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J. Biol. Chem., Vol. 268, Issue 10, 7290-7297, 04, 1993
LY Bourguignon, H Jin, N Iida, NR Brandt and SH Zhang
Mouse T-lymphoma cells contain a unique type of internal vesicle which
bands at the relatively light density of 1.07 g/cc. These vesicles do not
contain any detectable Golgi, endoplasmic reticulum, plasma membrane, or
lysosomal marker protein activities. Binding of [3H]inositol
1,4,5-trisphosphate (IP3) to these internal vesicles reveals the presence
of a single, high affinity class of IP3 receptor with a dissociation
constant (Kd) of 1.6 +/- 0.3 nM. Using a panel of monoclonal and polyclonal
antibodies against IP3 receptor, we have established that the IP3 receptor
(approximately 260 kDa) displays immunological cross-reactivity with the
rat brain IP3 receptor. Polymerase chain reaction analysis of first-strand
cDNAs from both mouse T-lymphoma cells and rat brain tissues reveals that
the IP3 receptor transcript in mouse T-lymphoma cells belongs to the short
form (non-neuronal form) and not the long form (neuronal form) detected in
rat brain tissue. Scatchard plot analysis shows that high affinity binding
occurs between ankyrin and the IP3 receptor with a Kd of 0.2 nM. Most
importantly, the binding of ankyrin to the light density vesicles
significantly inhibits IP3 binding and IP3-induced internal Ca2+ release.
These findings suggest that the cytoskeleton plays a pivotal role in the
regulation of IP3 receptor-mediated internal Ca2+ release during lymphocyte
activation.
The involvement of ankyrin in the regulation of inositol 1,4,5- trisphosphate receptor-mediated internal Ca2+ release from Ca2+ storage vesicles in mouse T-lymphoma cells
Department of Cell Biology and Anatomy, School of Medicine, University of Miami, Florida 33101.
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