Biophysical parameters of glucocorticoid-binding proteins from rat inflammatory tissues.
The complexes of [3H]glucocorticoid and cytoplasmic proteins of the inflammatory tissue were characterized by the gel filtration and by the sucrose density gradient centrifugation. Protein-bound [3H]cortisol sedimented at about 4 S with a Stokes radius of about 4 nm and an apparent molecular weight (Mr) of about 70 kDa, irrespective with the presence of 0.4 M KCl. The complex of [3H]triamcinolone acetonide (TAA) and protein sedimented at about 7 S and showed about 170 kDa of Mr and about 6 nm of the Stokes radius in the absence of 0.4 M KCl. In the presence of 0.4 M KCl, the [3H]TAA-protein complex changed into a smaller form (4 S) with about 4 nm of the Stokes radius and about 60 kDa of Mr. This suggests that the so-called glucocorticoid receptor of the inflammatory tissue associates with a 110 kDa protein.
Endo
Y
Y
Department of Pharmacotherapeutics, Hokkaido Institute of Pharmaceutical Sciences, Japan.
Fujihira
E
E
D000818:Animals; D002351:Carrageenan; D002499:Centrifugation, Density Gradient; D002850:Chromatography, Gel; D006099:Granuloma / Q000139:chemically induced; D006854:Hydrocortisone / Q000378:metabolism; D007249:Inflammation / Q000139:chemically induced / Q000378:metabolism*; D008297:Male; D008970:Molecular Weight; D051381:Rats; D017207:Rats, Sprague-Dawley; D011965:Receptors, Glucocorticoid / Q000737:chemistry* / Q000378:metabolism
D011965:Receptors, Glucocorticoid; D002351:Carrageenan; D006854:Hydrocortisone