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Vol. 53, Issue 4, 656-662, April 1998
Department of Pharmacology, College of Medicine, State University
of New York Health Science Center at Syracuse, Syracuse, New York
13210-2339
Type I, II, and III inositol-1,4,5-trisphosphate (InsP3)
receptors are expressed selectively in different cell lines and
tissues. We examined whether type I, II, and III InsP3
receptors differ in ligand-binding affinity and whether such
differences influence the sensitivity of Ca2+ stores to
InsP3. Initially, SH-SY5Y human neuroblastoma cells, AR4-2J rat pancreatoma cells, and RINm5F rat insulinoma cells were
studied because these cells express predominantly (>85%) type I, II,
and III receptors, respectively. Immunopurification of receptors from
these cell lines and measurement of InsP3 binding revealed
that the rank order of affinity for InsP3 was type I > type II > type III (binding sites were half-maximally
saturated at 1.5, 2.5, and 22.4 nM InsP3,
respectively). Examination of Ca2+ store mobilization in
permeabilized cells showed that InsP3 was equipotent in
SH-SY5Y and AR4-2J cells but was ~5-fold less potent in RINm5F
cells. In contrast, Ca2+ uptake and
InsP3-independent Ca2+ release were very
similar in the three cell types. The binding affinity of
InsP3 in permeabilized SH-SY5Y, AR4-2J, and RINm5F cells
correlated well with its potency as a Ca2+-mobilizing agent
and with binding affinity to immunopurified type I, II, and III
receptors. Thus, InsP3 receptor binding affinity seems to
influence the potency of InsP3 as a
Ca2+-mobilizing agent. Finally, immunopurification of type
I, II, and III receptors from rat tissues revealed that the affinity differences seen in receptors purified from cultured cells are paralleled in vivo. In combination, the data from cell
lines and rat tissues reveal that type I, II, and III receptors bind
InsP3 with Kd values
of ~1, ~2, and ~40 nM, respectively, and that
the selective expression of a particular receptor type will influence
the sensitivity of cellular Ca2+ stores to
InsP3.
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