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Volume 16, Number 15,
Issue of August 1, 1996
pp. 4543-4550
Copyright ©1996 Society for Neuroscience
Phenotypic Alteration of a Human BK (hSlo) Channel by
hSlo Subunit Coexpression: Changes in Blocker
Sensitivity, Activation/Relaxation and Inactivation Kinetics, and
Protein Kinase A Modulation
Received March 7, 1996; revised May 3, 1996; accepted May 7, 1996.
Steven I. Dworetzky,
Christopher G. Boissard,
Janet T. Lum-Ragan,
M. Craig McKay,
Debra J. Post-Munson,
Joanne T. Trojnacki,
Chia-Ping Chang, and
Valentin K. Gribkoff
Central Nervous System Drug Discovery, Bristol-Myers Squibb
Pharmaceutical Research Institute, Wallingford, Connecticut 06492
A human homolog of the large-conductance calcium-activated
potassium (BK) channel  subunit (hSlo) was cloned, and
its effects on a human BK channel (hSlo) phenotype are
reported. Coexpression of hSlo and hSlo, in
both oocytes and human embryonic kidney 293 cells, resulted in
increased Ca2+ sensitivity, marked slowing of BK
channel activation and relaxation, and a significant reduction in slow
inactivation. In addition, coexpression changed the pharmacology of the
BK channel phenotype: hSlo-mediated currents in oocytes were
more sensitive to the peptide toxin iberiotoxin than were
hSlo + hSlo currents, and the potency of
blockade by the alkaloid BK blocker tetrandrine was much greater on
hSlo + hSlo-mediated currents compared with
hSlo currents alone. No significant differences in the
response to charybdotoxin or the BK channel opener NS1619 were
observed. Modulation of BK channel activity by phosphorylation was also
affected by the presence of the hSlo subunit. Application
of cAMP-dependent protein kinase increased
POPEN of hSlo channels, but
decreased POPEN of most hSlo + hSlo channels. Taken together, these altered
characteristics may explain some of the wide diversity of BK channel
phenotypes observed in native tissues.
Key words:
BK channels;
coexpression;
hSlo;
modulation;
channel blockers;
BK phenotypes
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D.H. Cox, J. Cui, and R.W. Aldrich
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M. Hanner, W. A. Schmalhofer, P. Munujos, H.-G. Knaus, G. J. Kaczorowski, and M. L. Garcia
The beta subunit of the high-conductance calcium-activated potassium channel contributes to the high-affinity receptor for charybdotoxin
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A. C. Gerlach, C. A. Syme, L. Giltinan, J. P. Adelman, and D. C. Devor
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M. M. Zarei, N. Zhu, A. Alioua, M. Eghbali, E. Stefani, and L. Toro
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