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participates in activation of store-operated Ca2+ channels in human glomerular mesangial
cells
Department of Physiology and Biophysics, University of Nebraska Medical Center, Omaha, Nebraska 68198-4575
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 Gö-6976 (a specific PKC
and
I inhibitor) and PKC antisense treatment (2.5 nM for 24-48
h). However, LY-379196 (PKC inhibitor) and
2,2',3,3',4,4'-hexahydroxy-1,1'-biphenyl-6,6'-dimethanoldimethyl ether
(HBDDE; PKC and 
inhibitor) failed to affect thapsigargin-evoked activation of SOC. Single-channel analysis in the cell-attached configuration revealed that Gö-6976 and PKC antisense
significantly depressed thapsigargin-induced activation of SOC.
However, LY-379196 and HBDDE did not affect the SOC responses. In
inside-out patches, application of purified PKC or I, but not
II or , significantly rescued SOC from postexcision 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 PKCI or II. These results
suggest that PKC participates in the intracellular signaling pathway
for activating SOC upon release of intracellular stores of
Ca2+.
thapsigargin; patch clamp; fura 2 fluorescence
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