A novel IgM-H-ficolin complement pathway to attack allogenic cancer cells in vitro.

Abstract

The pentameric serum IgMs are critical to immune defense and surveillance through cytotoxicity against microbes and nascent cancer cells. Ficolins, a group of oligomeric lectins with an overall structure similar to C1q and mannose-binding lectin (MBL) participate in microbe infection and apoptotic cell clearance by activating the complement lectin pathway or a primitive opsonophagocytosis. It remains unknown whether serum IgMs interplay with ficolins in cancer immunosurveillance. Here we report a natural cancer killing of different types of cancer cells by sera from a healthy human population mediated by a novel IgM-H-ficolin complement activation pathway. We demonstrate for the first time that H-ficolin bound to a subset of IgMs in positive human sera and IgM-H-ficolin deposited on cancer cells to activate complement attack in cancer cells. Our data suggest that the IgM-H-ficolin -mediated complement activation pathway may be another defensive strategy for human cancer immunosurveillance.

• Authors: Xiaoying Lei, Chaoxu Liu, Kazem Azadzoi, Cuiling Li, Fan Lu, An Xiang, Jianbin Sun, Yanhai Guo, Qingchuan Zhao, Zhen Yan, Jinghua Yang
• Journal: Scientific reports (Sci Rep) Vol. 5 Pg. 7824 (Jan 16 2015) ISSN: 2045-2322 [Electronic] England
• PMID: 25592840 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• FCN3 protein, human
• Glycoproteins
• Immunoglobulin M
• Lectins
• Complement System Proteins

Topics

• Adult
• Aged
• Apoptosis
• Cell Line, Tumor
• Complement Activation
• Complement System Proteins (metabolism)
• Female
• Glycoproteins (chemistry, immunology, metabolism)
• HT29 Cells
• Humans
• Immunoglobulin M (chemistry, immunology, metabolism)
• Lectins (chemistry, immunology, metabolism)
• MCF-7 Cells
• Male
• Microscopy, Electron, Transmission
• Microscopy, Fluorescence
• Middle Aged
• Protein Binding
• Serum (immunology, metabolism)