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Journal of Biomedicine and Biotechnology
Volume 2012 (2012), Article ID 929803, 12 pages
http://dx.doi.org/10.1155/2012/929803
Research Article

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

1Divisions of Neuroradiology and Nuclear Medicine and Molecular Imaging, Department of Radiology, Massachusetts General Hospital, Harvard Medical School, Boston, MA 02114, USA
2Division of Nuclear Medicine and Molecular Imaging, Department of Radiology, Massachusetts General Hospital, Harvard Medical School, Boston, MA 02114, USA
3Department of Pediatrics, Massachusetts General Hospital, Harvard Medical School, Boston, MA 02114, USA
4Department of Medicine, Boston University School of Medicine, Boston, MA 02118, USA
5Department of Anesthesiology, Perioperative and Pain Medicine, Center for Experimental Therapeutics and Reperfusion Injury, Harvard Institute of Medicine, Harvard Medical School, Boston, MA 02115, USA

Received 15 September 2011; Revised 26 November 2011; Accepted 4 December 2011

Academic Editor: Misao Matsushita

Copyright © 2012 Mykol Larvie et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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 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.