Abstract
The steady-state level of peptide hormones represents a balance between their biosynthesis and proteolytic processing by convertases and their catabolism by proteolytic enzymes. Low levels of neuropeptide Y, somatostatin and corticotropin-releasing factor, described in Alzheimer disease (AD), were related to a defect in proteolytic processing of their protein precursors. In contrast the abundance of β-amyloid peptides, the major protein constituents of senile plaques is likely related to inefficient catabolism. Therefore, attention is mainly focused on convertases that generate active peptides and counter-regulatory proteases that are involved in their catabolism. Some well-described proteases such as NEP are thought to be involved in β-amyloid catabolism. The search of other possible candidates represents a primary effort in the field. A variety of vascular risk factors such as diabetes, hypertension and arteriosclerosis suggest that the functional vascular defect contributes to AD pathology. It has also been described that β-amyloid peptides potentiate endothelin-1 induced vasoconstriction. In this review, we will critically evaluate evidence relating proteases implicated in amyloid protein precursor proteolytic processing and β-amyloid catabolism.
Keywords: alzheimer, amyloid peptide, proteolytic processing, catabolism, endothelin-1, vasoconstriction
Current Neurovascular Research
Title: Abnormalities of Peptide Metabolism in Alzheimer Disease
Volume: 1 Issue: 4
Author(s): Mai Panchal, Mohamed Rholam and Noureddine Brakch
Affiliation:
Keywords: alzheimer, amyloid peptide, proteolytic processing, catabolism, endothelin-1, vasoconstriction
Abstract: The steady-state level of peptide hormones represents a balance between their biosynthesis and proteolytic processing by convertases and their catabolism by proteolytic enzymes. Low levels of neuropeptide Y, somatostatin and corticotropin-releasing factor, described in Alzheimer disease (AD), were related to a defect in proteolytic processing of their protein precursors. In contrast the abundance of β-amyloid peptides, the major protein constituents of senile plaques is likely related to inefficient catabolism. Therefore, attention is mainly focused on convertases that generate active peptides and counter-regulatory proteases that are involved in their catabolism. Some well-described proteases such as NEP are thought to be involved in β-amyloid catabolism. The search of other possible candidates represents a primary effort in the field. A variety of vascular risk factors such as diabetes, hypertension and arteriosclerosis suggest that the functional vascular defect contributes to AD pathology. It has also been described that β-amyloid peptides potentiate endothelin-1 induced vasoconstriction. In this review, we will critically evaluate evidence relating proteases implicated in amyloid protein precursor proteolytic processing and β-amyloid catabolism.
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Cite this article as:
Panchal Mai, Rholam Mohamed and Brakch Noureddine, Abnormalities of Peptide Metabolism in Alzheimer Disease, Current Neurovascular Research 2004; 1 (4) . https://dx.doi.org/10.2174/1567202043362117
DOI https://dx.doi.org/10.2174/1567202043362117 |
Print ISSN 1567-2026 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5739 |
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