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Volume 272, Number 25, Issue of June 20, 1997 pp. 15687-15696
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Ryanodine Receptor Type III (Ry₃R) Identification In Mouse Parotid Acini
PROPERTIES AND MODULATION OF [³H]RYANODINE-BINDING SITES

(Received for publication, October 11, 1996, and in revised form, February 10, 1997)

Dennis H. DiJulio , Eileen L. Watson ^§ , Isaac N. Pessah , Kerry L. Jacobson , Sabrina M. Ott , Edmond D. Buck and Jean C. Singh

From the Departments of  Oral Biology and ^§ Pharmacology, University of Washington, Seattle, Washington 98195 and the  Department of Molecular Biosciences, University of California, Davis, California 95616

Immunoblot analysis and [³H]ryanodine binding were used to characterize and identify ryanodine receptors (RyRs) in nonexcitable mouse parotid acini. Western analysis revealed ryanodine receptor type III (Ry₃R) to be the only detectable isoform in parotid microsomal membranes. Binding of [³H]ryanodine to microsomal fractions was dependent on Ca²⁺, salt, pH, and temperature. At 23 °C, and in the presence of 0.5 M KCl and 100 µM Ca²⁺, [³H]ryanodine bound specifically to membranes with high affinity (K_d = 6 nM); maximum binding capacity (B_max) was 275 fmol/mg protein. Mg²⁺ and ruthenium red inhibited [³H]ryanodine binding (IC₅₀ = 1.4 mM and 0.5 µM, respectively). 4-Chloro-3-ethylphenol enhanced the binding of [³H]ryanodine 2.5-fold; whereas ATP and caffeine were much less efficacious toward activating Ry₃R (56% and 18% maximal enhancement, respectively). Bastadin, a novel modulator of the 12-kDa FK506 binding protein·RyR complex, increased [³H]ryanodine binding 3-4-fold by enhancing K_d. The immunosuppressant FK506 enhanced [³H]ryanodine receptor occupancy at >100 µM and antagonized the action of bastadin, suggesting that an immunophilin modulates Ry₃R in parotid acini. These results suggest that Ry₃R may play an important role in Ca²⁺ homeostasis in mouse parotid acini.

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