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2000
Volume 11, Issue 5
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

Abstract

Members of several metalloprotease families have been proposed to be involved in non-classical processing of neuroendocrine precursors. Among them, endothelin converting enzyme-2 (ECE-2) is a good candidate since it exhibits a neuroendocrine distribution, intracellular subcellular localization, and an acidic pH optimum. The enzyme is able to generate a number of biologically active peptides from peptide intermediates, suggesting an important role for this enzyme in the biosynthesis of regulatory peptides. These results are consistent with an important role for ECE-2 in the processing of regulatory peptides at non-classical sites.

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/content/journals/ppl/10.2174/0929866043406463
2004-10-01
2025-10-04
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