Protein Kinase C Is Crucial for the Stimulation of Sodium-Dependent Phosphate Transport by Parathyroid Hormone-Related Peptide in Osteoblast-like Cells

1994 ◽  
Vol 199 (3) ◽  
pp. 1216-1222 ◽  
Author(s):  
M. Arao ◽  
T. Yamaguchi ◽  
T. Sugimoto ◽  
M. Fukase ◽  
K. Chihara
Keyword(s):  
Protein Kinase C ◽  
Parathyroid Hormone ◽  
Protein Kinase ◽  
Phosphate Transport ◽  
Related Peptide ◽  
Kinase C ◽  
Sodium Dependent ◽  
Parathyroid Hormone Related Peptide ◽  
Stimulation Of

Stimulation of transient elevations in cytosolic Ca2+ is related to inhibition of Pi transport in OK cells

1990 ◽  
Vol 259 (3) ◽  
pp. F485-F493 ◽  
Author(s):  
A. Miyauchi ◽  
V. Dobre ◽  
M. Rickmeyer ◽  
J. Cole ◽  
L. Forte ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Parathyroid Hormone ◽  
Protein Kinase ◽  
Phospholipase C ◽  
Cytosolic Calcium ◽  
Wild Type ◽  
Kinase C ◽  
Pi Transport ◽  
Sodium Dependent ◽  
Stimulation Of

Stimulation of changes in cytosolic free calcium by parathyroid hormone was determined in three opossum kidney (OK) cell types, OK wild-type, OKP clone, and OKH clone. All three types of OK cells express parathyroid hormone (PTH)-sensitive adenylate cyclase and adenosine 3',5'-cyclic monophosphate (cAMP) production. However, only the OK wild-type and the OKP clone respond to PTH with inhibition of sodium-dependent Pi transport and transient increase in cytosolic calcium. Characterization of the increases in cytosolic calcium in the wild-type and OKP clones revealed they were due in part to stimulation of Ca2+ release from intracellular stores, probably by inositol 1,4,5-trisphosphate (IP3), which was stimulated by PTH. PTH-stimulated Ca2+ transients were also inhibited by protein kinase C activation. These data are compatible with PTH receptor-mediated phospholipase C activation and its feedback inhibition by protein kinase C. The OKH cells demonstrated a slow increase in cytosolic calcium when stimulated by cyclic nucleotides but no evidence for PTH stimulation of Ca2+ release from intracellular stores. Thus the absence of an inhibitory response of sodium-dependent Pi transport to PTH in the OKH cells is associated with the absence of the rapid transient elevations of cytosolic Ca2+ such as those produced by IP3 production. These data suggest an important cooperative role for cAMP and the phospholipase C-stimulated Ca2(+)-protein kinase C message system in the regulation of Pi transport.

A dual mechanism for regulation of kidney phosphate transport by parathyroid hormone

1987 ◽  
Vol 253 (2) ◽  
pp. E221-E227 ◽  
Author(s):  
J. A. Cole ◽  
S. L. Eber ◽  
R. E. Poelling ◽  
P. K. Thorne ◽  
L. R. Forte
Keyword(s):  
Protein Kinase C ◽  
Parathyroid Hormone ◽  
Protein Kinase ◽  
Phorbol Esters ◽  
Rank Order ◽  
Phosphate Transport ◽  
Opossum Kidney ◽  
Ok Cells ◽  
Kinase C ◽  
Camp Formation

Regulation of phosphate transport by parathyroid hormone (PTH) was investigated in continuous lines of kidney cells. Phosphate transport was reduced by PTH-(1-34) at physiological concentrations (EC50 5 X 10(-11) M), whereas much higher concentrations were required to stimulate cAMP formation (EC50 1 X 10(-8) M) in opossum kidney (OK) cells. The PTH analogue [Nle]PTH-(3-34) also inhibited phosphate transport but did not enhance cAMP formation. Instead, [Nle]PTH-(3-34) was a competitive antagonist of PTH-(1-34) at cyclase-coupled receptors. PTH-(7-34) had no effect on phosphate transport or cAMP formation. Phorbol esters or mezerein were potent inhibitors of phosphate transport but did not affect cAMP synthesis. Their potencies paralleled the rank-order potency of these agents as activators of protein kinase c in other systems. Maximally effective concentrations of PTH-(1-34) and mezerein did not produce additive inhibition of phosphate transport in OK cells. Phorbol esters stimulated phosphate transport in JTC-12 cells, but PTH-(1-34) had no effect. We concluded that PTH regulates OK cell phosphate transport by interacting with two classes of receptors, and transmembrane-signaling mechanisms. Physiological levels of PTH-(1-34) may regulate phosphate transport by activation of protein kinase c, whereas higher concentrations appear to activate adenylate cyclase.

scholarly journals Dual Regulation of the Parathyroid Hormone (PTH)/PTH-Related Peptide Receptor Signaling by Protein Kinase C and β-Arrestins

Endocrinology ◽  
2002 ◽  
Vol 143 (10) ◽  
pp. 3854-3865 ◽  
Author(s):  
Marián Castro ◽  
Frank Dicker ◽  
Jean-Pierre Vilardaga ◽  
Cornelius Krasel ◽  
Manfred Bernhardt ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Parathyroid Hormone ◽  
Protein Kinase ◽  
Receptor Signaling ◽  
Peptide Receptor ◽  
Related Peptide ◽  
Kinase C

Calcitonin gene-related peptide and calcitonin secretion from a human medullary thyroid carcinoma cell line: effects of ionomycin, phorbol ester and forskolin

1988 ◽  
Vol 119 (1) ◽  
pp. 147-152 ◽  
Author(s):  
S. Haller-Brem ◽  
R. Muff ◽  
J. A. Fischer
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Thyroid Carcinoma ◽  
Cell Line ◽  
Medullary Thyroid Carcinoma ◽  
Medullary Thyroid ◽  
Related Peptide ◽  
Kinase C ◽  
Calcitonin Gene ◽  
Stimulation Of

ABSTRACT Calcitonin gene-related peptide (CGRP) and calcitonin are secreted together from medullary thyroid carcinoma (MTC) cells. Interactions of cytosolic free calcium concentration (Cai2+) and the protein kinase C and A pathways on the secretion of immunoreactive CGRP and calcitonin have been investigated in a human MTC cell line. Ionomycin (10 μmol/l) raised the concentration of Cai2+, concomitant with a transient stimulation of the secretion of CGRP and calcitonin. 12-O-tetradecanoylphorbol-13-acetate (TPA; 16 nmol/l) did not affect the concentration of Cai2+, but caused a gradual rise of the secretion of CGRP and calcitonin. Combined addition of 10 μmol ionomycin/1 and 16 nmol TPA/1 resulted in additive stimulation of CGRP and calcitonin secretory responses. Forskolin (10 μmol/l) alone did not change the concentration of Cai2+, marginally enhanced (P>0·1) the release of CGRP and calcitonin and increased by 23-fold the cellular levels of cyclic AMP (cAMP). Ionomycin and TPA did not change cellular cAMP. Forskolin synergistically enhanced (P<0·01) the ionomycin-induced early phase as well as the TPA-induced late phase of the CGRP and calcitonin secretory responses. In conclusion, increased concentrations of Cai2+ together with protein kinase C and A activation mediate the secretion of CGRP and calcitonin in MTC cells. J. Endocr. (1988) 119, 147–152

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