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Articles in PresS, published online ahead of print July 24, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00141.2002
Submitted on March 28, 2002
Accepted on June 24, 2002
participates in activation of store-operated Ca2+ channels in human glomerular mesangial cells
1 Physiology and Biophysics, University of Nebraska Medical Center, Omaha, NE, USA
* To whom correspondence should be addressed. E-mail: rongma{at}unmc.edu.
Protein kinase C (PKC) plays an important role in activating store-operated Ca2+ channels (SOC) in human mesangial cells (MC). The present study was performed to determine the specific isoform(s) of conventional PKC involved in activating SOC in MC. Fura-2 fluorescence ratiometry showed that the thapsigargin-induced Ca2+ entry (equivalent to SOC) was significantly inhibited by 1 µM Go6976 (a specific PKC and ßI inhibitor) and PKCα antisense treatment (2.5 nM for 24-48 hr). However, LY379196 (PKCß inhibitor) and
HBDDE (PKC and 
inhibitor) failed to affect thapsigargin-evoked activation of SOC. Single
channel analysis in the cell attached configuration revealed that Go6976 and PKC antisense significantly depressed thapsigargin-induced activation of SOC. However, LY379196 and HBDDE did not affect the SOC responses. In inside-out patches, application of purified PKC or ßI, but not ßII or , significantly rescued SOC from post-excision rundown. Western blot analysis revealed that thapsigargin evoked a decrease in cytosolic expression with a corresponding increase in membrane expression of PKC and . However, the translocation from cytosol to membranes was not detected for PKCßI or ßII. These results suggest that PKC participates in the intracellular signaling pathway for activating SOC upon release of intracellular stores of Ca2+.
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