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.
Keywords: processing enzymes, prohormone convertase, opioid peptides, saas peptides, neuropeptides, peptide neurotransmitters, peptide hormones
Protein & Peptide Letters
Title: Endothelin Converting Enzyme-2: A Processing Enzyme Involved in the Generation of Novel Neuropeptides
Volume: 11 Issue: 5
Author(s): Hui Pan, Nino Mzhavia and Lakshmi A. Devi
Affiliation:
Keywords: processing enzymes, prohormone convertase, opioid peptides, saas peptides, neuropeptides, peptide neurotransmitters, peptide hormones
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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Cite this article as:
Pan Hui, Mzhavia Nino and Devi A. Lakshmi, Endothelin Converting Enzyme-2: A Processing Enzyme Involved in the Generation of Novel Neuropeptides, Protein & Peptide Letters 2004; 11 (5) . https://dx.doi.org/10.2174/0929866043406463
DOI https://dx.doi.org/10.2174/0929866043406463 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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