Inhibition of translational initiation by metalloendoprotease antagonists. Evidence for involvement of sequestered Ca super(2+) stores

Synthetic oligopeptide inhibitors of metalloendoprotease activity have been shown to block membrane fusion events, to slow transport of secretory proteins from the endoplasmic reticulum (ER) to the Golgi, and to perturb Ca super(2+) homeostasis. Effects of such agents on translational activity, whic...

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Veröffentlicht in:The Journal of biological chemistry 1991-01, Vol.266 (11), p.7037-7043
Hauptverfasser: Brostrom, MA, Prostko, C R, Gmitter-Yellen, D, Grandison, L J, Kuznetsov, G, Wong, Wai Lam, Brostrom, C O
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Sprache:eng
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Zusammenfassung:Synthetic oligopeptide inhibitors of metalloendoprotease activity have been shown to block membrane fusion events, to slow transport of secretory proteins from the endoplasmic reticulum (ER) to the Golgi, and to perturb Ca super(2+) homeostasis. Effects of such agents on translational activity, which requires Ca super(2+) sequestered putatively within the ER, were examined in this study. It is concluded that metalloendoprotease antagonists suppress translational initiation as a consequence of their capacity to mobilize sequestered Ca super(2+) stores.
ISSN:0021-9258