Protein expression of the transcriptional regulator MI-ER1 alpha in adult mouse tissues

Thorne, Leanne B.; McCarthy, Patti; Paterno, Gary D.; Gillespie, Laura L.

doi:10.1007/s10735-007-9116-3

Cited by 4 publications

(10 citation statements)

References 23 publications

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“…The control peptide, on the other hand, did not affect antibody binding, and the staining was similar to that obtained with the anti-MI-ER1a IgG alone. Additional positive and negative controls included sections of normal human adrenal cortex and small intestine, respectively; previously, we reported positive staining in the murine adrenal gland, whereas most areas of the small intestine were negative (Thorne et al, 2008). As can be seen in Figure 3E and F, staining of the human tissues was similar to that seen in the mouse, with intense staining of the adrenal cortex and no immunoreactivity in the ileum.…”

Section: Immunohistochemical Analysis Of Mi-er1a In Normal Breast Andsupporting

confidence: 58%

“…The MI-ER1a antibody is a rabbit polyclonal antibody directed against a synthetic peptide representing alpha-specific sequence (amino acids 413 -426); its production has been described and its specificity has been determined previously (Paterno et al, 2002;Thorne et al, 2008). Purified IgG was prepared from pre-immune or immune serum using the Melon Gel IgG purification kit (Pierce, Rockford, IL, USA) according to the manufacturer's instructions.…”

Section: Antibodiesmentioning

confidence: 99%

“…Immunohistochemistry and preabsorption with peptide was performed as described previously (Thorne et al, 2008) using the Universal LSAB þ -HRP kit (Dako, Denmark) and 1.25 mg ml À1 of anti-MI-ER1a IgG or pre-immune IgG. Antigen retrieval was performed in 10 mM sodium citrate, pH 6.0, in a 95 1C water bath.…”

Section: Tissue Microarrays Whole Tissue Sections and Immunohistochementioning

confidence: 99%

“…The MI-ER1a antibody used in this study has been well characterised and shown to be specific for the MI-ER1a protein (Paterno et al, 2002;Thorne et al, 2008). For this study, we used purified anti-MI-ER1a IgG and performed initial tests to confirm the specificity of antibody staining on paraffin sections of human tissue.…”

Section: Immunohistochemical Analysis Of Mi-er1a In Normal Breast Andmentioning

confidence: 99%

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Changes in subcellular localisation of MI-ER1α, a novel oestrogen receptor-α interacting protein, is associated with breast cancer progression

et al. 2008

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The oestrogen receptor-a (ERa) plays a key role in breast development and tumorigenesis and inhibiting its activity remains a prime strategy in the treatment of ERa-positive breast cancers. Thus, elucidation of the molecular mechanisms responsible for regulating ERa activity may facilitate the design of new, more effective breast cancer therapies. The MI-ER1a is a novel transcriptional repressor that contains an LXXLL motif for interaction with nuclear hormone receptors. We investigated the ability of MI-ER1a to bind to ERa in HEK293 and MCF-7 breast carcinoma cells, using co-immunoprecipitation assays. In both cell lines, MI-ER1a interacted with ERa in the presence and absence of oestrogen, but the interaction was stronger in the absence of ligand. Functional analysis revealed that overexpression of MI-ER1a in T47D breast carcinoma cells results in inhibition of oestrogen-stimulated anchorage-independent growth, suggesting that MI-ER1a may play a role in regulating breast carcinoma cell proliferation in vivo. To explore this further, we performed an immunohistochemical analysis of normal breast tissue and breast carcinoma; a total of 110 cases were examined in whole tissue sections and 771 cases were analysed in tissue microarrays. No consistent difference in the MI-ER1a expression level between normal breast tissue and breast carcinoma was discernible. However, there was a dramatic shift in the subcellular localisation: nuclear MI-ER1a was detectable in 75% of normal breast samples and in 77% of hyperplasia, but in breast carcinoma, only 51% of DCIS, 25% of ILC and 4% of IDC contained nuclear staining. This shift from nuclear to cytoplasmic localisation of MI-ER1a during breast cancer progression suggests that loss of nuclear MI-ER1a might contribute to the development of invasive breast carcinoma.

