Mouse Ficolin B Has an Ability to Form Complexes with Mannose-Binding Lectin-Associated Serine Proteases and Activate Complement through the Lectin Pathway
Joint Authors
Takahashi, Minoru
Endo, Yuichi
Ishida, Yumi
Fujita, Teizo
Iwaki, Daisuke
Matsushita, Misao
Source
Issue
Vol. 2012, Issue 2012 (31 Dec. 2012), pp.1-7, 7 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2012-02-29
Country of Publication
Egypt
No. of Pages
7
Main Subjects
Abstract EN
Ficolins are thought to be pathogen-associated-molecular-pattern-(PAMP-) recognition molecules that function to support innate immunity.
Like mannose-binding lectins (MBLs), most mammalian ficolins form complexes with MBL-associated serine proteases (MASPs), leading to complement activation via the lectin pathway.
However, the ability of murine ficolin B, a homologue of human M-ficolin, to perform this function is still controversial.
The results of the present study show that ficolin B in mouse bone marrow is an oligomeric protein.
Ficolin B, pulled down using GlcNAc-agarose, contained very low, but detectable, amounts of MASP-2 and small MBL-associated protein (sMAP) and showed detectable C4-deposition activity on immobilized N-acetylglucosamine.
These biochemical features of ficolin B were confirmed using recombinant mouse ficolin B produced in CHO cells.
Taken together, these results suggest that like other mammalian homologues, murine ficolin B has an ability to exert its function via the lectin pathway.
American Psychological Association (APA)
Endo, Yuichi& Iwaki, Daisuke& Ishida, Yumi& Takahashi, Minoru& Matsushita, Misao& Fujita, Teizo. 2012. Mouse Ficolin B Has an Ability to Form Complexes with Mannose-Binding Lectin-Associated Serine Proteases and Activate Complement through the Lectin Pathway. BioMed Research International،Vol. 2012, no. 2012, pp.1-7.
https://search.emarefa.net/detail/BIM-991451
Modern Language Association (MLA)
Endo, Yuichi…[et al.]. Mouse Ficolin B Has an Ability to Form Complexes with Mannose-Binding Lectin-Associated Serine Proteases and Activate Complement through the Lectin Pathway. BioMed Research International No. 2012 (2012), pp.1-7.
https://search.emarefa.net/detail/BIM-991451
American Medical Association (AMA)
Endo, Yuichi& Iwaki, Daisuke& Ishida, Yumi& Takahashi, Minoru& Matsushita, Misao& Fujita, Teizo. Mouse Ficolin B Has an Ability to Form Complexes with Mannose-Binding Lectin-Associated Serine Proteases and Activate Complement through the Lectin Pathway. BioMed Research International. 2012. Vol. 2012, no. 2012, pp.1-7.
https://search.emarefa.net/detail/BIM-991451
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-991451