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  • Title: Carboxypeptidase E does not mediate von Willebrand factor targeting to storage granules.
    Author: Methia N, Denis CV, Wagner DD.
    Journal: Eur J Cell Biol; 1999 Dec; 78(12):884-91. PubMed ID: 10669107.
    Abstract:
    Sorting of von Willebrand factor precursor (pro-vWf) from the trans-Golgi network to secretory granules (Weibel-Palade bodies) is critical for its conversion to the biologically active highly multimeric form, as well as for regulated secretion by the endothelial cells. When expressed in hormone-secretory cells, vWf is also recognized as a stored protein and is directed to storage granules. Recently, carboxypeptidase E (CPE) was proposed as a granular sorting receptor for prohormones (Cool et al., Cell 88: 73, 1997). To explore whether CPE is also involved in pro-vWf sorting, we initially examined its expression in human umbilical vein endothelial cells. A specific message for CPE and the protein itself were detected making it a plausible candidate as a targeting receptor for vWf in endothelium. To investigate this possibility, we used mice lacking CPE. The highly multimeric forms, subunit composition and plasma levels of vWf in CPE-deficient mice were similar to those of their wild-type littermates. vWf was also found in alpha-granules of platelets and in Weibel-Palade bodies of endothelial cells obtained from the CPE-deficient mice. Furthermore, vWf was released from the cultured CPE-deficient endothelial cells after stimulation with a secretagogue. We conclude that CPE is not essential for sorting vWf to the regulated secretory pathway. Thus, a CPE-independent mechanism must exist for protein sorting to storage granules.
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