Oxytocin-Stimulated Myosin Phosphorylation in Mammary Myoepithelial Cells: Roles of Calcium Ions and Cyclic Nucleotides*

Olins, Gillian M.; Bremel, Robert D.

doi:10.1210/endo-114-5-1617

Cited by 37 publications

(20 citation statements)

References 31 publications

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“…Olins and Bremel [11] have shown that OT exerts a double action on target cells: it activates contraction through myosin phosphorylation, and causes an increase in cytoplasmic cAMP [11]. However, while cell contraction is stimulated by OT concentrations in the range of 10 -9 M, the level of intracytoplasmic cAMP is only affected by OT concentrations in the range of 10 -8 or 10 -7 M or higher [20].…”

Section: Discussionmentioning

confidence: 99%

Oxytocin inhibits proliferation of human breast cancer cell lines

Cassoni

Sapino

Negro

et al. 1994

Vichows Archiv A Pathol Anat

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In this study we show that treatment of MDA-MB231 hormone-independent human breast cancer cells with oxytocin (OT) or with the OT analogue F314 induces significant growth inhibition together with a change in cell phenotype. In MCF7 and T47D human breast cancer cells, OT inhibits oestrogen-induced cell growth. In these same cells, OT administration significantly enhances the inhibitory effect of tamoxifen on cell proliferation. MDA-MB231, MCF7 and T47D cells all express mRNA specific for the OT receptor. These data suggest that it may be possible to inhibit breast cancer growth using OT and OT analogues.

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Section: Discussionmentioning

confidence: 99%

Oxytocin inhibits proliferation of human breast cancer cell lines

Cassoni

Sapino

Negro

et al. 1994

Vichows Archiv A Pathol Anat

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“…This discrepancy could be due to a variety of technical considerations (Arturi et al 2005). The oxytocin receptor is present in 50-90% of breast cancers (Bussolati et al 1996, Ito et al 1996, Sapino et al 1998 and is a G protein-coupled receptor capable of activating the G s -cAMP-protein kinase A (PKA) pathway (Olins & Bremel 1984) (Fig. 2).…”

Section: Nis Regulation In Breast Cancermentioning

confidence: 99%

Iodide transport and breast cancer

Poole¹,

McCabe²

2015

Journal of Endocrinology

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Breast cancer is the second most common cancer worldwide and the leading cause of cancer death in women, with incidence rates that continue to rise. The heterogeneity of the disease makes breast cancer exceptionally difficult to treat, particularly for those patients with triple-negative disease. To address the therapeutic complexity of these tumours, new strategies for diagnosis and treatment are urgently required. The ability of lactating and malignant breast cells to uptake and transport iodide has led to the hypothesis that radioiodide therapy could be a potentially viable treatment for many breast cancer patients. Understanding how iodide is transported, and the factors regulating the expression and function of the proteins responsible for iodide transport, is critical for translating this hypothesis into reality. This review covers the three known iodide transporters -the sodium iodide symporter, pendrin and the sodium-coupled monocarboxylate transporter -and their role in iodide transport in breast cells, along with efforts to manipulate them to increase the potential for radioiodide therapy as a treatment for breast cancer.

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“…The mode of contraction in myoepithelial cells involves an increase in [Ca 2+ ] i , and the subsequent activation of Ca 2+ -calmodulin-regulated myosin light chain kinase [32,33]. We previously demonstrated that oxytocin and ATP increase [Ca 2+ ] i and stimulate contraction in cultured mouse mammary myoepithelial cells [30].…”

Section: Introductionmentioning

confidence: 99%

Synergistic effects of ATP on oxytocin-induced intracellular Ca2+ response in mouse mammary myoepithelial cells

Nakano¹,

Furuya

Yamagishi

2001

Pflügers Arch - Eur J Physiol

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An increase in intracellular Ca2+ ([Ca2+]i) is essential for mammary myoepithelial cells to contract, leading to milk ejection during lactation. In this study, the intracellular signaling leading to the increase in [Ca2+]i in cultured myoepithelial cells from mouse lactating mammary glands was investigated using fura-2 fluorescence ratiometry. [Ca2+]i increased in cultured myoepithelial cells in response to either oxytocin (1 nM) or ATP (10 microM), and the cells then contracted. These [Ca2+]i responses were diminished by treatment with an inhibitor of phospholipase C (> or = 1 microM U73122). Intracellular application of inositol 1,4,5-trisphosphate (IP3: 10 or 100 microM) increased [Ca2+]i. Pretreatment with pertussis toxin (PTX: 0.1 or 1 microgram/ml) inhibited the [Ca2+]i response to ATP, but had less of an effect on the response to oxytocin. These results indicate that oxytocin and purinergic receptors are coupled to PTX-insensitive and PTX-sensitive G proteins, respectively, and that their activation leads to the increase in [Ca2+]i through the release of Ca2+ from IP3-sensitive intracellular stores via the inositol-phospholipid signaling pathway. Furthermore, we found that the [Ca2+]i responses to oxytocin at physiological doses (0.01-0.1 nM) were augmented in the presence of a sub-responsive dose of ATP (1 microM). The activation of purinergic receptors may facilitate myoepithelial cell contraction in milk-ejection responses.

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Oxytocin-Stimulated Myosin Phosphorylation in Mammary Myoepithelial Cells: Roles of Calcium Ions and Cyclic Nucleotides*

Cited by 37 publications

References 31 publications

Oxytocin inhibits proliferation of human breast cancer cell lines

Oxytocin inhibits proliferation of human breast cancer cell lines

Iodide transport and breast cancer

Synergistic effects of ATP on oxytocin-induced intracellular Ca2+ response in mouse mammary myoepithelial cells

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