Photoaffinity labeling of plasma membrane receptors for aldosterone from human mononuclear leukocytes.
Non-genomic effects of aldosterone on the sodium-proton-antiport have been shown in human mononuclear leukocytes which could be related to a new aldosterone membrane receptor. In the present paper plasma membranes from human mononuclear leukocytes were covalently photolabeled with a [125I]-aldosterone derivative. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed significant aldosterone binding at a molecular weight of approximately 50000 Dalton which was absent with 1 microM cold aldosterone, but not cortisol in the binding media. The presence of the sulfhydryl agent dithiothreitol did not affect results suggesting the absence of disulfide bridges in the steroid binding domain of the receptor. These data are the first to define the molecular weight of the membrane receptor for aldosterone.
Wehling
M
M
Medizinische Klinik, Klinikum Innenstadt, University of Munich, Germany.
Eisen
C
C
Aktas
J
J
Christ
M
M
Theisen
K
K
D000345:Affinity Labels / Q000378:metabolism; D000450:Aldosterone / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D004229:Dithiothreitol / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007457:Iodine Radioisotopes; D007963:Leukocytes, Mononuclear / Q000378:metabolism*; D008970:Molecular Weight; D018161:Receptors, Mineralocorticoid / Q000187:drug effects / Q000302:isolation & purification / Q000378:metabolism*
D000345:Affinity Labels; D007457:Iodine Radioisotopes; D018161:Receptors, Mineralocorticoid; D000450:Aldosterone; D004229:Dithiothreitol