Long-term regulation of Na+,K+-ATPase in opossum kidney cells by ouabain

2011 ◽  
Vol 226 (9) ◽  
pp. 2391-2397 ◽  
Author(s):  
E. Silva ◽  
P. Soares-da-Silva
Keyword(s):  
Kidney Cells ◽  
Opossum Kidney ◽  
Opossum Kidney Cells

Short- and long-term A3 adenosine receptor activation inhibits the Na+/H+ exchanger NHE3 activity and expression in opossum kidney cells

2008 ◽  
Vol 216 (1) ◽  
pp. 221-233 ◽  
Author(s):  
Francesca Di Sole ◽  
Robert Cerull ◽  
Victor Babich ◽  
Valeria Casavola ◽  
Corinna Helmle-Roth ◽  
...  
Keyword(s):  
Adenosine Receptor ◽  
Receptor Activation ◽  
Kidney Cells ◽  
Opossum Kidney ◽  
Opossum Kidney Cells ◽  
A3 Adenosine Receptor ◽  
Short And Long Term ◽  
Adenosine Receptor Activation

Evidence for interference of vitamin D with PTH/PTHrP receptor expression in opossum kidney cells

1998 ◽  
Vol 436 (2) ◽  
pp. 289-294 ◽  
Author(s):  
H. Wald ◽  
Michal Dranitzki-Elhalel ◽  
R. Backenroth ◽  
Mordecai M. Popovtzer
Keyword(s):  
Vitamin D ◽  
Receptor Expression ◽  
Kidney Cells ◽  
Opossum Kidney ◽  
Opossum Kidney Cells ◽  
Pthrp Receptor

Parathormone sensitivity and responses to protein kinases in subclones of opossum kidney cells

2005 ◽  
Vol 20 (6) ◽  
pp. 721-724 ◽  
Author(s):  
Douglas M. Silverstein ◽  
Adrian Spitzer ◽  
Mario Barac-Nieto
Keyword(s):  
Protein Kinases ◽  
Kidney Cells ◽  
Opossum Kidney ◽  
Opossum Kidney Cells

scholarly journals Structure/function analysis of Na+-K+-ATPase central isoform-specific region: involvement in PKC regulation

2002 ◽  
Vol 283 (5) ◽  
pp. F1066-F1074 ◽  
Author(s):  
Sandrine V. Pierre ◽  
Marie-Josée Duran ◽  
Deborah L. Carr ◽  
Thomas A. Pressley
Keyword(s):  
Structure Function ◽  
Function Analysis ◽  
Specific Region ◽  
Stable Transfection ◽  
Kidney Cells ◽  
Opossum Kidney ◽  
Opossum Kidney Cells ◽  
Structural Divergence ◽  
Chimeric Molecules ◽  
Pkc Activation

Specific functions served by the various Na+-K+-ATPase α-isoforms are likely to originate in regions of structural divergence within their primary structures. The isoforms are nearly identical, with the exception of the NH2 terminus and a 10-residue region near the center of each molecule (isoform-specific region; ISR). Although the NH2 terminus has been clearly identified as a source of isoform functional diversity, other regions seem to be involved. We investigated whether the central ISR could also contribute to isoform variability. We constructed chimeric molecules in which the central ISRs of rat α1- and α2-isoforms were exchanged. After stable transfection into opossum kidney cells, the chimeras were characterized for two properties known to differ dramatically among the isoforms: their K+ deocclusion pattern and their response to PKC activation. Comparisons with rat full-length α1- and α2-isoforms expressed under the same conditions suggest an involvement of the central ISR in the response to PKC but not in K+ deocclusion.

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