Premium
Glucocorticoid Receptors in Human Polymorphonuclear and Mononuclear Leucocytes
Author(s) -
Kontula K.,
Myllylä G.,
Andersson Leif C.
Publication year - 1981
Publication title -
scandinavian journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.904
H-Index - 84
eISSN - 1600-0609
pISSN - 0036-553X
DOI - 10.1111/j.1600-0609.1981.tb00465.x
Subject(s) - glucocorticoid receptor , receptor , glucocorticoid , endocrinology , steroid , medicine , dexamethasone , steroid hormone , peripheral blood mononuclear cell , dissociation constant , aldosterone , transcortin , mineralocorticoid , biology , chemistry , hormone , in vitro , biochemistry , globulin
Both polymorphonuclear (PMN) and mononuclear (MN) leucocytes constitute targets for glucocorticoid hormones. In order to comparatively characterize the earliest steps of steroid action in these cell populations, we investigated the concentrations and specificities of glucocorticoid receptors in purified human PMNs and MNs by a whole‐cell binding assay using ( 3 H)dexamethasone as the ligand. PMNs and MNs were found to contain the same amounts of glucocorticoid receptors (4720 and 4900 receptor sites/cell, respectively). The equilibrium dissociation constant (K d ) of the interaction between the cellular receptor and ( 3 H)dexamethasone was about the same (1 times 10 ‐8 M) in both cell populations. No significant differences in the specificities of the steroid binding sites in PMNs and MNs were found; competition studies revealed the following order of relative binding affinities for a number of compounds: betamethasone > dexamethasone > prednisolone > cortisol > deoxycortico‐sterone = progesterone > aldosterone > testosterone > estradiol‐17β. We conclude that known differences in the sensitivities of PMNs and MNs to glucocorticoids are apparently not caused by differences in the concentrations or characteristics of their glucocorticoid receptors.