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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2001-6-6
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pubmed:abstractText |
Microglial ingestion of the amyloid beta-peptide (Abeta) has been viewed as a therapeutic target in Alzheimer's disease, in that approaches that enhance clearance of Abeta relative to its production are predicted to result in decreased senile plaque formation, a proposed contributor to neuropathology. In vitro, scavenger receptors mediate ingestion of fibrillar Abeta (fAbeta) by microglia. However, the finding that cerebral amyloid deposition in a transgenic mouse model of Alzheimer's disease was diminished by inoculation with synthetic Abeta has suggested a possible therapeutic role for anti-Abeta Ab-mediated phagocytosis. Microglia also express C1qR(P), a receptor for complement protein C1q, ligation of which in vitro enhances phagocytosis of immune complexes formed with IgG levels below that required for optimal FcR-mediated phagocytosis. The data presented here demonstrate FcR-dependent ingestion of Abeta-anti-Abeta complexes (IgG-fAbeta) by microglia that is a function of the amount of Ab used to form immune complexes. In addition, C1q incorporated into IgG-fAbeta enhanced microglial uptake of these complexes when they contained suboptimal levels of anti-Abeta Ab. Mannose binding lectin and lung surfactant protein A, other ligands of C1qR(P), also enhanced ingestion of suboptimally opsonized IgG-fAbeta, whereas control proteins did not. Our data suggest that C1qR(P)-mediated events may promote efficient ingestion of Abeta at low Ab titers, and this may be beneficial in paradigms that seek to clear amyloid via FcR-mediated mechanisms by minimizing the potential for destructive Ab-induced complement-mediated processes.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Antigen-Antibody Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD44,
http://linkedlifedata.com/resource/pubmed/chemical/C1QBP protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/C1qbp protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/C1qbp protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Collagen,
http://linkedlifedata.com/resource/pubmed/chemical/Complement C1q,
http://linkedlifedata.com/resource/pubmed/chemical/Ferritins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Poly I,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Complement,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Lipoprotein,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Scavenger,
http://linkedlifedata.com/resource/pubmed/chemical/Scarb1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Scavenger Receptors, Class B,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin,
http://linkedlifedata.com/resource/pubmed/chemical/amyloid beta-protein (1-42),
http://linkedlifedata.com/resource/pubmed/chemical/complement 1q receptor,
http://linkedlifedata.com/resource/pubmed/chemical/fucoidan
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0022-1767
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
166
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7496-503
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:11390503-Amyloid beta-Peptides,
pubmed-meshheading:11390503-Animals,
pubmed-meshheading:11390503-Antibodies,
pubmed-meshheading:11390503-Antigen-Antibody Complex,
pubmed-meshheading:11390503-Antigens, CD44,
pubmed-meshheading:11390503-Carrier Proteins,
pubmed-meshheading:11390503-Cell Line,
pubmed-meshheading:11390503-Cells, Cultured,
pubmed-meshheading:11390503-Centrifugation,
pubmed-meshheading:11390503-Collagen,
pubmed-meshheading:11390503-Complement C1q,
pubmed-meshheading:11390503-Ferritins,
pubmed-meshheading:11390503-Flow Cytometry,
pubmed-meshheading:11390503-Humans,
pubmed-meshheading:11390503-Ligands,
pubmed-meshheading:11390503-Membrane Glycoproteins,
pubmed-meshheading:11390503-Membrane Proteins,
pubmed-meshheading:11390503-Microglia,
pubmed-meshheading:11390503-Mitochondrial Proteins,
pubmed-meshheading:11390503-Peptide Fragments,
pubmed-meshheading:11390503-Phagocytosis,
pubmed-meshheading:11390503-Poly I,
pubmed-meshheading:11390503-Polysaccharides,
pubmed-meshheading:11390503-Rats,
pubmed-meshheading:11390503-Receptors, Complement,
pubmed-meshheading:11390503-Receptors, Immunologic,
pubmed-meshheading:11390503-Receptors, Lipoprotein,
pubmed-meshheading:11390503-Receptors, Scavenger,
pubmed-meshheading:11390503-Scavenger Receptors, Class B,
pubmed-meshheading:11390503-Serum Albumin
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pubmed:year |
2001
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pubmed:articleTitle |
Antibody-mediated phagocytosis of the amyloid beta-peptide in microglia is differentially modulated by C1q.
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pubmed:affiliation |
Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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