Lateral mobility of β-receptors involved in adenylate cyclase activation

Daphne Atlas; David J. Volsky; Alexander Levitzki

doi:10.1016/0005-2736(80)90150-9

Lateral mobility of β-receptors involved in adenylate cyclase activation

Daphne Atlas^*, David J. Volsky, Alexander Levitzki

^*Corresponding author for this work

Alexander Silberman Institute of Life Sciences

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

16 Scopus citations

Abstract

Cationized ferritin was found to inhibit the lateral mobility of intramembrane proteins in turkey erythrocyte membranes and the activation of adenylate cyclase by the (-)-epinephrine-bound β-adrenergic receptor. It was observed that cationized ferritin has only a small direct effect on the β-receptor and on the adenylate cyclase moiety. It is concluded that the cationized ferritin-induced inhibition of the hormone-dependent cyclase activity results from the inhibition of the lateral mobility of the receptor and therefore a decrease in the bimolecular rate of interaction between the receptor and the enzyme.

Original language	English
Pages (from-to)	64-69
Number of pages	6
Journal	Biochimica et Biophysica Acta - Biomembranes
Volume	597
Issue number	1
DOIs	https://doi.org/10.1016/0005-2736(80)90150-9
State	Published - 27 Mar 1980

Keywords

(Erythrocyte membrane)
Adenylate cyclase activation
Ferritin
β-Receptor

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10.1016/0005-2736(80)90150-9

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title = "Lateral mobility of β-receptors involved in adenylate cyclase activation",

abstract = "Cationized ferritin was found to inhibit the lateral mobility of intramembrane proteins in turkey erythrocyte membranes and the activation of adenylate cyclase by the (-)-epinephrine-bound β-adrenergic receptor. It was observed that cationized ferritin has only a small direct effect on the β-receptor and on the adenylate cyclase moiety. It is concluded that the cationized ferritin-induced inhibition of the hormone-dependent cyclase activity results from the inhibition of the lateral mobility of the receptor and therefore a decrease in the bimolecular rate of interaction between the receptor and the enzyme.",

keywords = "(Erythrocyte membrane), Adenylate cyclase activation, Ferritin, β-Receptor",

author = "Daphne Atlas and Volsky, \{David J.\} and Alexander Levitzki",

year = "1980",

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day = "27",

doi = "10.1016/0005-2736(80)90150-9",

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AU - Atlas, Daphne

AU - Volsky, David J.

AU - Levitzki, Alexander

PY - 1980/3/27

Y1 - 1980/3/27

N2 - Cationized ferritin was found to inhibit the lateral mobility of intramembrane proteins in turkey erythrocyte membranes and the activation of adenylate cyclase by the (-)-epinephrine-bound β-adrenergic receptor. It was observed that cationized ferritin has only a small direct effect on the β-receptor and on the adenylate cyclase moiety. It is concluded that the cationized ferritin-induced inhibition of the hormone-dependent cyclase activity results from the inhibition of the lateral mobility of the receptor and therefore a decrease in the bimolecular rate of interaction between the receptor and the enzyme.

AB - Cationized ferritin was found to inhibit the lateral mobility of intramembrane proteins in turkey erythrocyte membranes and the activation of adenylate cyclase by the (-)-epinephrine-bound β-adrenergic receptor. It was observed that cationized ferritin has only a small direct effect on the β-receptor and on the adenylate cyclase moiety. It is concluded that the cationized ferritin-induced inhibition of the hormone-dependent cyclase activity results from the inhibition of the lateral mobility of the receptor and therefore a decrease in the bimolecular rate of interaction between the receptor and the enzyme.

KW - (Erythrocyte membrane)

KW - Adenylate cyclase activation

KW - Ferritin

KW - β-Receptor

UR - https://www.scopus.com/pages/publications/0018821309

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JO - Biochimica et Biophysica Acta - Biomembranes

JF - Biochimica et Biophysica Acta - Biomembranes

IS - 1

ER -

Lateral mobility of β-receptors involved in adenylate cyclase activation

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