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J Biol Chem, Vol. 273, Issue 49, 32730-32738, December 4, 1998
From the Department of Neurology and Program in Neuroscience,
Harvard Medical School and Center for Neurologic Diseases, Brigham and
Women's Hospital, Boston, Massachusetts 02115-5716, the
Excessive cerebral accumulation of the 42-residue
amyloid
Insulin-degrading Enzyme Regulates Extracellular Levels of
Amyloid
-Protein by Degradation
, Ben May Institute for Cancer Research, University of
Chicago, Chicago, Illinois 60637, and the § Department of
Biochemistry, University of Kentucky, Chandler Medical Center,
Lexington, Kentucky 40536-0084
-protein (A) is an early and invariant step in the
pathogenesis of Alzheimer's disease. Many studies have examined the
cellular production of A from its membrane-bound precursor,
including the role of the presenilin proteins therein, but almost
nothing is known about how A is degraded and cleared following its
secretion. We previously screened neuronal and nonneuronal cell lines
for the production of proteases capable of degrading naturally secreted A under biologically relevant conditions and concentrations. The
major such protease identified was a metalloprotease released particularly by a microglial cell line, BV-2. We have now purified and
characterized the protease and find that it is indistinguishable from
insulin-degrading enzyme (IDE), a thiol metalloendopeptidase that
degrades small peptides such as insulin, glucagon, and atrial natriuretic peptide. Degradation of both endogenous and synthetic A
at picomolar to nanomolar concentrations was completely inhibited by
the competitive IDE substrate, insulin, and by two other IDE inhibitors. Immunodepletion of conditioned medium with an IDE antibody
removed its A-degrading activity. IDE was present in BV-2 cytosol,
as expected, but was also released into the medium by intact, healthy
cells. To confirm the extracellular occurrence of IDE in
vivo, we identified intact IDE in human cerebrospinal fluid of
both normal and Alzheimer subjects. In addition to its ability to
degrade A, IDE activity was unexpectedly found be associated with a
time-dependent oligomerization of synthetic A at
physiological levels in the conditioned media of cultured cells; this
process, which may be initiated by IDE-generated proteolytic fragments
of A, was prevented by three different IDE inhibitors. We conclude
that a principal protease capable of down-regulating the levels of
secreted A extracellularly is IDE.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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K. Shirotani, S. Tsubuki, N. Iwata, Y. Takaki, W. Harigaya, K. Maruyama, S. Kiryu-Seo, H. Kiyama, H. Iwata, T. Tomita, et al. Neprilysin Degrades Both Amyloid beta Peptides 1-40 and 1-42 Most Rapidly and Efficiently among Thiorphan- and Phosphoramidon-sensitive Endopeptidases J. Biol. Chem., June 8, 2001; 276(24): 21895 - 21901. [Abstract] [Full Text] [PDF]
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E.-S. Song, A. Mukherjee, M. A. Juliano, J. St. Pyrek, J. P. Goodman Jr., L. Juliano, and L. B. Hersh Analysis of the Subsite Specificity of Rat Insulysin Using Fluorogenic Peptide Substrates J. Biol. Chem., January 5, 2001; 276(2): 1152 - 1155. [Abstract] [Full Text] [PDF]
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