Specific patterns of amyloid β-protein precursor isoform secretion and proteolysis in cultured human cells
| Autor: | Michael F Murphy, Steven L. Wagner, Robert Steven Siegel, Blake A. Rowe, Thomas S. Vedvick |
|---|---|
| Rok vydání: | 1996 |
| Předmět: | |
| Zdroj: | Amyloid. 3:100-109 |
| ISSN: | 1744-2818 1350-6129 |
| DOI: | 10.3109/13506129609014361 |
| Popis: | A characteristic neuropathologic feature of Alzheimer c disease is an abundance of brain-localized neuritic plaques. These plaques are identified as areas of degenerating nerve terminals surrounding cores of aggregated and insoluble fibrils of amyloid β-protein (Aβ). Aβ is generated by proteolytic cleavage of a large precursor protein, the amyloid β-protein precursor (AβPP). In this study, soluble AβPPs (sAβPPs) secreted by human cell lines originating from different tissues were characterized. Various human cell types were shown to secrete different characteristic isoforms of AβPP. Peripheral cells (i.e., fibroblasts and keratinocytes) secreted only the soluble derivative of the 770-amino acid isoform (sAβPP770). In contrast, cells derived from the central and peripheral nervous system (i.e., neumblastoma and glioblastoma) secreted the soluble derivative of the 751-amino acid isoform (sAβPP751), while the 695-amino acid isoform (sAβPP695) was secreted exclusively by neuronal-type cells. We have also dete... |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|