Amyloid beta-protein aggregation nullifies its pathologic properties in cultured cerebrovascular smooth muscle cells
| Autor: | J Davis-Salinas, W E Van Nostrand |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
chemistry.chemical_classification
Amyloid beta-Peptides Amyloid biology Amyloid beta P3 peptide Neurotoxicity Peptide Cell Biology Protein aggregation medicine.disease Biochemistry In vitro Muscle Smooth Vascular Cell biology medicine.anatomical_structure chemistry Alzheimer Disease Immunology biology.protein Neuropil medicine Humans Molecular Biology Cells Cultured |
| Zdroj: | The Journal of biological chemistry. 270(36) |
| ISSN: | 0021-9258 |
| Popis: | Alzheimer's disease and related disorders are characterized by deposition of aggregated amyloid beta-protein (A beta) and accompanying pathologic changes in the neuropil and in the walls of cerebral blood vessels. A beta induces neurotoxicity in vitro, and this effect is markedly enhanced when the peptide is preaggregated. Recently, we reported that freshly solubilized A beta 1-42 can induce cellular degeneration and a striking increase in the levels of cellular amyloid beta-protein precursor 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 present 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 mechanisms for A beta-induced cytotoxicity exist for cultured neurons and cerebrovascular smooth muscle cells, supporting that different processes may be involved in the parenchymal and cerebrovascular pathology of Alzheimer's disease and related disorders. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|