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- W2073602267 abstract "Abstract PTH, a major regulator of bone remodeling and a therapeutically effective bone anabolic agent, stimulates several signaling pathways in osteoblastic cells. Our recent studies have revealed that PTH activates phospholipase D (PLD) -mediated phospholipid hydrolysis through a RhoA-dependent mechanism in osteoblastic cells, raising the question of the upstream link to the PTH receptor. In the current study, we investigated the role of heterotrimeric G proteins in mediating PTH-stimulated PLD activity in UMR-106 osteoblastic cells. Transfection with antagonist minigenes coding for small peptide antagonists to Gα12 and Gα13 subunits of heterotrimeric G proteins prevented PTH-stimulated activation of PLD, whereas an antagonist minigene to Gαs failed to produce this effect. Effects of pharmacological inhibitors (protein kinase inhibitor, Clostridium botulinum exoenzyme C3) were consistent with a role of Rho small G proteins, but not of cAMP, in the effect of PTH on PLD. Expression of constitutively active Gα12 and Gα13 activated PLD, an effect that was inhibited by dominant-negative RhoA. The results identify Gα12 and Gα13 as upstream transducers of PTH effects on PLD, mediated through RhoA in osteoblastic cells." @default.
- W2073602267 created "2016-06-24" @default.
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- W2073602267 date "2005-05-01" @default.
- W2073602267 modified "2023-10-17" @default.
- W2073602267 title "Gα12/Gα13 Subunits of Heterotrimeric G Proteins Mediate Parathyroid Hormone Activation of Phospholipase D in UMR-106 Osteoblastic Cells" @default.
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- W2073602267 doi "https://doi.org/10.1210/en.2004-1283" @default.
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