Robert Butters

TL;DR: The cloning of complementary DNA encoding an extracellular Ca2+ -sensing receptor from bovine parathyroid is reported with pharmacological and functional properties nearly identical to those of the native receptor.

TL;DR: The data strongly suggest that the osteoblastic cell line MC3T3‐E1 possesses both CaR protein and mRNA very similar, if not identical, to those in parathyroid and kidney, and the CaR in these osteoblasts could play a key role in regulating bone turnover by stimulating the proliferation and migration of such cells to sites of bone resorption as a result of local release of Ca2+o.

TL;DR: Whether the MCF-7 and MDA-MB-231 human breast cancer cell lines express the CaR and whether CaR agonists modulate PTHrP secretion is investigated, which could potentially participate in a vicious cycle in which PTHRP-induced bone resorption raises the levels of Ca2+(o) and TGFbeta within the bony microenvironment, which then act in concert to evoke further P THrP release and worsening osteolysis.

TL;DR: The extracellular Ca2+ (Cao2+)‐sensing receptor (CaR) is a G protein–coupled receptor that activates phospholipase C (PLC), providing for coordinate, receptor‐mediated regulation of multiple signal transduction pathways in parathyroid and presumably other CaR‐expressing cells.

TL;DR: Findings indicate the presence of CaR mRNA and protein in the breast, providing indirect evidence that the CaR may have some role(s) in the control of Ca2+ transport, epithelial cell proliferation, and/or other processes in normal and abnormal breast tissue.