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Section: Immunohistochemical Analysis Of Mi-er1a In Normal Breast Andsupporting

confidence: 58%

Section: Antibodiesmentioning

confidence: 99%

Section: Tissue Microarrays Whole Tissue Sections and Immunohistochementioning

confidence: 99%

Section: Immunohistochemical Analysis Of Mi-er1a In Normal Breast Andmentioning

confidence: 99%

See 2 more Smart Citations

Changes in subcellular localisation of MI-ER1α, a novel oestrogen receptor-α interacting protein, is associated with breast cancer progression

et al. 2008

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“…Its specificity for detecting MIER1α protein in paraffin-embedded tissue sections has been described previously Thorne et al 2008). Briefly, the immunohistochemical specificity was tested by pre-incubation of the MIER1α IgG for half an hour with 0.1 μg of the alpha peptide used to generate the antibody or with 0.1 μg of an unrelated peptide (control peptide), prior to application to the sections.…”

Section: Antibody and Tissue Sectionsmentioning

confidence: 99%

Protein expression pattern of human MIER1 alpha, a novel estrogen receptor binding protein

2013

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MIER1 is a transcriptional regulator that exists as several isoforms. Of particular interest is the MIER1α isoform, which contains in its unique C-terminus an LXXLL motif for interaction with nuclear hormone receptors. Indeed, MIER1α has been shown to interact with ERα and inhibit estrogen-stimulated growth of breast carcinoma cells. Moreover, the subcellular localization of MIER1α changes dramatically, from nuclear to cytoplasmic, during progression to invasive breast carcinoma. While human MIER1 RNA and protein expression pattern data have been posted on several websites, none of these studies use probes or antibodies that distinguish between the α and β isoforms. We report here the first immunohistochemical study of the MIER1α protein expression pattern in human tissues. Our analysis revealed intense staining of specific cell types within virtually every endocrine and reproductive tissue except for the thyroid gland. In particular, we detected intense staining of ovarian follicles and germinal epithelium, ductal epithelial cells of the breast, pancreatic islet cells, all areas of the anterior pituitary and all zones of the adrenal cortex; moderate staining of germ cells and Leydig cells within the testis, patches of chromaffin cells in the adrenal medulla and weak staining of the fibromuscular stroma within the prostate. Immunoreactivity was limited to the cytoplasm in all positive cells except for oocytes and germinal epithelial cells in which the nucleus was also stained and in ductal epithelial cells of the breast in which staining was exclusively nuclear. In general, non-endocrine tissues were negative, however a few exceptions were noted. These included hepatocytes, myocardial fibers and neurons in all regions of the brain examined, with the exception of the thalamus. Neuronal staining was restricted to the cell bodies and dendrites, as most axons were negative. These data suggest that human MIER1α functions specifically in endocrine tissues and in a limited number of nonendocrine organs.

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MIER3 induces epithelial-mesenchymal transition and promotes breast cancer cell aggressiveness via forming a co-repressor complex with HDAC1/HDAC2/Snail

Huang

Chen

Liu

et al. 2021

Experimental Cell Research

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Protein expression of the transcriptional regulator MI-ER1 alpha in adult mouse tissues

Cited by 4 publications

References 23 publications

Changes in subcellular localisation of MI-ER1α, a novel oestrogen receptor-α interacting protein, is associated with breast cancer progression

Changes in subcellular localisation of MI-ER1α, a novel oestrogen receptor-α interacting protein, is associated with breast cancer progression

Protein expression pattern of human MIER1 alpha, a novel estrogen receptor binding protein

MIER3 induces epithelial-mesenchymal transition and promotes breast cancer cell aggressiveness via forming a co-repressor complex with HDAC1/HDAC2/Snail

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