Mid-region parathyroid hormone-related protein (PTHrP) and gene expression of MDA-MB231 breast cancer cells

2007 ◽  
Vol 388 (5) ◽  
Author(s):  
Rosalia Sirchia ◽  
Claudio Luparello
Keyword(s):  
Breast Cancer ◽  
Gene Expression ◽  
Parathyroid Hormone ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Related Protein ◽  
Parathyroid Hormone Related Protein

scholarly journals Parathyroid Hormone-related Protein Regulates Tumor-relevant Genes in Breast Cancer Cells

2006 ◽  
Vol 281 (21) ◽  
pp. 14563-14572 ◽  
Author(s):  
Angela Dittmer ◽  
Martina Vetter ◽  
Dario Schunke ◽  
Paul N. Span ◽  
Fred Sweep ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Parathyroid Hormone ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Related Protein ◽  
Parathyroid Hormone Related Protein

Mid-region parathyroid hormone-related protein (PTHrP) binds chromatin of MDA-MB231 breast cancer cells and isolated oligonucleotides “in vitro”

2006 ◽  
Vol 105 (1) ◽  
pp. 105-116 ◽  
Author(s):  
Rosalia Sirchia ◽  
Marcella Priulla ◽  
Giulia Sciandrello ◽  
Fabio Caradonna ◽  
Giuseppa Barbata ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Parathyroid Hormone ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Related Protein ◽  
Parathyroid Hormone Related Protein

scholarly journals Mammary gland serotonin regulates parathyroid hormone-related protein and other bone-related signals

2012 ◽  
Vol 302 (8) ◽  
pp. E1009-E1015 ◽  
Author(s):  
Laura L. Hernandez ◽  
Karen A. Gregerson ◽  
Nelson D. Horseman
Keyword(s):  
Breast Cancer ◽  
Mammary Gland ◽  
Parathyroid Hormone ◽  
Epithelial Cells ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Related Protein ◽  
Bone Demineralization ◽  
Parathyroid Hormone Related Protein ◽  
Pthrp Expression

Breast cells drive bone demineralization during lactation and metastatic cancers. A shared mechanism among these physiological and pathological states is endocrine secretion of parathyroid hormone-related protein (PTHrP), which acts through osteoblasts to stimulate osteoclastic bone demineralization. The regulation of PTHrP has not been accounted for fully by any conventional mammotropic stimuli or tumor growth factors. Serotonin (5-HT) synthesis within breast epithelial cells is induced during lactation and in advancing breast cancer. Here we report that serotonin deficiency (knockout of tryptophan hydroxylase-1) results in a reduction of mammary PTHrP expression during lactation, which is rescued by restoring 5-HT synthesis. 5-HT induced PTHrP expression in lactogen-primed mammary epithelial cells from either mouse or cow. In human breast cancer cells 5-HT induced both PTHrP and the metastasis-associated transcription factor Runx2/Cbfa1. Based on receptor expression and pharmacological evidence, the 5-HT2 receptor type was implicated as being critical for induction of PTHrP and Runx2. These results connect 5-HT synthesis to the induction of bone-regulating factors in the normal mammary gland and in breast cancer cells.

scholarly journals Ets2 and protein kinase Cepsilon are important regulators of parathyroid hormone-related protein expression in MCF-7 breast cancer cells

2003 ◽  
Vol 372 (3) ◽  
pp. 787-797 ◽  
Author(s):  
Ralph K. LINDEMANN ◽  
Melanie BRAIG ◽  
Craig A. HAUSER ◽  
Alfred NORDHEIM ◽  
Jürgen DITTMER
Keyword(s):  
Breast Cancer ◽  
Protein Kinase ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Related Protein ◽  
Parathyroid Hormone Related Protein ◽  
Pthrp Expression ◽  
Mcf 7

Parathyroid hormone-related protein (PTHrP) promotes the metastatic potential and proliferation of breast cancer cells, and acts anti-apoptotically. In invasive MDA-MB-231 breast cancer cells, transforming growth factor β-regulated PTHrP synthesis is mediated by an Ets1/Smad3-dependent activation of the PTHrP P3 promoter. In the present study, we studied the regulation of PTHrP expression in non-invasive, Ets1-deficient and transforming growth factor β-resistant MCF-7 cells. We found PMA to be a strong stimulator of P3-dependent PTHrP expression in MCF-7 cells. Mitogen-activated protein kinase (MAPK)/extracellular-signal-regulated kinase (ERK) kinase 1 (MEK-1)/ERK1/2 inhibitor PD98059 interfered with this activity. Promoter studies revealed that the PMA effect depended on the Ets and stimulating protein-1 (Sp1)-binding sites. Of several Ets factors tested, Ets2, but not Ese-1, Elf-1 or Ets1, supported the PMA-dependent increase in promoter activity. PD98059 and a threonine to alanine mutation of the ERK1/2-responsive Ets2 phosphorylation site at position 72 inhibited the Ets2/PMA effect. Activated protein kinase C (PKC)ε could mimic PMA by stimulating the P3 promoter alone or in co-operation with Ets2 in an MEK-1/ERK1/2-dependent manner. Activated PKCα, although capable of co-operating with Ets2, failed to induce transcription from the P3 promoter on its own. The Ets2/PKCα synergistic effect was neither sensitive to PD98059 nor to Thr72/Ala72 mutation. PMA neither increased the expression of Sp1 nor modulated the transcriptional activity of Sp1. However, it induced the displacement of a yet unknown factor from the Sp1-binding site, which may result in Sp1 recruitment to the promoter. Our results suggest an ERK1/2-dependent Ets2/PKCε synergism to be involved in PTHrP expression in MCF-7 breast cancer cells.

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