Hunold, Katja and Weber-Steffens, Dorothea and Runza, Valeria L. and Jensenius, Jens C. and Maennel, Daniela N. (2012) Functional analysis of mouse ficolin-B and detection in neutrophils. IMMUNOBIOLOGY, 217 (10). pp. 982-985. ISSN 0171-2985,
Full text not available from this repository. (Request a copy)Abstract
Ficolins and mannan-binding lectin recognize pathogen-associated molecular patterns and initiate the lectin pathway of complement activation via the associated serine proteases. In contrast to human ficolins and mouse ficolin-A, mouse ficolin-B has been considered incapable of complement activation. Dose-dependent binding of recombinant ficolin-B to immobilized GIcNAc, acetylated BSA, acetylated LDL, and fetuin was detected with ficolin-B-specific monoclonal antibodies. Recombinant ficolin-B bound to immobilized acetylated bovine serum albumin interacted with recombinant human mannan-binding lectin-associated serine protease-2, which led to C4 cleavage, thus demonstrating the capability of ficolin-B to activate the lectin pathway. Ficolin-B-specific monoclonal antibodies identified natural ficolin-B protein in lysates of mouse granulocytes isolated from the bone marrow. These results identify mouse ficolin-B as a functional member of the ficolin family activating complement via the lectin pathway. (c) 2012 Elsevier GmbH. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | LECTIN COMPLEMENT PATHWAY; SERINE PROTEASE-2; ACETYL GROUPS; H-FICOLIN; BINDING; PATTERNS; MOLECULE; MASP-2; MBL; Complement; Lectin pathway; Ficolin; Pattern recognition molecule |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Immunologie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 05 May 2020 11:09 |
| Last Modified: | 05 May 2020 11:09 |
| URI: | https://pred.uni-regensburg.de/id/eprint/18031 |
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