AMYLOID BETA-PROTEIN AGGREGATION NULLIFIES ITS PATHOLOGICAL PROPERTIES IN CULTURED CEREBROVASCULAR SMOOTH-MUSCLE CELLS

Citation
J. Davissalinas et We. Vannostrand, AMYLOID BETA-PROTEIN AGGREGATION NULLIFIES ITS PATHOLOGICAL PROPERTIES IN CULTURED CEREBROVASCULAR SMOOTH-MUSCLE CELLS, The Journal of biological chemistry, 270(36), 1995, pp. 20887-20890
Citations number
39
Categorie Soggetti
Biology
ISSN journal
00219258
Volume
270
Issue
36
Year of publication
1995
Pages
20887 - 20890
Database
ISI
SICI code
0021-9258(1995)270:36<20887:ABANIP>2.0.ZU;2-3
Abstract
Alzheimer's disease and related disorders are characterized by deposit ion of aggregated amyloid beta-protein (A beta) and accompanying patho logic changes in the neuropil and in the walls of cerebral blood vesse ls. A beta induces neurotoxicity in vitro, and this effect is markedly enhanced when the peptide is preaggregated. Recently, we reported tha t freshly solubilized A beta(1-42) can induce cellular degeneration an d a striking increase in the levels of cellular amyloid beta-protein p recursor and soluble A beta peptide in cultured cerebrovascular smooth muscle cells (Davis-Salinas, J., Saporito-Irwin, S. M., Cotman, C. W. , and Van Nostrand, W. E, (1995) J, Neurochem. 65, 931-934). In the pr esent study, we show that preaggregation of A beta(1-42) abolishes the ability of the peptide to induce these cellular pathologic responses in these cells in vitro. These findings suggest that distinct mechanis ms for A beta-induced cytotoxicity exist for cultured neurons and cere brovascular smooth muscle cells, supporting that different processes m ay be involved in the parenchymal and cerebrovascular pathology of Alz heimer's disease and related disorders.