scholarly journals Expression of parathyroid hormone-related protein (PTHrP) and the PTH/PTHrP receptor in the rat uterus during early pregnancy and following artificial deciduoma induction

Reproduction ◽  
1998 ◽  
Vol 112 (1) ◽  
pp. 1-10 ◽  
Author(s):  
J. Tucci ◽  
F. Beck
Keyword(s):  
Parathyroid Hormone ◽  
Early Pregnancy ◽  
Related Protein ◽  
Rat Uterus ◽  
Parathyroid Hormone Related Protein ◽  
Pthrp Receptor

scholarly journals Nitric oxide as a second messenger in parathyroid hormone-related protein signaling

2001 ◽  
Vol 170 (2) ◽  
pp. 433-440 ◽  
Author(s):  
L Kalinowski ◽  
LW Dobrucki ◽  
T Malinski
Keyword(s):  
Nitric Oxide ◽  
Endothelial Cells ◽  
Parathyroid Hormone ◽  
Smooth Muscles ◽  
Calcium Ionophore ◽  
No Production ◽  
Related Protein ◽  
Parathyroid Hormone Related Protein ◽  
No Release ◽  
Pthrp Receptor

Parathyroid hormone (PTH)-related protein (PTHrP) is produced in smooth muscles and endothelial cells and is believed to participate in the local regulation of vascular tone. No direct evidence for the activation of endothelium-derived nitric oxide (NO) signaling pathway by PTHrP has been found despite attempts to identify it. Based on direct in situ measurements, it is reported here for the first time that the human PTH/PTHrP receptor analogs, hPTH(1--34) and hPTHrP(1--34), stimulate NO release from a single endothelial cell. A highly sensitive porphyrinic microsensor with a response time of 0.1 ms and a detection limit of 1 nmol/l was used for the measurement of NO. Both hPTH(1--34) and hPTHrP(1--34) stimulated NO release at nanomolar concentrations. The peak concentration of 0.1 micromol/l hPTH(1--34)- and 0.1 micromol/l hPTHrP(1--34)-stimulated NO release was 175+/-9 and 248+/-13 nmol/l respectively. This represents about 30%--40% of maximum NO concentration recorded in the presence of (0.1 micromol/l) calcium ionophore. Two competitive PTH/PTHrP receptor antagonists, 10 micromol/l [Leu(11),d -Trp(12)]-hPTHrP(7--34)amide and 10 micromol/l [Nle(8,18),Tyr(34)]-bPTH(3--34)amide, were equipotent in antagonizing hPTH(1--34)-stimulated NO release; [Leu(11),d -Trp(12)]-hPTHrP(7--34)amide was more potent than [Nle(8,18),Tyr(34)]-bPTH(3--34)amide in inhibiting hPTHrP(1--34)-stimulated NO release. The PKC inhibitor, H-7 (50 micromol/l), did not change hPTH(1--34)- and hPTHrP(1--34)-stimulated NO release, whereas the combined effect of 10 micromol/l of the cAMP antagonist, Rp-cAMPS, and 50 micromol/l of the calmodulin inhibitor, W-7, was additive. The present studies show that both hPTH(1--34) and hPTHrP(1--34) activate NO production in endothelial cells. The activation of NO release is through PTH/PTHrP receptors and is mediated via the calcium/calmodulin pathway.

Parathyroid hormone-related protein maintains mammary epithelial fate and triggers nipple skin differentiation during embryonic breast development

Development ◽  
2001 ◽  
Vol 128 (4) ◽  
pp. 513-525 ◽  
Author(s):  
J. Foley ◽  
P. Dann ◽  
J. Hong ◽  
J. Cosgrove ◽  
B. Dreyer ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Epithelial Cells ◽  
Cell Fate ◽  
Mesenchymal Cells ◽  
Mammary Development ◽  
Mammary Epithelial ◽  
Related Protein ◽  
Parathyroid Hormone Related Protein ◽  
Mammary Mesenchyme ◽  
Pthrp Receptor

Prior reports have demonstrated that both parathyroid hormone-related protein (PTHrP) and the type I PTH/PTHrP receptor are necessary for the proper development of the embryonic mammary gland in mice. Using a combination of loss-of-function and gain-of-function models, we now report that PTHrP regulates a series of cell fate decisions that are central to the survival and morphogenesis of the mammary epithelium and the formation of the nipple. PTHrP is made in the epithelial cells of the mammary bud and, during embryonic mammary development, it interacts with the surrounding mesenchymal cells to induce the formation of the dense mammary mesenchyme. In response, these mammary-specific mesenchymal cells support the maintenance of mammary epithelial cell fate, trigger epithelial morphogenesis and induce the overlying epidermis to form the nipple. In the absence of PTHrP signaling, the mammary epithelial cells revert to an epidermal fate, no mammary ducts are formed and the nipple does not form. In the presence of diffuse epidermal PTHrP signaling, the ventral dermis is transformed into mammary mesenchyme and the entire ventral epidermis becomes nipple skin. These alterations in cell fate require that PTHrP be expressed during development and they require the presence of the PTH/PTHrP receptor. Finally, PTHrP signaling regulates the epidermal and mesenchymal expression of LEF1 and (β)-catenin, suggesting that these changes in cell fate involve an interaction between the PTHrP and Wnt signaling pathways.

scholarly journals Renal expression of parathyroid hormone-related protein (PTHrP) and PTH/PTHrP receptor in a rat model of tubulointerstitial damage

1999 ◽  
Vol 55 (1) ◽  
pp. 82-90 ◽  
Author(s):  
Raquel Largo ◽  
Dulcenombre Gómez-Garre ◽  
Soledad Santos ◽  
Carlos Peñaranda ◽  
Julia Blanco ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Rat Model ◽  
Related Protein ◽  
Parathyroid Hormone Related Protein ◽  
Tubulointerstitial Damage ◽  
Pthrp Receptor ◽  
Renal Expression

Co-expression of parathyroid hormone-related protein (PTHrP) and PTH/PTHrP receptor in cartilaginous tumours: a marker for malignancy?

Pathology ◽  
2002 ◽  
Vol 34 (2) ◽  
pp. 133-137 ◽  
Author(s):  
Toshiyuki Kunisada ◽  
Jane M. Moseley ◽  
John L. Slavin ◽  
T. John Martin ◽  
Peter F.M. Choong
Keyword(s):  
Parathyroid Hormone ◽  
Related Protein ◽  
Parathyroid Hormone Related Protein ◽  
Pthrp Receptor

Expression of parathyroid hormone-related protein (PTHrP) and PTH/PTHrP receptor in the continuum from benign to malignant liver nodules

2003 ◽  
Vol 124 (4) ◽  
pp. A565
Author(s):  
Mary McStay ◽  
Kay Savage ◽  
Korsa Khan ◽  
Mark Stubbs ◽  
Amar P. Dhillon ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Related Protein ◽  
Liver Nodules ◽  
Parathyroid Hormone Related Protein ◽  
Malignant Liver ◽  
Pthrp Receptor ◽  
The Continuum

Stromal and epithelial cells of the canine prostate express parathyroid hormone-related protein, but not the PTH/PTHrP receptor

The Prostate ◽  
1998 ◽  
Vol 36 (2) ◽  
pp. 110-120 ◽  
Author(s):  
Eric A.G. Blomme ◽  
Yasuro Sugimoto ◽  
Laurie K. McCauley ◽  
Young C. Lin ◽  
Charles C. Capen ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Epithelial Cells ◽  
Related Protein ◽  
Parathyroid Hormone Related Protein ◽  
Pthrp Receptor
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