Role of nuclear factor of activated T-cells 5 in regulating hypertonic-mediated secretin receptor expression in kidney collecting duct cells

2016 ◽  
Vol 1859 (7) ◽  
pp. 922-932
Author(s):  
Oscar W.H. Chua ◽  
Kenneth K.L. Wong ◽  
Ben C. Ko ◽  
Sookja K. Chung ◽  
Billy K.C. Chow ◽  
...  
Keyword(s):  
T Cells ◽  
Collecting Duct ◽  
Receptor Expression ◽  
Nuclear Factor ◽  
Activated T Cells ◽  
Kidney Collecting Duct ◽  
Duct Cells ◽  
Secretin Receptor ◽  
Collecting Duct Cells

Role of AQP2 during apoptosis in cortical collecting duct cells

2009 ◽  
Vol 101 (4) ◽  
pp. 237-250 ◽  
Author(s):  
Pilar Flamenco ◽  
Luciano Galizia ◽  
Valeria Rivarola ◽  
Juan Fernandez ◽  
Paula Ford ◽  
...  
Keyword(s):  
Collecting Duct ◽  
Cortical Collecting Duct ◽  
Duct Cells ◽  
Collecting Duct Cells

Response of rat inner medullary collecting duct to epidermal growth factor

1989 ◽  
Vol 256 (6) ◽  
pp. F1117-F1124 ◽  
Author(s):  
R. C. Harris
Keyword(s):  
Growth Factor ◽  
Binding Sites ◽  
Collecting Duct ◽  
Affinity Binding ◽  
Inner Medullary Collecting Duct ◽  
Duct Cells ◽  
Epidermal Growth ◽  
Collecting Duct Cells ◽  
Medullary Collecting Duct

Urine is an abundant source of epidermal growth factor (EGF) and prepro-EGF has been localized to the thick ascending limb and distal convoluted tubule of the kidney. However, the functional role of EGF in the kidney is poorly understood. Determination of EGF receptors and functional responses to EGF in intrarenal structures distal to the site of renal EGF production may prove critical to our understanding of the role of this peptide. These studies were designed to investigate the response to EGF of rat inner medullary collecting duct cells in culture and in freshly isolated suspensions. Primary cultures of inner medullary collecting duct cells demonstrated equilibrium binding of 125I-labeled EGF at 4 and 23 degrees C. At 23 degrees C, there was 89 +/- 1% specific binding (n = 30). Scatchard analysis of 125I-EGF binding suggested the presence of both high-affinity binding with a dissociation constant (Kd) of 5 X 10(-10) M and maximal binding sites (Ro) of 2.7 X 10(3) binding sites/cell and low-affinity binding, with Kd of 8.3 X 10(-9) M and Ro of 1.8 X 10(4) binding sites/cell. Bound EGF, 68 +/- 3%, was internalized by 45 min. EGF binding was not inhibited by antidiuretic hormone, atrial natriuretic peptide or bradykinin at 23 degrees C, but there was concentration-dependent inhibition of binding by transforming growth factor-alpha. Incubation with phorbol myristate acetate decreased 125I-EGF binding in a concentration-dependent manner. 125I-EGF binding was also demonstrated in freshly isolated suspensions of rat inner medullary collecting duct cells.(ABSTRACT TRUNCATED AT 250 WORDS)

Adaptation to alkalosis induces cell cycle delay and apoptosis in cortical collecting duct cells: Role of aquaporin-2

2010 ◽  
Vol 224 (2) ◽  
pp. 405-413 ◽  
Author(s):  
Valeria Rivarola ◽  
Pilar Flamenco ◽  
Luciana Melamud ◽  
Luciano Galizia ◽  
Paula Ford ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Collecting Duct ◽  
Cortical Collecting Duct ◽  
Cell Cycle Delay ◽  
Aquaporin 2 ◽  
Duct Cells ◽  
Collecting Duct Cells

scholarly journals The Essential Role of MEKK3 Signaling in Angiotensin II-induced Calcineurin/Nuclear Factor of Activated T-cells Activation

2005 ◽  
Vol 280 (44) ◽  
pp. 36737-36746 ◽  
Author(s):  
Shahrzad Abbasi ◽  
Bing Su ◽  
Rodney E. Kellems ◽  
JianHua Yang ◽  
Yang Xia
Keyword(s):  
T Cells ◽  
Angiotensin Ii ◽  
Essential Role ◽  
Nuclear Factor ◽  
Activated T Cells

Generation of AQP2-Cre transgenic mini-pigs specifically expressing Cre recombinase in kidney collecting duct cells

