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1 in activation of human mesangial BK channels by cGMP-kinase
1 Department of Physiology and Biophysics, University of Nebraska Medical Center, Omaha, NE, USA
* To whom correspondence should be addressed. E-mail: ssansom{at}unmc.edu.
In vascular smooth muscle and glomerular mesangial cells, relaxing agents such as nitric oxide and atrial natriuretic peptide activate large conductance Ca2+-activated K+ channels (BK) via the cGMP-kinase pathway. BK are comprised of pore-forming 
subunits, encoded by the slopoke gene (Slo), and one of four cell-specific accessory 
subunits (H1-4). We used patch clamp analysis to determine the influence of H1, 2 and 4 on activation of human mesangial BK by cGMP-kinase. We found that HEK 293 cells, co-expressing hSlo with either H1 or H2, contained single BK currents activated by db-cGMP in cell attached patches. However, recombinant BK were not activated by db-cGMP when hSlo was expressed alone or with H4. DNA-RNA hybridization revealed that mesangial cells contained mRNA for H1 but not H2 or H4. The BK response to db-cGMP was decreased when H1 antisense, but not scrambled, oligonucleotides were incorporated into mesangial cells. Western Blot analysis showed that H1 antisense inhibited the amount of H1-V5 fusion protein expressed in HEK293 cells by approximately 50%. These results show that mesangial cells contain H1, a BK accessory protein, which confers activation of BK by cGMP-kinase.
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