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Neurochem Res. 1989 Oct;14(10):933-9.

Evidence for lysosomal processing of amyloid beta-protein precursor in cultured cells.

Author information

1
Department of Neurosciences, University of California, San Diego, School of Medicine, La Jolla 92093.

Abstract

Amyloid beta-protein precursor (ABPP) of Alzheimer's disease (AD) represents a family of proteins which includes the parent protein which generates a small (4 kD) fragment that self-assembles to form amyloid fibrils in AD. Thus, the normal and abnormal proteolysis of ABPP may be directly relevant to AD pathogenesis. We have examined the accumulation of ABPP in cultured rodent and human neuronal cell lines in the presence and absence of a battery of protease inhibitors using immunohistochemistry and Western blot analysis. Here we present evidence for a lysosomal pathway for the turnover of ABPP and discuss the relevance of these results to plaque pathology and abnormal ABPP immunostaining in AD.

PMID:
2514387
DOI:
10.1007/bf00965926
[Indexed for MEDLINE]

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