Oestrogen-mediated tyrosine phosphorylation of caveolin-1 and its effect on the oestrogen receptor localisation: An in vivo study

Kiss, Anna L.; Turi, Ágnes; Müllner, Nándor; Kovács, Enikő; Botos, Erzsébet; Greger, Anikó

doi:10.1016/j.mce.2005.11.005

Cited by 29 publications

(24 citation statements)

References 55 publications

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“…In the present study, we demonstrate that ER-positive normal breast luminal epithelial cells express negligible levels of caveolin 2 and that, in breast cancer, caveolin 2 expression is inversely correlated with the expression of ER. Our findings support the idea that the ER signalling inhibits the expression of caveolin 1 and 2 in normal smooth muscle cells and breast cancer cells [48][49][50]. The study by Razandi et al [48] demonstrated, in cell line experiments, that ER associates with caveolin proteins in the plasma membrane and that oestrogen can modulate this association depending on the cellular context.…”

Section: Discussionsupporting

confidence: 91%

Distribution and significance of caveolin 2 expression in normal breast and invasive breast cancer: an immunofluorescence and immunohistochemical analysis

Savage

Leung

Todd

et al. 2007

Breast Cancer Res Treat

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Section: Discussionsupporting

confidence: 91%

Distribution and significance of caveolin 2 expression in normal breast and invasive breast cancer: an immunofluorescence and immunohistochemical analysis

Savage

Leung

Todd

et al. 2007

Breast Cancer Res Treat

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“…Src-mediated in vitro phosphorylation of endogenous caveolin-1 on tyrosine 14 also has been demonstrated in NIH 3T3 cells, after stimulation with a variety of cellular stressors (i.e. high osmolarity, H 2 O 2 and UV light) (Volonte et al, 2001), in v-Src transformed NIH 3T3 cells (Li et al, 1996) and in uterine smooth muscle cells after E 2 treatment (Kiss et al, 2005) but ours is the first report demonstrating that caveolin-1 can be rapidly phosphorylated in response to progestins. We also have demonstrated the existence of an interaction between caveolin-1 and PR by coimmunoprecipitacion studies and by immunofluorescence and confocal microscopy.…”

Section: Discussionsupporting

confidence: 56%

Progestin-induced caveolin-1 expression mediates breast cancer cell proliferation

et al. 2006

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Progestin regulation of gene expression was assessed in the progestin-dependent murine tumor line C4HD which requires MPA, a synthetic progestin, for in vivo growth and expresses high levels of progesterone receptor (PR). By using suppressive subtractive hybridization, caveolin-1 was identified as a gene whose expression was increased with in vivo MPA treatment. By Northern and Western blot analysis, we further confirmed that caveolin-1 mRNA and protein expression increased in MPA-treated tumors as compared with untreated tumors. When primary cultures of C4HD cells were treated in vitro with MPA, caveolin-1 levels also increased, effect that was abolished by pre-treatment with progestin antagonist RU486. In addition, MPA promoted strong caveolin-1 promoter transcriptional activation both in mouse and human breast cancer cells. We also showed that MPA regulation of caveolin-1 expression involved in activation of two signaling pathways: MAPK and PI-3K. Short-term MPA treatment of C4HD cells led to tyrosine phosphorylation of caveolin-1 protein, where Src was the kinase involved. Additionally, we showed that MPA-induced association of caveolin-1 and PR, which was detected by coimmunoprecipitation and by confocal microscopy. Finally, we proved that MPA-induced proliferation of C4HD cells was inhibited by suppression of caveolin-1 expression with antisense oligodeoxynucleotides to caveolin-1 mRNA. Furthermore, we observed that inhibition of caveolin-1 expression abrogated PR capacity to induced luciferase activity from a progesterone response elementdriven reporter plasmid. Comprehensively, our results demonstrated for the first time that caveolin-1 expression is upregulated by progestin in breast cancer. We also demonstrated that caveolin-1 is a downstream effector of MPA that is partially responsible for the stimulation of growth of breast cancer cells.

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“…Several recent studies have indicated that many signaling molecules, such Raf1 and Src family tyrosine kinases, are recruited into caveolae by caveolins, which, through the scaffolding domain, interact with the caveolin-binding motifs in these signal molecules (Kiss et al 2005). These groups of signal molecules can form 'preassembled signaling complexes' on the plasma membrane.…”

Section: Discussionmentioning

confidence: 99%

Association of estrogen receptor with plasma-membrane caveola components: implication in control of vitamin D receptor

Gilad

Schwartz

2007

Journal of Molecular Endocrinology

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This study was designed to provide a direct demonstration of the importance of caveolin-1 in the compartmentalization of estrogen receptor b (ERb) to the membrane, thus allowing 7b-estradiol (E2) to control vitamin D receptor (VDR) transcription and expression. Our strategy was to obtain cell lines expressing different levels of caveolin-1. To this end, we transfected human embryonic kidney 293 cells with a caveolin-1-expressing vector and obtained three cell-line variants: one expressing high amounts of caveolin-1 (clone A), one expressing low amounts of caveolin-1 (clone B), and one expressing high amounts of the nonfunctional P132L caveolin-1 mutant (clone C), and compared these with parental (wild-type, WT) cells expressing negligible levels of caveolin-1. In clone A, ERb colocalized to membrane preparations and E2 treatment induced significant ERK 1/2 phosphorylation and enhanced VDR expression. In clones B and C and the WT, ERb did not localize to membrane preparations and E2 treatment was ineffective at inducing VDR upregulation associated with ERK 1/2 phosphorylation. Luciferase reporter gene expression assays showed that the human VDR promoter is only highly responsive to E2 treatment in clone A, except in the presence of the ER-specific inhibitor ICI182 780. Cotransfection of clone A with the VDR promoter and several mutants of MAPK kinase (MEK) demonstrated that the constitutively active form of MEK significantly increases VDR promoter activation, while the catalytically inactive construct is ineffective in this regard. In clone A cells transfected with an activation protein-1 (AP-1)-luciferase construct, E2 significantly upregulated the promoter activity, while ICI182 780 completely eliminated this E2-mediated effect. Clone A cells transfected with a VDR promoter bearing a targeted mutation towards the AP-1 site showed reduced E2-mediated activation of luciferase activity. Taken together, our data confirm the importance of caveolin-1 in the association of ERb to the membrane caveolae, allowing ERK 1/2 phosphorylation and upregulation of VDR.

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Oestrogen-mediated tyrosine phosphorylation of caveolin-1 and its effect on the oestrogen receptor localisation: An in vivo study

Cited by 29 publications

References 55 publications

Distribution and significance of caveolin 2 expression in normal breast and invasive breast cancer: an immunofluorescence and immunohistochemical analysis

Distribution and significance of caveolin 2 expression in normal breast and invasive breast cancer: an immunofluorescence and immunohistochemical analysis

Progestin-induced caveolin-1 expression mediates breast cancer cell proliferation

Association of estrogen receptor with plasma-membrane caveola components: implication in control of vitamin D receptor

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