Mannose-Binding Lectin Binds to Amyloid \(\beta\) Protein and Modulates Inflammation
View/ Open
Author
Chang, Wei-Chuan
Chigweshe, Lorencia
Hartshorn, Kevan
White, Mitchell R.
Published Version
https://doi.org/10.1155/2012/929803Metadata
Show full item recordCitation
Larvie, Mykol, Timothy Shoup, Wei-Chuan Chang, Lorencia Chigweshe, Kevan Hartshorn, Mitchell R. White, Gregory L. Stahl, David R. Elmaleh, and Kazue Takahashi. 2012. Mannose-binding lectin binds to amyloid \(\beta\) protein and modulates inflammation. Journal of Biomedicine and Biotechnology 2012:929803.Abstract
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 \(\beta\) 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 A\(\beta\) 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.Other Sources
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3322523/pdf/Terms of Use
This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAACitable link to this page
http://nrs.harvard.edu/urn-3:HUL.InstRepos:10347163
Collections
- HMS Scholarly Articles [17917]
Contact administrator regarding this item (to report mistakes or request changes)