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Induction of prostacyclin receptor expression in human erythroleukemia cells
Author(s) -
Murray Rosemary,
Furci Lucinda,
FitzGerald Garret A.
Publication year - 1989
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(89)81084-1
Subject(s) - prostacyclin , cyclase , receptor , adenylate kinase , iloprost , gtp' , stimulation , chemistry , endocrinology , medicine , microbiology and biotechnology , biochemistry , biology , enzyme
We have identified both high‐affinity (K D = 36±3 nM) and low‐affinity (K D = 2.1±0.8 μM) prostacyclin (PGI 2 )‐receptor sites on human erythroleukemia (HEL) cells using the radiolabelled prostacyclin analogue, [ 3 H]iloprost. The addition of the phorbol ester, TPA, to the culture medium caused a 5–10‐fold increase in the number of both the low‐ and the high‐affinity sites, without any change in their affinity constants. Iloprost stimulated HEL cell membrane adenylate cyclase activity 5‐fold. This stimulation was potentiated in the presence of GTP, indicating a conventional PGI 2 receptor‐G s ‐adenylate cyclase system. HEL cells represent a source of prostacyclin receptor mRNA which may be of value in expression cloning of this receptor.