Freezing eliminates a specific population of l-glutamate receptors in synaptic membranes

Graham E. Fagg; E. Edward Mena; Daniel T. Monaghan; Carl W. Cotman

doi:10.1016/0304-3940(83)90033-2

Freezing eliminates a specific population of l-glutamate receptors in synaptic membranes

Graham E. Fagg, E. Edward Mena, Daniel T. Monaghan, Carl W. Cotman

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

43 Scopus citations

Abstract

The binding of l-[³H]glutamate (l-Glu) to freeze-thawed synaptic membranes (SPMs) exhibited saturation kinetics, with K_d 507 nM and B_max 6.99 pmol/mg protein. The effects of ions, the susceptibility to Triton X-100 and the pharmacological properties of the binding indicated that those sites detected in freeze-thawed SPMs were only of the C1^-/Ca²⁺-independent type. The C1^-/Ca²⁺-dependent (2-amino-4-phosphonobutyrate-sensitive) l-Glu binding sites which are additionally present in fresh SPMs are abolished by freezing.

Original language	English (US)
Pages (from-to)	157-162
Number of pages	6
Journal	Neuroscience Letters
Volume	38
Issue number	2
DOIs	https://doi.org/10.1016/0304-3940(83)90033-2
State	Published - Jul 29 1983
Externally published	Yes

Keywords

2-amino-4-phosphonobutyrate
acidic amino acid receptor classes
freezing
glutamate receptors
ions
synaptic membranes

ASJC Scopus subject areas

General Neuroscience

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10.1016/0304-3940(83)90033-2

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title = "Freezing eliminates a specific population of l-glutamate receptors in synaptic membranes",

abstract = "The binding of l-[3H]glutamate (l-Glu) to freeze-thawed synaptic membranes (SPMs) exhibited saturation kinetics, with Kd 507 nM and Bmax 6.99 pmol/mg protein. The effects of ions, the susceptibility to Triton X-100 and the pharmacological properties of the binding indicated that those sites detected in freeze-thawed SPMs were only of the C1-/Ca2+-independent type. The C1-/Ca2+-dependent (2-amino-4-phosphonobutyrate-sensitive) l-Glu binding sites which are additionally present in fresh SPMs are abolished by freezing.",

keywords = "2-amino-4-phosphonobutyrate, acidic amino acid receptor classes, freezing, glutamate receptors, ions, synaptic membranes",

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year = "1983",

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doi = "10.1016/0304-3940(83)90033-2",

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volume = "38",

pages = "157--162",

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T1 - Freezing eliminates a specific population of l-glutamate receptors in synaptic membranes

AU - Fagg, Graham E.

AU - Edward Mena, E.

AU - Monaghan, Daniel T.

AU - Cotman, Carl W.

PY - 1983/7/29

Y1 - 1983/7/29

N2 - The binding of l-[3H]glutamate (l-Glu) to freeze-thawed synaptic membranes (SPMs) exhibited saturation kinetics, with Kd 507 nM and Bmax 6.99 pmol/mg protein. The effects of ions, the susceptibility to Triton X-100 and the pharmacological properties of the binding indicated that those sites detected in freeze-thawed SPMs were only of the C1-/Ca2+-independent type. The C1-/Ca2+-dependent (2-amino-4-phosphonobutyrate-sensitive) l-Glu binding sites which are additionally present in fresh SPMs are abolished by freezing.

AB - The binding of l-[3H]glutamate (l-Glu) to freeze-thawed synaptic membranes (SPMs) exhibited saturation kinetics, with Kd 507 nM and Bmax 6.99 pmol/mg protein. The effects of ions, the susceptibility to Triton X-100 and the pharmacological properties of the binding indicated that those sites detected in freeze-thawed SPMs were only of the C1-/Ca2+-independent type. The C1-/Ca2+-dependent (2-amino-4-phosphonobutyrate-sensitive) l-Glu binding sites which are additionally present in fresh SPMs are abolished by freezing.

KW - 2-amino-4-phosphonobutyrate

KW - acidic amino acid receptor classes

KW - freezing

KW - glutamate receptors

KW - ions

KW - synaptic membranes

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JO - Neuroscience Letters

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ER -

Freezing eliminates a specific population of l-glutamate receptors in synaptic membranes

Abstract

Keywords

ASJC Scopus subject areas

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