Mannose-Binding Lectin Binds to Amyloid β Protein and Modulates Inflammation

Mannose-binding lectin (MBL), a soluble factor of the innate immune system, is a pattern recognition molecule with a number of known ligands, including viruses, bacteria, and molecules from abnormal self tissues. In addition to its role in immunity, MBL also functions in the maintenance of tissue ho...

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Bibliographic Details
Published in:Journal of biomedicine & biotechnology 2012-01, Vol.2012 (2012), p.1-12
Main Authors: Larvie, Mykol, Shoup, Timothy, Chang, Wei-Chuan, Chigweshe, Lorencia, Hartshorn, Kevan, White, Mitchell R., Stahl, Gregory L., Elmaleh, David R., Takahashi, Kazue
Format: Article
Language:English
Subjects:
Amyloid beta-Peptides - chemistry
Amyloid beta-Peptides - immunology
Amyloid beta-Peptides - metabolism
Animals
Calcium
Calcium - metabolism
Cytokines - metabolism
Dose-Response Relationship, Drug
Humans
Inflammation - immunology
Inflammation - metabolism
Inflammation - microbiology
Influenza A virus - immunology
Macrophages - immunology
Macrophages - metabolism
Mannose-Binding Lectin - genetics
Mannose-Binding Lectin - immunology
Mannose-Binding Lectin - metabolism
Mice
Mice, Inbred C57BL
Mice, Knockout
Models, Biological
Polysaccharides - metabolism
Polysaccharides - pharmacology
Staphylococcus aureus - immunology
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Summary:Mannose-binding lectin (MBL), a soluble factor of the innate immune system, is a pattern recognition molecule with a number of known ligands, including viruses, bacteria, and molecules from abnormal self tissues. In addition to its role in immunity, MBL also functions in the maintenance of tissue homeostasis. We present evidence here that MBL binds to amyloid β peptides. MBL binding to other known carbohydrate ligands is calcium-dependent and has been attributed to the carbohydrate-recognition domain, a common feature of other C-type lectins. In contrast, we find that the features of MBL binding to Aβ are more similar to the reported binding characteristics of the cysteine-rich domain of the unrelated mannose receptor and therefore may involve the MBL cysteine-rich domain. Differences in MBL ligand binding may contribute to modulation of inflammatory response and may correlate with the function of MBL in processes such as coagulation and tissue homeostasis.
ISSN:1110-7243
1110-7251
DOI:10.1155/2012/929803