Regulation of MAP kinase by calcium-sensing receptor in bovine parathyroid and CaR-transfected HEK293 cells.

@article{Kifor2001RegulationOM,
  title={Regulation of MAP kinase by calcium-sensing receptor in bovine parathyroid and CaR-transfected HEK293 cells.},
  author={Olga Kifor and R. John Macleod and R Diaz and Mei Bai and T. Yamaguchi and T L Yao and Imre Kifor and Edward Meigs Brown},
  journal={American journal of physiology. Renal physiology},
  year={2001},
  volume={280 2},
  pages={
          F291-302
        }
}
Regulation of the extracellular signal-regulated kinase 1 and 2 (ERK1/2) pathway by the extracellular calcium (Ca2+o)-sensing receptor (CaR) was investigated in bovine parathyroid and CaR-transfected human embryonic kidney (HEKCaR) cells. Elevating Ca2+o or adding the selective CaR activator NPS R-467 elicited rapid, dose-dependent phosphorylation of ERK1/2. These phosphorylations were attenuated by pretreatment with pertussis toxin (PTX) or by treatment with the phosphotyrosine kinase (PTK… Expand
Activation of the MAP kinase cascade by exogenous calcium-sensing receptor
TLDR
CaR-transfected HEK293 cells are utilized to demonstrate that functional CaR is necessary and sufficient for calcium-induced ERK activation and suggest that usage of distinct pathways downstream of the CaR varies in a cell-type specific manner, suggesting a potential mechanism by which activation of theCaR could couple to distinct calcium-dependent responses. Expand
Extracellular calcium-sensing receptor transactivates the epidermal growth factor receptor by a triple-membrane-spanning signaling mechanism.
TLDR
Inhibitors of matrix metalloproteinase and heparin bound-EGF prevented the CaR-mediated increases of pERK and PTHrP, consistent with a "triple-membrane-spanning signaling" requirement for transactivation of the EGFR by the Ca R. Expand
PTHrP stimulated by the calcium-sensing receptor requires MAP kinase activation.
TLDR
It is concluded that CaR specifically mediates the effect of increasing [Ca(2+)](o) on PTHrP synthesis and secretion and that activated MEK1/2 and p38 MAP kinases are determinants of the CaR's stimulation of P THrP secretion. Expand
Calcium-sensing receptor stimulates PTHrP release by pathways dependent on PKC, p38 MAPK, JNK, and ERK1/2 in H-500 cells.
TLDR
It is shown for the first time that high [Ca2+]o-induced activation of the stress-activated protein kinase SEK1 is PKC independent, because there is an additive effect of a PKC inhibitor in combination with the JNK inhibitor on [Ca1-o-stimulated PTHrP release. Expand
Calcium-sensing Receptor-mediated ERK1/2 Activation Requires Gαi2 Coupling and Dynamin-independent Receptor Internalization*
TLDR
Data suggest that both 4 mm Ca2+ and NPS R-467/CaCl2 activate ERK1/2 via distinguishable pathways in HEK-hCaR cells and may represent a nexus to differentially regulate differentiation versus proliferation via CaR activation. Expand
Allosteric activation of the extracellular Ca2+-sensing receptor by L-amino acids enhances ERK1/2 phosphorylation.
TLDR
The data indicate that L-phenylalanine and other amino acids enhance the Ca2+o-sensitivity of CaR-stimulated ERK1/2 phosphorylation; however, the effect is comparatively small and operates in the form of a fine-tuning mechanism. Expand
Calcium-sensing receptor-dependent activation of CREB phosphorylation in HEK293 cells and human parathyroid cells.
TLDR
Analysis of the signaling pathways using specific inhibitors demonstrated that phosphoinositide-specific phospholipase C and conventional protein kinase C isoforms make major contributions to Ca(2+)o-induced p-CREB in both cell-types, suggesting key roles for Gq/11. Expand
Decreased expression of caveolin-1 and altered regulation of mitogen-activated protein kinase in cultured bovine parathyroid cells and human parathyroid adenomas.
TLDR
Caveolins are key components of caveolae membranes, and reduced levels of caveolin-1 could participate in the abnormal cellular function and proliferation of cultured bovine PT cells and PT adenomas. Expand
The Role of Protein Kinase C in the Extracellular Ca2+-regulated Secretion of Parathyroid Hormone
The sensing of extracellular Ca(2+) concentration ([Ca(2+)](o)) and modulation of cellular processes associated with acute or sustained changes in [Ca(2+)](o) are cell-type specific and mediated byExpand
Mitogen-activated protein kinase cascade in human normal and tumoral parathyroid cells.
TLDR
It is demonstrated that CaR activation, through the PKC pathway and, to a lesser extent, PI3K, increases ERK1 and -2 activity in normal parathyroid cells and this cascade seems to be involved in the modulation of PTH secretion by Ca(o)(2+). Expand
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TLDR
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. Expand
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