scholarly journals Shear stress and oxygen availability drive differential changes in opossum kidney proximal tubule cell metabolism and endocytosis

Traffic ◽  
2019 ◽  
Vol 20 (6) ◽  
pp. 448-459 ◽  
Author(s):  
Qidong Ren ◽  
Megan L. Gliozzi ◽  
Natalie L. Rittenhouse ◽  
Lia R. Edmunds ◽  
Youssef Rbaibi ◽  
...  
Keyword(s):  
Shear Stress ◽  
Proximal Tubule ◽  
Cell Metabolism ◽  
Oxygen Availability ◽  
Proximal Tubule Cell ◽  
Tubule Cell ◽  
Opossum Kidney ◽  
Kidney Proximal Tubule

scholarly journals Author response for "Shear stress and oxygen availability drive differential changes in OK proximal tubule cell metabolism and endocytosis"

2019 ◽  
Author(s):  
Qidong Ren ◽  
Megan L. Gliozzi ◽  
Natalie L. Rittenhouse ◽  
Lia R. Edmunds ◽  
Youssef Rbaibi ◽  
...  
Keyword(s):  
Shear Stress ◽  
Proximal Tubule ◽  
Cell Metabolism ◽  
Oxygen Availability ◽  
Author Response ◽  
Proximal Tubule Cell ◽  
Tubule Cell

Author response for "Shear stress and oxygen availability drive differential changes in OK proximal tubule cell metabolism and endocytosis"

2019 ◽  
Author(s):  
Qidong Ren ◽  
Megan L. Gliozzi ◽  
Natalie L. Rittenhouse ◽  
Lia R. Edmunds ◽  
Youssef Rbaibi ◽  
...  
Keyword(s):  
Shear Stress ◽  
Proximal Tubule ◽  
Cell Metabolism ◽  
Oxygen Availability ◽  
Author Response ◽  
Proximal Tubule Cell ◽  
Tubule Cell

Nitric oxide activates PKCα and inhibits Na+-K+-ATPase in opossum kidney cells

1999 ◽  
Vol 277 (6) ◽  
pp. F859-F865 ◽  
Author(s):  
Mingyu Liang ◽  
Franklyn G. Knox
Keyword(s):  
Nitric Oxide ◽  
Protein Kinase ◽  
Proximal Tubule ◽  
Cell Line ◽  
Soluble Guanylate Cyclase ◽  
Inhibitory Effect ◽  
Proximal Tubule Cell ◽  
Tubule Cell ◽  
Opossum Kidney ◽  
Ok Cells

Nitric oxide (NO) reduces the molecular activity of Na+-K+-ATPase in opossum kidney (OK) cells, a proximal tubule cell line. In the present study, we investigated the cellular mechanisms for the inhibitory effect of NO on Na+-K+-ATPase. Sodium nitroprusside (SNP), a NO donor, inhibited Na+-K+-ATPase in OK cells, but not in LLC-PK1cells, another proximal tubule cell line. Similarly, phorbol 12-myristate 13-acetate, a protein kinase C (PKC) activator, inhibited Na+-K+-ATPase in OK, but not in LLC-PK1, cells. PKC inhibitors staurosporine or calphostin C, but not the protein kinase G inhibitor KT-5823, abolished the inhibitory effect of NO on Na+-K+-ATPase in OK cells. Immunoblotting demonstrated that treatment with NO donors caused significant translocation of PKCα from cytosolic to particulate fractions in OK, but not in LLC-PK1, cells. Furthermore, the translocation of PKCα in OK cells was attenuated by either the phospholipase C inhibitor U-73122 or the soluble guanylate cyclase inhibitor 1H-[1,2,4]oxadiazolo-[4,3-a]quinoxalin-1-one. U-73122 also blunted the inhibitory effect of SNP on Na+-K+-ATPase in OK cells. The phospholipase A2inhibitor AACOCF3 did not blunt the inhibitory effect of SNP on Na+-K+-ATPase in OK cells. AACOCF3 alone, however, also decreased Na+-K+-ATPase activity in OK cells. In conclusion, our results demonstrate that NO activates PKCα in OK, but not in LLC-PK1, cells. The activation of PKCα in OK cells by NO is associated with inhibition of Na+-K+-ATPase.

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