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Department of Microbiology and Immunology, University of Leicester, Leicester, United Kingdom;
Department of Medical Microbiology and Immunology, University of Aarhus, Aarhus, Denmark;
Theodor-Kocher-Institute, University of Bern, Bern, Switzerland; and
§
Institute for Anatomy and Cell Biology, University of Marburg, Marburg, Germany
Mannan-binding lectin (MBL) forms a multimolecular complex with at least two MBL-associated serine proteases, MASP-1 and MASP-2. This complex initiates the MBL pathway of complement activation by binding to carbohydrate structures present on bacteria, yeast, and viruses. MASP-1 and MASP-2 are composed of modular structural motifs similar to those of the C1q-associated serine proteases C1r and C1s. Another protein of 19 kDa with the same N-terminal sequence as the 76-kDa MASP-2 protein is consistently detected as part of the MBL/MASP complex. In this study, we present the primary structure of this novel MBL-associated plasma protein of 19 kDa, MAp19, and demonstrate that MAp19 and MASP-2 are encoded by two different mRNA species generated by alternative splicing/polyadenylation from one structural gene.
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C.-B. Chen and R. Wallis Stoichiometry of Complexes between Mannose-binding Protein and Its Associated Serine Proteases. DEFINING FUNCTIONAL UNITS FOR COMPLEMENT ACTIVATION J. Biol. Chem., July 6, 2001; 276(28): 25894 - 25902. [Abstract] [Full Text] [PDF]
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V. Rossi, S. Cseh, I. Bally, N. M. Thielens, J. C. Jensenius, and G. J. Arlaud Substrate Specificities of Recombinant Mannan-binding Lectin-associated Serine Proteases-1 and -2 J. Biol. Chem., October 26, 2001; 276(44): 40880 - 40887. [Abstract] [Full Text] [PDF]
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