecting crosslinking effeiciency. Several structurally related agents, including reduced glutathione, cysteine, β-mercaptoethanol and ethanolamine, were without effect on receptor binding. The enhancement of binding by cysteamine could be reversed by washing the membranes. These studies suggest that cysteamine may change the conformation of the NPY Y2 receptor and increase its binding activity.",

author = "Wei Li and Hexum, {Terry D.}",

note = "Funding Information: This work was supported by a Grant-in-Aid from the American Heart Association, Nebraska Affiliate. Wei Li is a recipient of a Pre-doctoral Fellowship from the American Heart Association, Nebraska Affiliate. We thank Dr. Richard G. MacDonald for his helpful assistance the affinity labeling studies. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.",

year = "1992",

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doi = "10.1016/0006-291X(92)91204-4",

language = "English (US)",

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AU - Li, Wei

AU - Hexum, Terry D.

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PY - 1992/4/15

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N2 - Affinity labeling of [125I]NPY to the bovine hippocampal NPY receptor has revealed a 50 kDa specific binding protein, the Y2 receptor. Cysteamine (10 μM - 10 mM) specifically enhanced NPY specific labeling of the Y2 receptor without affecting crosslinking effeiciency. Several structurally related agents, including reduced glutathione, cysteine, β-mercaptoethanol and ethanolamine, were without effect on receptor binding. The enhancement of binding by cysteamine could be reversed by washing the membranes. These studies suggest that cysteamine may change the conformation of the NPY Y2 receptor and increase its binding activity.

AB - Affinity labeling of [125I]NPY to the bovine hippocampal NPY receptor has revealed a 50 kDa specific binding protein, the Y2 receptor. Cysteamine (10 μM - 10 mM) specifically enhanced NPY specific labeling of the Y2 receptor without affecting crosslinking effeiciency. Several structurally related agents, including reduced glutathione, cysteine, β-mercaptoethanol and ethanolamine, were without effect on receptor binding. The enhancement of binding by cysteamine could be reversed by washing the membranes. These studies suggest that cysteamine may change the conformation of the NPY Y2 receptor and increase its binding activity.

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