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Human oestrogen receptors: differential expression of ERalpha and beta and the identification of ERbeta variants

Steroids, ISSN: 0039-128X, Vol: 67, Issue: 12, Page: 985-992
2002
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Article Description

Two structurally related subtypes of oestrogen receptor (ER), known as alpha (ERα, NR3A1) and beta (ERβ, NR3A2) have been identified. ERβ mRNA and protein have been detected in a wide range of tissues including the vasculature, bone, and gonads in both males and females, as well as in cancers of the breast and prostate. In many tissues the pattern of expression of ERβ is distinct from that of ERα. A number of variant isoforms of the wild type beta receptor (ERβ1), have been identified. In the human these include: (1) use of alternative start sites within the mRNA leading to translation of either a long (530 amino acids, hERβ1L) or a truncated form (487aa hERβ1s); (2) deletion of exons by alternative splicing; (3) formation of several isoforms (ERβ2-β5) due to alternative splicing of exons encoding the carboxy terminus (F domain). We have raised monoclonal antibodies specific for hERβ1 as well as to three of the C terminal isoforms (β2, β4 and β5). Using these antibodies we have found that ERβ2, β4 and β5 proteins are expressed in nuclei of human tissues including the ovary, placenta, testis and vas deferens.

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