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Biophys J, November 2000, p. 2509-2525, Vol. 79, No. 5
and
*Department of Molecular Biosciences, School of Veterinary
Medicine, University of California Davis, Davis, California 95616 USA;
Department of Anesthesia Research, Brigham and Women's
Hospital, Boston, Massachusetts 02115 USA; and
Department of Biochemistry and Molecular Biology,
University of Calgary, Alberta, Canada
Of the three known ryanodine receptor (RyR) isoforms
expressed in muscle, RyR1 and RyR2 have well-defined roles in
contraction. However, studies on mammalian RyR3 have been difficult
because of low expression levels relative to RyR1 or RyR2. Using the
herpes simplex virus 1 (HSV-1) helper-free amplicon system, we
expressed either RyR1 or RyR3 in 1B5 RyR-deficient myotubes. Western
blot analysis revealed that RyR1- or RyR3-transduced cells expressed the appropriate RyR isoform of the correct molecular mass. Although RyR1 channels exhibited the expected unitary conductance for
Cs+ in bilayer lipid membranes, 74 of 88 RyR3 channels
exhibited pronounced subconductance behavior. Western blot analysis
with an FKBP12/12.6-selective antibody reveals that differences in gating behavior exhibited by RyR1 and RyR3 may be, in part, the result
of lower affinity of RyR3 for FKBP12. In calcium imaging studies, RyR1
restored skeletal-type excitation-contraction coupling, whereas RyR3
did not. Although RyR3-expressing myotubes were more sensitive to
caffeine than those expressing RyR1, they were much less sensitive to
4-chloro-m-cresol (CMC). In RyR1-expressing cells,
regenerative calcium oscillations were observed in response to caffeine
and CMC but were never seen in RyR3-expressing 1B5 cells. In
[3H]ryanodine binding studies, only RyR1 exhibited
sensitivity to CMC, but both RyR isoforms responded to caffeine. These
functional differences between RyR1 and RyR3 expressed in a mammalian
muscle context may reflect differences in association with accessory proteins, especially FKBP12, as well as structural differences in
modulator binding sites.
Biophys J, November 2000, p. 2509-2525, Vol. 79, No. 5
© 2000 by the Biophysical Society 0006-3495/00/11/2509/17 $2.00
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