scholarly journals A Protein Tyrosine Phosphatase Inhibitor, Sodium Orthovanadate, Causes Parthenogenetic Activation of Pig Oocytes via an Increase in Protein Tyrosine Kinase Activity1

1999 ◽  
Vol 61 (4) ◽  
pp. 900-905 ◽  
Author(s):  
Jae-Hwan Kim ◽  
Hyun-Jin Do ◽  
Wei-Hua Wang ◽  
Zoltan Macháty ◽  
Yong-Mahn Han ◽  
...  
2009 ◽  
Vol 28 (1) ◽  
pp. 25-30 ◽  
Author(s):  
Sei-Heon Jang ◽  
Si Ae Hwang ◽  
Mijin Kim ◽  
Sung-Hae Yun ◽  
Moon-Sook Kim ◽  
...  

2001 ◽  
Vol 281 (4) ◽  
pp. C1188-C1195 ◽  
Author(s):  
Rui-Min Gu ◽  
Yuan Wei ◽  
John R. Falck ◽  
U. Murali Krishna ◽  
Wen-Hui Wang

We have previously demonstrated that the protein level of c-Src, a nonreceptor type of protein tyrosine kinase (PTK), was higher in the renal medulla from rats on a K-deficient (KD) diet than that in rats on a high-K (HK) diet (Wang WH, Lerea KM, Chan M, and Giebisch G. Am J Physiol Renal Physiol 278: F165–F171, 2000). We have now used the patch-clamp technique to investigate the role of PTK in regulating the apical K channels in the medullary thick ascending limb (mTAL) of the rat kidney. Inhibition of PTK with herbimycin A increased NP o, a product of channel number ( N) and open probability ( P o), of the 70-pS K channel from 0.12 to 0.42 in the mTAL only from rats on a KD diet but had no significant effect in tubules from animals on a HK diet. In contrast, herbimycin A did not affect the activity of the 30-pS K channel in the mTAL from rats on a KD diet. Moreover, addition of N-methylsulfonyl-12,12-dibromododec-11-enamide, an agent that inhibits the cytochrome P-450-dependent production of 20-hydroxyeicosatetraenoic acid, further increased NP o of the 70-pS K channel in the presence of herbimycin A. Furthermore, Western blot detected the presence of PTP-1D, a membrane-associated protein tyrosine phosphatase (PTP), in the renal outer medulla. Inhibition of PTP with phenylarsine oxide (PAO) decreased NP o of the 70-pS K channel in the mTAL from rats on a HK diet. However, PAO did not inhibit the activity of the 30-pS K channel in the mTAL. The effect of PAO on the 70-pS K channel was due to indirectly stimulating PTK because pretreatment of the mTAL with herbimycin A abolished the inhibitory effect of PAO. Finally, addition of exogenous c-Src reversibly blocked the activity of the 70-pS K channel in inside-out patches. We conclude that PTK and PTP have no effect on the low-conductance K channels in the mTAL and that PTK-induced tyrosine phosphorylation inhibits, whereas PTP-induced tyrosine dephosphorylation stimulates, the apical 70-pS K channel in the mTAL.


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