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Biophys J, March 1998, p. 1263-1277, Vol. 74, No. 3
*Programa de Fisiología y Biofísica and
#Programa de Biología Molecular y Celular,
The calcium dependence of ryanodine-sensitive single
calcium channels was studied after fusing with planar lipid bilayers sarcoendoplasmic reticulum vesicles isolated from excitable tissues. Native channels from mammalian or amphibian skeletal muscle displayed three different calcium dependencies, cardiac (C), mammalian skeletal (MS), and low fractional open times (low
Po), as reported for channels from brain
cortex. Native channels from cardiac muscle presented only the MS and C
dependencies. Channels with the MS or low Po
behaviors showed bell-shaped calcium dependencies, but the latter had
fractional open times of <0.1 at all [Ca2+]. Channels
with C calcium dependence were activated by [Ca2+] < 10 µM and were not inhibited by increasing cis
[Ca2+] up to 0.5 mM. After oxidation with
2,2'-dithiodipyridine or thimerosal, channels with low
Po or MS dependencies increased their
activity. These channels modified their calcium dependencies sequentially, from low Po to MS and C, or
from MS to C. Reduction with glutathione of channels with C dependence
(native or oxidized) decreased their fractional open times in 0.5 mM
cis [Ca2+], from near unity to 0.1-0.3.
These results show that all native channels displayed at least two
calcium dependencies regardless of their origin, and that these changed
after treatment with redox reagents.
Biophys J, March 1998, p. 1263-1277, Vol. 74, No. 3
© 1998 by the Biophysical Society 0006-3495/98/03/1263/15 $2.00
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