2013 ◽  
Vol 23 (2) ◽  
pp. 365-375 ◽  
Author(s):  
Weiwei Luo ◽  
Zhanjun Li ◽  
Yongye Huang ◽  
Yang Han ◽  
Chaogang Yao ◽  
...  
Keyword(s):  
Collecting Duct ◽  
Cre Recombinase ◽  
Kidney Collecting Duct ◽  
Duct Cells ◽  
Collecting Duct Cells ◽  
Mini Pigs

scholarly journals Dynamic equilibrium between calcineurin and kinase activities regulates the phosphorylation state and localization of the nuclear factor of activated T-cells

1997 ◽  
Vol 324 (2) ◽  
pp. 597-603 ◽  
Author(s):  
John E. SCOTT ◽  
Valerie A. RUFF ◽  
Karen L. LEACH
Keyword(s):  
T Cells ◽  
Nuclear Localization ◽  
T Cell Activation ◽  
Cell Activation ◽  
Kinase Inhibitors ◽  
Dynamic Equilibrium ◽  
Nuclear Factor ◽  
Activated T Cells ◽  
Phosphorylation State

The nuclear factor of activated T-cells (NFATp) is a phosphorylated transcription factor that resides in the cytoplasm of unactivated T-cells. T-cell activation results in the activation of the phosphatase calcineurin (CaN), which leads to the dephosphorylation and subsequent nuclear localization of NFATp. We have investigated the role of kinases in the phosphorylation state and subcellular localization of NFATp. The phosphorylation state and nuclear/cytoplasmic location of NFATp were determined in unstimulated murine HT-2 cells treated with a panel of kinase inhibitors. Two of the seven kinase inhibitors, staurosporine (St) and bisindolylmaleimide I (BI), resulted in the dephosphorylation and nuclear localization of NFATp. These St-induced effects were inhibited by pretreatment with FK506, indicating that CaN activity was required for the observed effects on NFATp. Treatment of cells with ionomycin resulted in NFATp dephosphorylation and nuclear localization. Removal of ionomycin from the cells resulted in the reappearance of phosphorylated NFATp in the cytosol. St and BI also inhibited the re-accumulation of NFATp in the cytoplasm and its re-phosphorylation after ionomycin removal. The re-accumulation of NFATp in the cytosol after ionomycin withdrawal was shown to be energy- and temperature-dependent. Taken together, these results suggest that in unstimulated cells NFATp is actively maintained in the cytoplasm by kinases acting in opposition to basal CaN activity.

scholarly journals Mice Lacking the Calcineurin Inhibitor Rcan2 Have an Isolated Defect of Osteoblast Function

Endocrinology ◽  
2012 ◽  
Vol 153 (7) ◽  
pp. 3537-3548 ◽  
Author(s):  
J. H. Duncan Bassett ◽  
John G. Logan ◽  
Alan Boyde ◽  
Moira S. Cheung ◽  
Holly Evans ◽  
...  
Keyword(s):  
T Cells ◽  
Bone Development ◽  
Skeletal Development ◽  
Dominant Negative ◽  
Nuclear Factor ◽  
Activated T Cells ◽  
Osteoblast Function ◽  
And Function

Calcineurin-nuclear factor of activated T cells signaling controls the differentiation and function of osteoclasts and osteoblasts, and regulator of calcineurin-2 (Rcan2) is a physiological inhibitor of this pathway. Rcan2 expression is regulated by T3, which also has a central role in skeletal development and bone turnover. To investigate the role of Rcan2 in bone development and maintenance, we characterized Rcan2−/− mice and determined its skeletal expression in T3 receptor (TR) knockout and thyroid-manipulated mice. Rcan2−/− mice had normal linear growth but displayed delayed intramembranous ossification, impaired cortical bone formation, and reduced bone mineral accrual during development as well as increased mineralization of adult bone. These abnormalities resulted from an isolated defect in osteoblast function and are similar to skeletal phenotypes of mice lacking the type 2 deiodinase thyroid hormone activating enzyme or with dominant-negative mutations of TRα, the predominant TR isoform in bone. Rcan2 mRNA was expressed in primary osteoclasts and osteoblasts, and its expression in bone was differentially regulated in TRα and TRβ knockout and thyroid-manipulated mice. However, in primary osteoblast cultures, T3 treatment did not affect Rcan2 mRNA expression or nuclear factor of activated T cells c1 expression and phosphorylation. Overall, these studies establish that Rcan2 regulates osteoblast function and its expression in bone is regulated by thyroid status in vivo.

Sign in / Sign up

Export Citation Format

Share Document