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J Biol Chem, Vol. 273, Issue 9, 5013-5019, February 27, 1998
From the § Department of Pathology, The University of
Melbourne, Parkville, 3052, Australia and The Mental Health Research
Institute of Victoria, Parkville 3052, Australia, the ¶ Genetics
and Aging Unit, Harvard Medical School, Massachusetts General Hospital,
Boston, Massachusetts 02114, and the Although a number of studies have examined
amyloid precursor protein (APP) mRNA levels in Alzheimer's disease
(AD), no clear consensus has emerged as to whether the levels of
transcripts for isoforms containing a Kunitz protease inhibitory
(KPI)-encoded region are increased or decreased in AD. Here we compare
AD and control brain for the relative amounts of APP protein containing KPI to APP protein lacking this domain. APP protein was purified from
the soluble subcellular fraction and Triton X-100 membrane pellet
extract of one hemisphere of AD (n = 10), normal
(n = 7), and neurological control (n = 5) brains. The amount of KPI-containing APP in the purified protein
samples was determined using two independent assay methods. The first
assay exploited the inhibitory action of KPI-containing APP on trypsin.
The second assay employed reflectance analysis of Western blots. The
proportion of KPI-containing forms of APP in the soluble subcellular
fraction of AD brains is significantly elevated (p < 0.01) compared with controls. Species containing a KPI domain comprise
32-41 and 76-77% of purified soluble APP from control and AD brains,
respectively. For purified membrane-associated APP, 72-77 and 65-82%
of control and AD samples, respectively, contain a KPI domain. Since
KPI-containing species of APP may be more amyloidogenic (Ho, L.,
Fukuchi, K., and Yonkin, S. G. (1996) J. Biol.
Chem. 271, 30929-30934), our findings support an imbalance of
isoforms as one possible mechanism for amyloid deposition in sporadic
AD.
Relative Increase in Alzheimer's Disease of Soluble Forms of
Cerebral A
Amyloid Protein Precursor Containing the Kunitz Protease
Inhibitory Domain
,, and Center for Molecular
Biology, The University of Heidelberg, Heidelberg, Germany
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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