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Parathyroid Hormone (PTH)-(1–34), [Nle^8,18,Tyr³⁴]PTH-(3–34) Amide, PTH-(1–31) Amide, and PTH-Related Peptide-(1–34) Stimulate Phosphatidylcholine Hydrolysis in UMR-106 Osteoblastic Cells: Comparison with Effects of Phorbol 12,13-Dibutyrate¹

Department of Molecular Pharmacology and Biological Chemistry, Northwestern University Medical School (A.T.K.S., J.G.K., P.J.S., P.H.S.), and the Department of Basic and Behavioral Sciences, Northwestern University Dental School (J.G.K.), Chicago, Illinois 60611-3008

Address all correspondence and requests for reprints to: Amareshwar T. K. Singh, Ph.D., Department of Molecular Pharmacology and Biological Chemistry, Northwestern University Medical School, 303 East Chicago Avenue, Chicago, Illinois 60611-3008. E-mail: a-singh{at}nwu.edu

Studies were performed to determine the effects of PTH and related compounds on phosphatidylcholine (PC) hydrolysis in UMR-106 cells and the pathway by which the PTH effects occurred. The responses were compared with those of phorbol 12,13-dibutyrate (PDBu). Both bovine PTH-(1–34) [bPTH-(1–34)] and PDBu stimulated PC hydrolysis within 10 min. Significant effects were elicited by concentrations of 0.3–1 nM bPTH-(1–34) and 5 nM PDBu. Dose-dependent increases were seen at higher concentrations of both compounds, however, the response to bPTH-(1–34) was reduced at 30 nM. Bovine or human PTH-(1–34) and human PTH-related peptide-(1–34) [hPTHrP-(1–34)] were equipotent in their effects, whereas bovine [Nle^8,18Tyr³⁴]PTH-(3–34) amide [bPTH-(3–34)] and hPTH-(1–31) amide [hPTH-(1–31)] were less potent than bPTH-(1–34). bPTH-(3–34) did not antagonize the effects of bPTH-(1–34). Down-regulation of protein kinase C isozymes by 24-h treatment with PDBu completely prevented the stimulatory effect of PDBu on PC hydrolysis, but did not significantly affect the stimulatory effect of bPTH-(1–34). Both bPTH-(1–34) and PDBu stimulated transphosphatidylation of PC, indicating a phospholipase D-stimulated mechanism. The results suggest that in the UMR-106 cell line PTH can stimulate activation of PLD by a mechanism other than through protein kinase C.

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