High affinity binding of reovirus type 3 to cells that lack beta adrenergic receptor activity

David G. Sawutz, Rhonda Bassel-Duby, Charles J. Homcy

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

A previous report demonstrated both immunological crossreactivity and structural similarity between the mammalian beta adrenergic receptor and the cell surface receptor for the reovirus type 3 (14). We now demonstrate that reovirus type 3 can bind selectively and with high affinity to cells that lack beta adrenergic receptor activity (L-cells). The present study was also designed to determine what effect reovirus binding has on beta adrenergic receptor function in cells (DDT1) that possess an intact ligand binding site. Based on computer analysis of reovirus competitive inhibition curves, the apparent dissociation binding constants (Kd) for reovirus binding to DDT1 and L-cells are 0.1 nM and 0.25 nM, respectively. High affinity [125I]-iodocyanopindolol (CYP) binding to beta adrenergic receptors can also be demonstrated in DDT1 cells but not in L-cells. In agreement with these ligand binding studies, adenylate cyclase activity is stimulated by the beta receptor agonist isoproterenol in DDT1 cell membranes but not in L-cell membranes. In addition, isoproterenol increases cAMP levels in DDT1 cells but not in L-cells. Neither reovirus serotype stimulates cAMP levels in either cell line, nor do they influence beta-adrenergic agonist stimulation of cAMP in DDT1 cells. These results argue against identity of the receptors for reovirus type 3 and beta adrenergic ligands.

Original languageEnglish (US)
Pages (from-to)399-406
Number of pages8
JournalLife Sciences
Volume40
Issue number4
DOIs
StatePublished - Jan 26 1987

Fingerprint

Mammalian orthoreovirus 3
Receptors, Adrenergic, beta
Cell membranes
Ligands
Isoproterenol
Iodocyanopindolol
Adrenergic beta-Agonists
Cell Surface Receptors
Adenylyl Cyclases
Adrenergic Agents
Adrenergic beta-3 Receptors
Binding Sites
Cells
Cell Membrane

ASJC Scopus subject areas

  • Pharmacology

Cite this

High affinity binding of reovirus type 3 to cells that lack beta adrenergic receptor activity. / Sawutz, David G.; Bassel-Duby, Rhonda; Homcy, Charles J.

In: Life Sciences, Vol. 40, No. 4, 26.01.1987, p. 399-406.

Research output: Contribution to journalArticle

@article{9988c9ccf1454e789695d60581465101,
title = "High affinity binding of reovirus type 3 to cells that lack beta adrenergic receptor activity",
abstract = "A previous report demonstrated both immunological crossreactivity and structural similarity between the mammalian beta adrenergic receptor and the cell surface receptor for the reovirus type 3 (14). We now demonstrate that reovirus type 3 can bind selectively and with high affinity to cells that lack beta adrenergic receptor activity (L-cells). The present study was also designed to determine what effect reovirus binding has on beta adrenergic receptor function in cells (DDT1) that possess an intact ligand binding site. Based on computer analysis of reovirus competitive inhibition curves, the apparent dissociation binding constants (Kd) for reovirus binding to DDT1 and L-cells are 0.1 nM and 0.25 nM, respectively. High affinity [125I]-iodocyanopindolol (CYP) binding to beta adrenergic receptors can also be demonstrated in DDT1 cells but not in L-cells. In agreement with these ligand binding studies, adenylate cyclase activity is stimulated by the beta receptor agonist isoproterenol in DDT1 cell membranes but not in L-cell membranes. In addition, isoproterenol increases cAMP levels in DDT1 cells but not in L-cells. Neither reovirus serotype stimulates cAMP levels in either cell line, nor do they influence beta-adrenergic agonist stimulation of cAMP in DDT1 cells. These results argue against identity of the receptors for reovirus type 3 and beta adrenergic ligands.",
author = "Sawutz, {David G.} and Rhonda Bassel-Duby and Homcy, {Charles J.}",
year = "1987",
month = "1",
day = "26",
doi = "10.1016/0024-3205(87)90142-1",
language = "English (US)",
volume = "40",
pages = "399--406",
journal = "Life Sciences",
issn = "0024-3205",
publisher = "Elsevier Inc.",
number = "4",

}

TY - JOUR

T1 - High affinity binding of reovirus type 3 to cells that lack beta adrenergic receptor activity

AU - Sawutz, David G.

AU - Bassel-Duby, Rhonda

AU - Homcy, Charles J.

PY - 1987/1/26

Y1 - 1987/1/26

N2 - A previous report demonstrated both immunological crossreactivity and structural similarity between the mammalian beta adrenergic receptor and the cell surface receptor for the reovirus type 3 (14). We now demonstrate that reovirus type 3 can bind selectively and with high affinity to cells that lack beta adrenergic receptor activity (L-cells). The present study was also designed to determine what effect reovirus binding has on beta adrenergic receptor function in cells (DDT1) that possess an intact ligand binding site. Based on computer analysis of reovirus competitive inhibition curves, the apparent dissociation binding constants (Kd) for reovirus binding to DDT1 and L-cells are 0.1 nM and 0.25 nM, respectively. High affinity [125I]-iodocyanopindolol (CYP) binding to beta adrenergic receptors can also be demonstrated in DDT1 cells but not in L-cells. In agreement with these ligand binding studies, adenylate cyclase activity is stimulated by the beta receptor agonist isoproterenol in DDT1 cell membranes but not in L-cell membranes. In addition, isoproterenol increases cAMP levels in DDT1 cells but not in L-cells. Neither reovirus serotype stimulates cAMP levels in either cell line, nor do they influence beta-adrenergic agonist stimulation of cAMP in DDT1 cells. These results argue against identity of the receptors for reovirus type 3 and beta adrenergic ligands.

AB - A previous report demonstrated both immunological crossreactivity and structural similarity between the mammalian beta adrenergic receptor and the cell surface receptor for the reovirus type 3 (14). We now demonstrate that reovirus type 3 can bind selectively and with high affinity to cells that lack beta adrenergic receptor activity (L-cells). The present study was also designed to determine what effect reovirus binding has on beta adrenergic receptor function in cells (DDT1) that possess an intact ligand binding site. Based on computer analysis of reovirus competitive inhibition curves, the apparent dissociation binding constants (Kd) for reovirus binding to DDT1 and L-cells are 0.1 nM and 0.25 nM, respectively. High affinity [125I]-iodocyanopindolol (CYP) binding to beta adrenergic receptors can also be demonstrated in DDT1 cells but not in L-cells. In agreement with these ligand binding studies, adenylate cyclase activity is stimulated by the beta receptor agonist isoproterenol in DDT1 cell membranes but not in L-cell membranes. In addition, isoproterenol increases cAMP levels in DDT1 cells but not in L-cells. Neither reovirus serotype stimulates cAMP levels in either cell line, nor do they influence beta-adrenergic agonist stimulation of cAMP in DDT1 cells. These results argue against identity of the receptors for reovirus type 3 and beta adrenergic ligands.

UR - http://www.scopus.com/inward/record.url?scp=0023665435&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023665435&partnerID=8YFLogxK

U2 - 10.1016/0024-3205(87)90142-1

DO - 10.1016/0024-3205(87)90142-1

M3 - Article

VL - 40

SP - 399

EP - 406

JO - Life Sciences

JF - Life Sciences

SN - 0024-3205

IS - 4

ER -