scholarly journals Adaptation of Opossum Kidney Cells to Luminal Phosphate: Effects of Phosphonoformic Acid and Kinase Inhibitors

2016 ◽  
Vol 41 (3) ◽  
pp. 298-310 ◽  
Author(s):  
Linto Thomas ◽  
Carsten A. Wagner ◽  
Jürg Biber ◽  
Nati Hernando
Keyword(s):  
Kinase Inhibitors ◽  
Kidney Cells ◽  
Opossum Kidney ◽  
Phosphonoformic Acid ◽  
Opossum Kidney Cells

scholarly journals Na+/Pi co-transport alters rapidly cytoskeletal protein polymerization dynamics in opossum kidney cells

1996 ◽  
Vol 315 (1) ◽  
pp. 241-247 ◽  
Author(s):  
Evangelia A. PAPAKONSTANTI ◽  
Dimitrios S. EMMANOUEL ◽  
Achille GRAVANIS ◽  
Christos STOURNARAS
Keyword(s):  
Immunoblot Analysis ◽  
Kidney Cells ◽  
Opossum Kidney ◽  
Protein Polymerization ◽  
Phosphonoformic Acid ◽  
Opossum Kidney Cells ◽  
Proximal Tubular ◽  
Microtubule Stabilizer ◽  
Dynamic Equilibria ◽  
Contrast Measurement

We studied with biochemical and immunofluorescent techniques the interactions between the actin microfilament and tubulin microtubule cytoskeleton and Na+/Pi co-transport in opossum kidney cells, a line with proximal tubular characteristics. On brief (5 min) incubation of the cells with a low (0.1 mM) concentration of Pi, a rapid F-actin depolymerization takes place, which fails to occur in cells incubated under similar conditions with 1 mM Pi. The disassembly of actin microfilaments could be quantitatively expressed as a 33% increase in the ratio of monomeric G-actin to polymerized F-actin (G/F-actin ratio from 0.80±0.03 to 1.06±0.06, n = 28, P < 0.01), owing to a significant decrease in the latter. Under these conditions microfilaments were also markedly destabilized, as shown by their diminished resistance to graded cytochalasin B concentrations. In addition, incubation of opossum kidney cells with low Pi concentrations (0.1 mM) resulted within 5 min in a substantial depolymerization of microtubules, shown by immunofluorescence microscopy and measured as a 70.9±6.9% (n = 11, P < 0.01) decrement by immunoblot analysis. These changes, which occur only when extracellular Pi concentrations are kept low, seem to be related to a significant increase within 5 min in the rate of cellular Pi uptake by 25.5% under these conditions. The shifts in the dynamic equilibria between monomeric and polymerized actin and tubulin in response to cellular Pi uptake were transient, being fully reversible within 30 min. Moreover, the effect of Pi seemed to be specific because inhibition of its uptake by phosphonoformic acid blunted microtubular disassembly markedly. In contrast, measurement of Pi uptake in the presence of agents known to stabilize cytoskeletal structures showed a substantial decrease with phallacidin, which stabilizes microfilaments, whereas the microtubule stabilizer taxol had no apparent effect. These results indicate that acute alterations in the polymerization dynamics and stability of both microfilaments and microtubules are involved in the modulation of Na+/Pi co-transport and suggest important cytoskeletal participation in proximal tubular transport functions.

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.

Sign in / Sign up

Export Citation Format

Share Document