Synthetic Alzheimer amyloid beta/A4 peptides enhance production of complement C3 component by cultured microglial cells
Autor: | Kazuhiko Ikeda, Seiichi Haga, T. Ishii, Maroto Sato |
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Rok vydání: | 1993 |
Předmět: |
Lipopolysaccharides
Amyloid Amyloid beta Immunoprecipitation Fluorescent Antibody Technique Peptide Mice Phagocytosis Extracellular medicine Animals Senile plaques Molecular Biology Cells Cultured chemistry.chemical_classification Mice Inbred BALB C Amyloid beta-Peptides Microglia biology General Neuroscience Macrophages Granulocyte-Macrophage Colony-Stimulating Factor Complement C3 Precipitin Tests Stimulation Chemical medicine.anatomical_structure Biochemistry chemistry Cell culture Parathyroid Hormone Astrocytes biology.protein Electrophoresis Polyacrylamide Gel Indicators and Reagents Neurology (clinical) Neuroglia Developmental Biology |
Zdroj: | Brain research. 601(1-2) |
ISSN: | 0006-8993 |
Popis: | Primary microglial cultures prepared from newborn mice showed the production and release of the third component of complement (C3). Newly synthesized [35S]methionine-labelled C3 was purified by immunoprecipitation using anti-C3-antibody. C3 was detected by SDS-PAGE and fluoroaraphy of the immunoprecipitated protein from cell lysates as a 195 kDa band, and from the supernatants of cultures as two major bands corresponding to the C3 alpha-chain (125 kDa) and beta-chain (75 kDa), consistent with known C3 characteristics. Increased biosynthesis of C3 was elicited by endotoxin lipopolysaccharide (LPS). Further, the synthesis of C3 was increased 5-10-fold in response to various synthetic peptides corresponding to the amyloid beta/A4 protein, which is the main constituent of extracellular amyloid deposits in Alzheimer's disease (AD). The increased synthesis of C3 was shown to be dose dependent at concentrations of beta/A4 peptide ranging from 10 micrograms/ml to 50 micrograms/ml. These results suggest that complement components found previously in amyloid deposits may be partly derived from reactive microglia preferentially associated with senile plaques in AD brain. |
Databáze: | OpenAIRE |
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