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Evidence for two structurally related progesterone receptors in chick oviduct cytosol
Author(s) -
Gronemeyer Hinrich,
Harry Paula,
Chambon Pierre
Publication year - 1983
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(83)80514-6
Subject(s) - oviduct , receptor , proteolysis , cytosol , progesterone receptor , peptide , chymotrypsin , photoaffinity labeling , steroid hormone , glucocorticoid receptor , biology , endocrinology , trypsin , medicine , biochemistry , steroid , transcortin , chemistry , hormone , enzyme , estrogen receptor , globulin , cancer , breast cancer
The existence of two progesterone receptor forms present in crude cytosol of chick oviduct has been demonstrated by photoaffinity labelling using [ 3 H]R5020. On SDS—polyacrylamide gels these two forms exhibit app. M r ‐values of 79 000 and 109 000 corresponding to the progesterone receptor forms A and B. Peptide maps of photoaffinity‐labelled steroid receptors have been established by limited proteolysis with α‐chymotrypsin. The peptide map obtained for chick oviduct cytosol progesterone receptor crosslinked with [ 3 H]R5020 proved to be the sum of peptides obtained from partially purified preparations of forms A and B. The peptide maps of both progesterone receptor forms were identical for peptides below the M r ‐value of form A, indicating extensive homology of the two forms. A significantly different peptide pattern was observed for the rat liver glucocorticoid receptor crosslinked with [ 3 H]triamcinolone acetonide. Prolonged proteolysis with chymotrypsin gave rise to peptides with M r ‐values of 6000 and 10 000 from the hormone‐binding domain of progesterone and glucocorticoid receptors, respectively.