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Volume 272, Number 19, Issue of May 9, 1997 pp. 12454-12461
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Angiotensin II-induced Down-regulation of Inositol Trisphosphate Receptors in WB Rat Liver Epithelial Cells
EVIDENCE FOR INVOLVEMENT OF THE PROTEASOME PATHWAY

(Received for publication, November 20, 1996, and in revised form, January 22, 1997)

From the Department of Pathology, Thomas Jefferson University School of Medicine, Philadelphia, Pennsylvania 19107

Chronic stimulation of WB rat liver epithelial cells by angiotensin II (Ang II) resulted in the down-regulation of both type I and type III myo-inositol 1,4,5-trisphosphate receptors (IP₃Rs). Stimulation with vasopressin, bradykinin, epidermal growth factor, or 12-O-tetradecanoylphorbol-13-acetate was without effect. Ang II-induced down-regulation of IP₃Rs could be detected within 2 h and resulted in an inhibition of IP₃-induced Ca²⁺ release from permeabilized cells. IP₃R down-regulation was reversible, and both homo- and heterooligomers of IP₃Rs were equally susceptible to Ang II-induced degradation. Chloroquine and NH₄Cl increased the basal levels of IP₃Rs by 2-fold, suggesting that the basal turnover of IP₃Rs occurs via a lysosomal pathway. However, Ang II-induced degradation of IP₃R was not affected by these inhibitors, suggesting that stimulated degradation of IP₃Rs occurs via a non-lysosomal pathway. The cysteine protease and proteasomal inhibitor N-acetyl-Leu-Leu-norleucinal completely prevented Ang II-mediated down-regulation of IP₃Rs, whereas the structural analog N-acetyl-Leu-Leu-methioninal was without effect. Lactacystin, a highly specific proteasome inhibitor, also blocked Ang II-mediated IP₃R degradation. Stimulation with Ang II increased the amount of IP₃R immunoprecipitated by anti-ubiquitin antibodies. We conclude that Ang II-stimulated IP₃R degradation involves enhanced ubiquitination of the protein and degradation by the proteasome pathway.

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