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Protein kinase C rapidly up‐regulates the number of AT 1 angiotensin receptors on cultured rat intestinal epithelial (RIE‐1) cells
Author(s) -
Smith Roger D.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00584-2
Subject(s) - receptor , angiotensin ii , angiotensin ii receptor type 1 , protein kinase c , angiotensin receptor , extracellular , microbiology and biotechnology , renin–angiotensin system , protein kinase a , chemistry , kinase , biology , medicine , biochemistry , endocrinology , blood pressure
Addition of 12‐ O ‐tetradecanoylphorbol‐13‐acetate to RIE‐1 rat intestinal epithelial cells stimulated a rapid (mean 3‐fold) increase in the subsequent binding of 125 I‐labelled angiotensin II which was reversed or prevented when cellular protein kinase C was depleted. The increased binding was due, in part, to an up‐regulation in the number of AT 1 angiotensin receptors on RIE‐1 cells, without any significant change in their binding affinity. Since this rapid up‐regulation was independent of receptor synthesis, it may result from an increased availability (to extracellular ligand) of preformed, but previously ‘cryptic’, AT 1 angiotensin receptors.