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Expression of oestrogen receptor beta (ERbeta1) protein in human breast cancer biopsies.

Saunders PT, Millar MR, Williams K, Macpherson S, Bayne C, O'Sullivan C, Anderson TJ, Groome NP, Miller WR - Br. J. Cancer (2002)

Bottom Line: Western blot analysis of breast tumours contained both forms of oestrogen receptor beta protein although in some samples lower molecular weight species (32--45 Kd) were identified.Expression of oestrogen receptor beta was exclusively nuclear and occurred in multiple cell types.There was no quantitative relationship between staining for the two ERs although in tumours in which both receptors were present immunoexpression of oestrogen receptor alpha was invariably more intense.

View Article: PubMed Central - PubMed

Affiliation: MRC Human Reproductive Sciences Unit, 37 Chalmers Street, Edinburgh, EH3 9ET, UK. p.saunders@ed.ac.uk

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Related in: MedlinePlus

Western analysis of proteins extracted from breast cancer samples. Proteins were separated, blotted and incubated with antibodies directed against ERα (upper panel) or ERβ (lower panel). The anti-ERα antibody bound to recombinant hERα but not to recombinant hERβ (βs, βL). The anti-ERβ1 antibody bound to both long (βL) and short (βs) forms of recombinant hERβ but not to recombinant hERα (α). Proteins migrating with the same apparent molecular size as recombinant ERα (α, upper panel, arrowhead) were detected in all breast samples (lanes 1 to 8, note identical samples were used for both gels and are loaded in the same order). In sample numbers 6 and 7 additional lower molecular weight forms of ERα were present. Variable amounts of ERβ proteins were detected in the same samples. Proteins migrating with the same apparent molecular size as both long and short forms of ERβ proteins (arrowheads) were detected in breast sample numbers 1, 3, 4, 6, 7, 8; additional lower molecular weight variants were present in these same extracts but samples 2 and 5 lacked significant levels of ERβ.
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fig2: Western analysis of proteins extracted from breast cancer samples. Proteins were separated, blotted and incubated with antibodies directed against ERα (upper panel) or ERβ (lower panel). The anti-ERα antibody bound to recombinant hERα but not to recombinant hERβ (βs, βL). The anti-ERβ1 antibody bound to both long (βL) and short (βs) forms of recombinant hERβ but not to recombinant hERα (α). Proteins migrating with the same apparent molecular size as recombinant ERα (α, upper panel, arrowhead) were detected in all breast samples (lanes 1 to 8, note identical samples were used for both gels and are loaded in the same order). In sample numbers 6 and 7 additional lower molecular weight forms of ERα were present. Variable amounts of ERβ proteins were detected in the same samples. Proteins migrating with the same apparent molecular size as both long and short forms of ERβ proteins (arrowheads) were detected in breast sample numbers 1, 3, 4, 6, 7, 8; additional lower molecular weight variants were present in these same extracts but samples 2 and 5 lacked significant levels of ERβ.

Mentions: On Western blots (Figure 2Figure 2


Expression of oestrogen receptor beta (ERbeta1) protein in human breast cancer biopsies.

Saunders PT, Millar MR, Williams K, Macpherson S, Bayne C, O'Sullivan C, Anderson TJ, Groome NP, Miller WR - Br. J. Cancer (2002)

Western analysis of proteins extracted from breast cancer samples. Proteins were separated, blotted and incubated with antibodies directed against ERα (upper panel) or ERβ (lower panel). The anti-ERα antibody bound to recombinant hERα but not to recombinant hERβ (βs, βL). The anti-ERβ1 antibody bound to both long (βL) and short (βs) forms of recombinant hERβ but not to recombinant hERα (α). Proteins migrating with the same apparent molecular size as recombinant ERα (α, upper panel, arrowhead) were detected in all breast samples (lanes 1 to 8, note identical samples were used for both gels and are loaded in the same order). In sample numbers 6 and 7 additional lower molecular weight forms of ERα were present. Variable amounts of ERβ proteins were detected in the same samples. Proteins migrating with the same apparent molecular size as both long and short forms of ERβ proteins (arrowheads) were detected in breast sample numbers 1, 3, 4, 6, 7, 8; additional lower molecular weight variants were present in these same extracts but samples 2 and 5 lacked significant levels of ERβ.
© Copyright Policy
Related In: Results  -  Collection

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getmorefigures.php?uid=PMC2375186&req=5

fig2: Western analysis of proteins extracted from breast cancer samples. Proteins were separated, blotted and incubated with antibodies directed against ERα (upper panel) or ERβ (lower panel). The anti-ERα antibody bound to recombinant hERα but not to recombinant hERβ (βs, βL). The anti-ERβ1 antibody bound to both long (βL) and short (βs) forms of recombinant hERβ but not to recombinant hERα (α). Proteins migrating with the same apparent molecular size as recombinant ERα (α, upper panel, arrowhead) were detected in all breast samples (lanes 1 to 8, note identical samples were used for both gels and are loaded in the same order). In sample numbers 6 and 7 additional lower molecular weight forms of ERα were present. Variable amounts of ERβ proteins were detected in the same samples. Proteins migrating with the same apparent molecular size as both long and short forms of ERβ proteins (arrowheads) were detected in breast sample numbers 1, 3, 4, 6, 7, 8; additional lower molecular weight variants were present in these same extracts but samples 2 and 5 lacked significant levels of ERβ.
Mentions: On Western blots (Figure 2Figure 2

Bottom Line: Western blot analysis of breast tumours contained both forms of oestrogen receptor beta protein although in some samples lower molecular weight species (32--45 Kd) were identified.Expression of oestrogen receptor beta was exclusively nuclear and occurred in multiple cell types.There was no quantitative relationship between staining for the two ERs although in tumours in which both receptors were present immunoexpression of oestrogen receptor alpha was invariably more intense.

View Article: PubMed Central - PubMed

Affiliation: MRC Human Reproductive Sciences Unit, 37 Chalmers Street, Edinburgh, EH3 9ET, UK. p.saunders@ed.ac.uk

Show MeSH
Related in: MedlinePlus