Abstract
Several specific topics on recent findings in the studies of memapsin 2 (β-secretase) are discussed in this article. New structural evidence on memapsin 2 has pointed to the structural basis of flap opening. Such a mechanism is thought to participate in the substrate sequence selection during the cellular function. Another potentially important area is the intracellular transport of memapsin 2. Here we discuss the involvement of APP in memapsin 2 endocytosis and the GGA proteins in recycling the protease back to the cell surface. These mechanisms may be connected with the cellular regulation of neuronal activity through the regulation of memapsin 2 activity and Aβ production.
Keywords: alzheimers disease, secretase, memapsin 2, neuronal activity, amyloid
Current Alzheimer Research
Title: Recent Developments on the Studies of Human Memapsin 2 (β-Secretase)
Volume: 2 Issue: 2
Author(s): Jordan Tang, Xiangyang He, Xianping Huang and Lin Hong
Affiliation:
Keywords: alzheimers disease, secretase, memapsin 2, neuronal activity, amyloid
Abstract: Several specific topics on recent findings in the studies of memapsin 2 (β-secretase) are discussed in this article. New structural evidence on memapsin 2 has pointed to the structural basis of flap opening. Such a mechanism is thought to participate in the substrate sequence selection during the cellular function. Another potentially important area is the intracellular transport of memapsin 2. Here we discuss the involvement of APP in memapsin 2 endocytosis and the GGA proteins in recycling the protease back to the cell surface. These mechanisms may be connected with the cellular regulation of neuronal activity through the regulation of memapsin 2 activity and Aβ production.
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Cite this article as:
Tang Jordan, He Xiangyang, Huang Xianping and Hong Lin, Recent Developments on the Studies of Human Memapsin 2 (β-Secretase), Current Alzheimer Research 2005; 2 (2) . https://dx.doi.org/10.2174/1567205053585800
DOI https://dx.doi.org/10.2174/1567205053585800 |
Print ISSN 1567-2050 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5828 |
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