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(Received for publication, September 28, 1995; and in revised form, December 27, 1995) Although the RNA for the third isoform (Ryr3) of ryanodine
receptor (RyR), a Ca
Volume 271,
Number 9,
Issue of March 1, 1996 pp. 5079-5084
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
release channel, is detected in
specific regions of mammalian brain, little is known about the protein.
We investigated Ryr3 in rabbit brain, using an antibody raised against
the synthetic peptide corresponding to amino acid sequence
4375-4387 of rabbit Ryr3, the homologue of bullfrog
-RyR.
The antibody which reacted with bullfrog -RyR, but not with the
other isoforms, Ryr1 or Ryr2, specifically precipitated a single
polypeptide from rabbit brain microsomes having a size similar to
-RyR. Sucrose gradient ultracentrifugation revealed that Ryr3
forms a homotetramer, as true of the other isoforms. Being consistent
with the distribution of its RNA, Ryr3 was abundantly expressed in
hippocampus, corpus striatum, and diencephalon. Ryr3 demonstrated
Ca-dependent [
H]ryanodine
binding, and caffeine increased its Ca sensitivity.
The Ca
sensitivity of Ryr3 was also enhanced in a
medium containing 1 M NaCl, as observed with
-RyR.
[H]Ryanodine binding gave an estimate of Ryr3
which would be only 2% or less of total RyR in rabbit brain. These
results confirm the expression of functional Ryr3 in mammalian brain
which is similar to nonmammalian -RyR.
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