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J Biol Chem, Vol. 275, Issue 19, 14025-14030, May 12, 2000

Protein Traffic from the Secretory Pathway to the Endosomal System in Pancreatic beta -Cells*

Mark D. TurnerDagger § and Peter ArvanDagger §

From the Dagger  Diabetes Center, Division of Endocrinology and the § Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, New York 10461

Constitutive-like secretion involves vesicular trafficking corresponding kinetically and biochemically with a post-trans-Golgi network (TGN) origin. In pancreatic beta -cells, the budding of AP-1/clathrin-coated vesicles, a portion of which is derived from immature secretory granules, has been hypothesized to initiate constitutive-like trafficking. However, ~30 min after release of a 20 °C intracellular transport block in pancreatic beta -cells (to synchronize protein egress from the TGN), addition of brefeldin A (BFA) (which inhibits AP-1 recruitment) was reported not to block subsequent constitutive-like secretion. To further explore post-TGN trafficking in pancreatic beta -cell lines, we have followed the fate of pulse-labeled procathepsin B (ProB, a lysosomal proenyzme) after postpulse wortmannin treatment or the BFA treatment described above. We find that continuous wortmannin treatment allows ProB to reach immature secretory granules but inhibits its egress from maturing granules. Remarkably, BFA treatment causes augmented unstimulated secretion of newly synthesized ProB that is not paralleled by insulin. This effect requires a delay of 25-35 min after release from the 20 °C block. Further, when ProB delivery to endosomes is inhibited, its BFA-augmented secretion is eliminated. We hypothesize that the constitutive-like pathway involves an endosomal intermediate.

* This work was supported National Institutes of Health Grant DK48280 (to P. A.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Division of Endocrinology, AECOM, 1300 Morris Park Ave., Bronx, NY 10461. E-mail: arvan@aecom.yu.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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