scholarly journals Identification and expression analysis of type II and type III Pi transporters in the opossum kidney cell line

2018 ◽  
Vol 104 (1) ◽  
pp. 149-161 ◽  
Author(s):  
Natalia Guillén ◽  
Yupanqui A. Caldas ◽  
Moshe Levi ◽  
Víctor Sorribas
Keyword(s):  
Cell Line ◽  
Expression Analysis ◽  
Kidney Cell ◽  
Type Ii ◽  
Kidney Cell Line ◽  
Opossum Kidney ◽  
Type Iii ◽  
Opossum Kidney Cell

Electrogenic transport of neutral and dibasic amino acids in a cultured opossum kidney cell line (OK)

1989 ◽  
Vol 414 (5) ◽  
pp. 543-550 ◽  
Author(s):  
Johann S. Schwegler ◽  
Almut Heuner ◽  
Stefan Silbernagl
Keyword(s):  
Amino Acids ◽  
Cell Line ◽  
Kidney Cell ◽  
Kidney Cell Line ◽  
Electrogenic Transport ◽  
Opossum Kidney ◽  
Opossum Kidney Cell ◽  
Dibasic Amino Acids

Structure-activity relationships of parathyroid hormone analogs in the opossum kidney cell line

2009 ◽  
Vol 4 (5) ◽  
pp. 723-730 ◽  
Author(s):  
David L. Carnes ◽  
Judith A. Cole ◽  
Leonard R. Forte ◽  
Richard E. Poelling ◽  
Pamela K. Thorne ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Cell Line ◽  
Kidney Cell ◽  
Kidney Cell Line ◽  
Opossum Kidney ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
Opossum Kidney Cell ◽  
Hormone Analogs

Type II Na-Pi cotransport is regulated transcriptionally by ambient bicarbonate/carbon dioxide tension in OK cells

1999 ◽  
Vol 276 (1) ◽  
pp. F46-F53 ◽  
Author(s):  
Andreas W. Jehle ◽  
Helene Hilfiker ◽  
Markus F. Pfister ◽  
Jürg Biber ◽  
Eleanor Lederer ◽  
...  
Keyword(s):  
Promoter Activity ◽  
Carbon Dioxide Tension ◽  
Type Ii ◽  
Kidney Cell Line ◽  
Mrna Transcription ◽  
Opossum Kidney ◽  
Ok Cells ◽  
Transporter Protein ◽  
Threefold Increase ◽  
Opossum Kidney Cell

The purpose of the present study was to determine whether isohydric changes in HCO3 concentration and Pco 2directly affect apical Na-dependent Pi(Na-Pi) cotransport in OK cells (opossum kidney cell line). Cells were kept at either 44 mM NaHCO3/10% CO2, pH 7.4 (high-HCO3/CO2condition), or 22 mM NaHCO3/5% CO2, pH 7.4 (low-HCO3/CO2condition) (for 14–24 h). Incubation in lower HCO3/CO2concentrations increased Na-Picotransport 1.5-fold. The increased Na-Pi cotransport was paralleled by a two- to threefold increased expression of the NaPi-4 transporter protein and a two- to threefold increase in NaPi-4 mRNA abundance. The increase in NaPi-4 mRNA could be completely prevented by incubation in the presence of a transcriptional inhibitor, suggesting that the increase in NaPi-4 mRNA results from an increased NaPi-4 mRNA transcription. In agreement, the NaPi-4 promoter activity was stimulated by 50% at lower HCO3/CO2concentrations. In conclusion, our data demonstrate that isohydric changes in HCO3 concentration and Pco 2exert a significant, direct cellular effect on Na-Pi cotransport and NaPi-4 protein expression in OK cells by affecting NaPi-4 mRNA transcription.

Insulin binding, internalization, and degradation by a cultured kidney cell line

1988 ◽  
Vol 254 (5) ◽  
pp. E601-E608
Author(s):  
C. Yagil ◽  
U. K. Ehmann ◽  
B. H. Frank ◽  
R. Rabkin
Keyword(s):  
Cell Line ◽  
Kidney Cell ◽  
Insulin Binding ◽  
Insulin Degradation ◽  
Kidney Cell Line ◽  
Insulin Metabolism ◽  
Opossum Kidney ◽  
Membrane Bound ◽  
Hormone Specificity ◽  
Insulin Uptake

Proximal tubules are a key site of insulin metabolism, which is in part a receptor-mediated process. To explore the interaction between insulin and the kidney and to evaluate the role of receptors in insulin uptake and processing, a study was carried out with a cultured proximal-like opossum kidney (OK) cell line. 125I-insulin associated with confluent monolayers in a specific manner, and this interaction was competitively inhibited by insulin; unrelated peptides were relatively ineffective. Insulin degradation exhibited time and temperature dependency and up to a concentration of 5 X 10(-8) M was not saturable. Degradation exhibited partial hormone specificity. Separation of plasma membrane bound from internalized insulin was achieved by lowering extracellular pH. At 4 degrees C, 94% of cell-associated radioactivity was membrane bound, whereas at 37 degrees C, in the steady state, 33% was membrane bound and 67% was internalized. There was a significant correlation between membrane-bound insulin and the rate of degradation. These findings reveal that the binding and processing of insulin by the kidney cell line are compatible with the description of the uptake of filtered insulin by the proximal tubule in the intact kidney. Accordingly we conclude that this cell line provides a good model for studying renal epithelial uptake and metabolism of insulin.

5?-reductase in human embryonic kidney cell line HEK293: Evidence for type II enzyme expression and activity

2005 ◽  
Vol 270 (1-2) ◽  
pp. 201-208 ◽  
Author(s):  
Baerbel U. Panter ◽  
Joachim Jose ◽  
Rolf W. Hartmann
Keyword(s):  
Cell Line ◽  
Kidney Cell ◽  
Type Ii ◽  
Kidney Cell Line ◽  
Human Embryonic Kidney ◽  
Enzyme Expression ◽  
Human Embryonic Kidney Cell ◽  
Expression And Activity

Trials for Preparation of Dog Kidney Cell Line

2014 ◽  
Vol 8 (1) ◽  
pp. 32-38
Author(s):  
Amani Abbas ◽  
Hemmat Alemam ◽  
Hanan El-zawahry
Keyword(s):  
Cell Line ◽  
Kidney Cell ◽  
Kidney Cell Line ◽  
Dog Kidney

scholarly journals Biosynthesis and secretion of an osteopontin-related 20-kDa polypeptide in the Madin-Darby canine kidney cell line

1991 ◽  
Vol 266 (6) ◽  
pp. 3518-3525
Author(s):  
O Ullrich ◽  
K Mann ◽  
W Haase ◽  
C Koch-Brandt
Keyword(s):  
Cell Line ◽  
Kidney Cell ◽  
Kidney Cell Line ◽  
Madin Darby Canine Kidney ◽  
Darby Canine Kidney ◽  
Canine Kidney
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