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Cellular redistribution of β‐adrenergic receptors in a human astrocytoma cell line: A comparison with the epidermal growth factor receptor in murine fibroblasts
Author(s) -
Wakshull E.,
Hertel C.,
O'Keefe E. J.,
Perkins J. P.
Publication year - 1985
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240290208
Subject(s) - endocytosis , receptor , epidermal growth factor , biology , microbiology and biotechnology , agonist , cell surface receptor , concanavalin a , biophysics , chemistry , biochemistry , in vitro
The redistribution of β‐adrenergic receptors (β‐AR) during agonist‐induced desensitization has been compared to the process of receptor‐mediated endocytosis of epidermal growth factor (EGF) in human astrocytoma cells (1321N1). [ 125 I]EGF exhibited saturable binding to high affinity (K D = 1–2 nM) receptor sites on intact 1321Nl cells. [ 125 I]EGF was found to internalize rapidly using an acid wash technique to remove surface bound hormone. Sucrose density gradient fractionation following exposure to EGF revealed a redistribution of EGF binding sites from high density (heavy peak) to low density (light peak) regions of the gradient. The light peak binding probably represents EGF in internalized vesicles formed during endocytosis. Low temperature (4 °C) or the presence of the lectin concanavalin A (con A) inhibited this ligand‐induced movement of EGF receptors. When cells were incubated simultaneously with EGF and the β‐AR agonist isoproterenol, both receptors were found to co‐migrate in the low density regions of sucrose gradients. No evidence of heterologous ligand‐induced receptor endocytosis was found. These results suggest that the EGF receptors and β‐AR are processed in parallel by 1321N1 cells.