Tissue Plasminogen Activator Requires Plasminogen to Modulate Amyloid-β Neurotoxicity and Deposition
| Autor: | Steven Estus, Sarah Wright, H. Michael Tucker, Russell E. Rydel, Muthoni Kihiko-Ehmann |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Plasmin
Excitotoxicity Pharmacology Biology medicine.disease_cause Biochemistry Tissue plasminogen activator Cellular and Molecular Neuroscience mental disorders medicine Animals Fibrinolysin Enzyme Inhibitors Cells Cultured Neurons Amyloid beta-Peptides Cell Death integumentary system Activator (genetics) T-plasminogen activator Neurotoxicity Drug Synergism Plasminogen medicine.disease Rats nervous system diseases Phenylmethylsulfonyl Fluoride Microscopy Electron Neuroprotective Agents Tissue Plasminogen Activator Toxicity Oxidative stress medicine.drug |
| Zdroj: | Journal of Neurochemistry. 75:2172-2177 |
| ISSN: | 0022-3042 |
| DOI: | 10.1046/j.1471-4159.2000.0752172.x |
| Popis: | Tissue plasminogen (plgn) activator (tPA) modulates neuronal death in models of stroke, excitotoxicity, and oxidative stress. Amyloid-beta (Abeta) appears central to Alzheimer's disease and is neurotoxic to neurons in vitro. Here, we evaluate tPA effects on Abeta toxicity. We report that tPA alone had no effect on Abeta toxicity. However, in combination with plgn, tPA reduced Abeta toxicity in a robust fashion. Moreover, the combined tPA and plgn treatment markedly inhibited Abeta accumulation. The addition of phenylmethylsulfonyl fluoride, a serine protease inhibitor, to a sample of tPA, plgn, and Abeta resulted in a marked reduction of Abeta degradation. We interpret the actions of tPA and plgn within the context of the ability of plasmin to degrade Abeta. |
| Databáze: | OpenAIRE |
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