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ERβ: Identification and characterization of a novel human estrogen receptor
Author(s) -
Mosselman Sietse,
Polman Jan,
Dijkema Rein
Publication year - 1996
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(96)00782-x
Subject(s) - transactivation , beta (programming language) , microbiology and biotechnology , estrogen receptor , estrogen receptor beta , estrogen receptor alpha , chinese hamster ovary cell , hormone response element , western blot , biology , alpha (finance) , chemistry , receptor , endocrinology , gene expression , biochemistry , gene , genetics , medicine , cancer , breast cancer , construct validity , nursing , computer science , patient satisfaction , programming language
A novel estrogen receptor (hereinafter referred to as ERβ) was cloned using degenerate PCR primers. A comparison of the amino acid sequence of ERβ with the ‘classical’ ER (ERα) shows a high degree of conservation of the DNA‐binding domain (96%), and of the ligand‐binding domain (58%). In contrast, the A/B domain, the hinge region and the F‐domain are not conserved. Northern blot analysis revealed that ERβ is expressed in human thymus, spleen, ovary and testis. Transient transfections of an ERβ expression construct together with an ERE‐based reporter construct in CHO cells clearly demonstrated transactivation of ERβ by 17β‐estradiol. In addition, the ERα antagonist ICI‐164384 is a potent antagonist for ERβ as well. Interestingly, the level of transactivation by 17β‐estradiol is higher for ERα than for ERβ, which may reflect suboptimal conditions for ERβ at the level of the ligand, responsive element or cellular context.