scholarly journals Parathyroid Hormone-Related Protein(1–34) Regulates Phex Expression in Osteoblasts through the Protein Kinase A Pathway

Endocrinology ◽  
2003 ◽  
Vol 144 (11) ◽  
pp. 4876-4885 ◽  
Author(s):  
Miguel Ángel Vargas ◽  
Mathieu St-Louis ◽  
Luc Desgroseillers ◽  
Jean-Louis Charli ◽  
Guy Boileau
Keyword(s):  
Parathyroid Hormone ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Related Protein ◽  
Parathyroid Hormone Related Protein ◽  
Kinase A

scholarly journals Parathyroid hormone-related peptide regulation of chick tibial growth plate chondrocyte maturation requires protein kinase A

2002 ◽  
Vol 20 (5) ◽  
pp. 1079-1090 ◽  
Author(s):  
Michael J. Zuscik ◽  
Regis J. O'Keefe ◽  
Thomas E. Gunter ◽  
J. Edward Puzas ◽  
Edward M. Schwarz ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Growth Plate ◽  
Chondrocyte Maturation ◽  
Related Peptide ◽  
Growth Plate Chondrocyte ◽  
Parathyroid Hormone Related Peptide ◽  
Tibial Growth Plate ◽  
Kinase A

Inhibition of PAH transport by parathyroid hormone in OK cells: involvement of protein kinase C pathway

1997 ◽  
Vol 273 (5) ◽  
pp. F674-F679 ◽  
Author(s):  
Junya Nagai ◽  
Ikuko Yano ◽  
Yukiya Hashimoto ◽  
Mikihisa Takano ◽  
Ken-Ichi Inui
Keyword(s):  
Protein Kinase C ◽  
Parathyroid Hormone ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Regulatory Control ◽  
Dependent Manner ◽  
Transcellular Transport ◽  
Ok Cells ◽  
Kinase C ◽  
Kinase A

We have previously shown that the p-aminohippurate (PAH) transport system in OK kidney epithelial cell line is under the regulatory control of protein kinase C. Parathyroid hormone (PTH) could activate protein kinase C, as well as protein kinase A, in OK cells. In the present study, the effect of PTH on PAH transport was studied in OK cells. PTH inhibited the transcellular transport of PAH from the basal to the apical side, as well as the accumulation of PAH in OK cells. Basolateral PAH uptake was inhibited by PTH in a dose- and time-dependent manner. Protein kinase A activators did not affect the transcellular transport or the accumulation of PAH. The PTH-induced inhibition of the accumulation of PAH was blocked by a protein kinase C inhibitor staurosporine. These results suggest that PTH inhibits the PAH transport in OK cells and that the messenger system mediated by protein kinase C, not protein kinase A, plays an important role in the regulation of PAH transport by PTH.

β-adrenergic enhancement of brain kynurenic acid production mediated via cAMP-related protein kinase A signaling

2009 ◽  
Vol 33 (3) ◽  
pp. 519-529 ◽  
Author(s):  
Elzbieta Luchowska ◽  
Renata Kloc ◽  
Bartosz Olajossy ◽  
Sebastian Wnuk ◽  
Marian Wielosz ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Acid Production ◽  
Kynurenic Acid ◽  
Related Protein ◽  
Kinase A

scholarly journals The phosphorylation status of Ser-637 in dynamin-related protein 1 (Drp1) does not determine Drp1 recruitment to mitochondria

2019 ◽  
Vol 294 (46) ◽  
pp. 17262-17277 ◽  
Author(s):  
Rong Yu ◽  
Tong Liu ◽  
Chenfei Ning ◽  
Fei Tan ◽  
Shao-Bo Jin ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Mitochondrial Fission ◽  
Elongation Factor ◽  
Subcellular Fractionation ◽  
Related Protein ◽  
Wild Type ◽  
Mitochondrial Elongation ◽  
Elongation Factor 1 ◽  
Kinase A

Recruitment of the GTPase dynamin-related protein 1 (Drp1) to mitochondria is a central step required for mitochondrial fission. Reversible Drp1 phosphorylation has been implicated in the regulation of this process, but whether Drp1 phosphorylation at Ser-637 determines its subcellular localization and fission activity remains to be fully elucidated. Here, using HEK 293T cells and immunofluorescence, immunoblotting, RNAi, subcellular fractionation, co-immunoprecipitation assays, and CRISPR/Cas9 genome editing, we show that Drp1 phosphorylated at Ser-637 (Drp1pS637) resides both in the cytosol and on mitochondria. We found that the receptors mitochondrial fission factor (Mff) and mitochondrial elongation factor 1/2 (MIEF1/2) interact with and recruit Drp1pS637 to mitochondria and that elevated Mff or MIEF levels promote Drp1pS637 accumulation on mitochondria. We also noted that protein kinase A (PKA), which mediates phosphorylation of Drp1 on Ser-637, is partially present on mitochondria and interacts with both MIEFs and Mff. PKA knockdown did not affect the Drp1-Mff interaction, but slightly enhanced the interaction between Drp1 and MIEFs. In Drp1-deficient HEK 293T cells, both phosphomimetic Drp1-S637D and phospho-deficient Drp1-S637A variants, like wild-type Drp1, located to the cytosol and to mitochondria and rescued a Drp1 deficiency-induced mitochondrial hyperfusion phenotype. However, Drp1-S637D was less efficient than Drp1-WT and Drp1-S637A in inducing mitochondrial fission. In conclusion, the Ser-637 phosphorylation status in Drp1 is not a determinant that controls Drp1 recruitment to mitochondria.

Parathyroid hormone regulates osterix and Runx2 mRNA expression predominantly through protein kinase A signaling in osteoblast-like cells

2006 ◽  
Vol 29 (2) ◽  
pp. 101-108 ◽  
Author(s):  
B. L. Wang ◽  
C. L. Dai ◽  
J. X. Quan ◽  
Z. F. Zhu ◽  
F. Zheng ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Protein Kinase ◽  
Mrna Expression ◽  
Protein Kinase A ◽  
Kinase A
Sign in / Sign up

Export Citation Format

Share Document