Parathyroid Hormone-Related Protein (107-139) Decreases Alkaline Phosphatase in Osteoblastic Osteosarcoma Cells UMR 106 by a Protein Kinase C-Dependent Pathway

1999 ◽  
Vol 65 (2) ◽  
pp. 148-151 ◽  
Author(s):  
A. Valín ◽  
F. de Miguel ◽  
A. García-Ocaña ◽  
P. Esbrit
Keyword(s):  
Alkaline Phosphatase ◽  
Protein Kinase C ◽  
Parathyroid Hormone ◽  
Related Protein ◽  
Osteosarcoma Cells ◽  
Parathyroid Hormone Related Protein ◽  
Kinase C ◽  
Umr 106 ◽  
Dependent Pathway ◽  
Osteoblastic Osteosarcoma

Parathyroid hormone stimulates translocation of protein kinase C isozymes in UMR-106 osteoblastic osteosarcoma cells

Bone ◽  
2001 ◽  
Vol 29 (3) ◽  
pp. 223-230 ◽  
Author(s):  
D.A Dossing ◽  
J.M Radeff ◽  
J Sanders ◽  
S.-K Lee ◽  
M.-R Hsieh ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Parathyroid Hormone ◽  
Protein Kinase ◽  
Osteosarcoma Cells ◽  
Kinase C ◽  
Umr 106 ◽  
Osteoblastic Osteosarcoma

Protein kinase C-activating domains of parathyroid hormone-related protein

2009 ◽  
Vol 8 (4) ◽  
pp. 497-503 ◽  
Author(s):  
Lyne Gagnon ◽  
Hervé Jouishomme ◽  
James F. Whitfield ◽  
Jon P. Durkin ◽  
Susanne MacLean ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Parathyroid Hormone ◽  
Protein Kinase ◽  
Related Protein ◽  
Parathyroid Hormone Related Protein ◽  
Kinase C

Protein kinase C activating phorbolesters enhance the cyclic AMP response to parathyroid hormone, forskolin and choleratoxin in mouse calvarial bones and rat osteosarcoma cells

1991 ◽  
Vol 11 (4) ◽  
pp. 203-211 ◽  
Author(s):  
Maria Ransjö
Keyword(s):  
Protein Kinase C ◽  
Parathyroid Hormone ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Phorbol Esters ◽  
Osteosarcoma Cells ◽  
Kinase C ◽  
Cyclic Amp Accumulation ◽  
Umr 106

The protein kinase C-(PKC) activating phorbol esters 12-O-tetradecanoylphorbol-13-acetate (TPA; 100 nmol/l) and phorbol 12, 13-dibutyrate (PDBU; 100 nmol/l) enhanced basal cyclin AMP accumulation in cultured neonatal mouse calvaria. The cyclic AMP response to parathyroid hormone (PTH; 10 nmol/l) and the adenylate cyclase activators forskolin (1–3 μmol/l) and choleratoxin (0.1 μmg/ml) was potentiated in a more than additive manner by TPA and PDBU. In contrast, phorbol 13-monoacetate (phorb-13; 100 nmol/l), a related compound but inactive on PKC, had no effect on basal or stimulated cyclic AMP accumulation. In the presence of indomethacin (1μmol/l), TPA and PDBU had no effect on cyclic AMP accumulation in calvarial bones per se, but were still able to cause a significant enhancement of the response to PTH, forskolin and choleratoxin. PTH-, forskolin- and choleratoxin-stimulated cyclic AMP accumulation in rat osteosarcoma cells UMR 106-01 was synergistically potentiated by TPA and PDBU, but not by phorb.-13. These data indicate that PKC enhances cyclic AMP formation and that the level of interaction may be at, or distal to, adenylate cyclase.

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