Disease relevance of Masp1

• Here we investigate the C components required for the C activation induced by mouse RaRF, by using hemolysis of Ra LPS-coated E (ELPS) as a model system [1].

High impact information on Masp1

• Hence, although the RaRF protease and C1s have similar structures and play similar roles in C activation, they also display clear differences in substrate range and in the details of their substrate recognition mechanisms [2].
• Finally, we found that RaRF does not cleave sex-limited protein even at a level 100-fold higher than necessary for C4 cleavage [2].
• In this study, we examined the substrate specificity of mouse RaRF by assaying its ability to cleave C components C3, C4, and C5, and its activity against the murine C4 isotype, sex-limited protein [2].
• Ra-reactive factor (RaRF) is a serum bactericidal factor whose function seems to be to activate C in a manner similar to that of C1, but with activation triggered by binding to bacterial polysaccharides instead of to immune complexes [2].
• Ra-reactive factor (RaRF), a C-dependent bactericidal factor in mice, is composed of one polysaccharide-binding component and one C4/C2-activating component [3].

Biological context of Masp1

• Human and mouse genes for the complement-activating component (P100) of Ra-reactive factor, a novel bactericidal factor (CRARF and Crarf), were mapped to R-banded metaphase chromosomes by fluorescence in situ hybridization with human and mouse P100 cDNA 2.7 and 2.0 kb long, respectively [4].
• In the present study, we cloned a cDNA with cDNA of mouse RaRF P100 as a probe from a human liver cDNA library [5].
• Administrationwith antiserum to RaRF prevented animals from death as a consequence of the inhibition of interaction of RaRF with the carbohydrate target and complement activation [6].

Anatomical context of Masp1

• The genes encoding two recently described cytotoxic T cell proteases, CCPI and CCPII, have been isolated and sequenced [7].

Associations of Masp1 with chemical compounds

• Presence of a serine protease in the complement-activating component of the complement-dependent bactericidal factor, RaRF, in mouse serum [8].
• Diisopropyl fluorophosphate (DFP) bound to RaRF and inhibited its ability to activate C4 and C2 [9].
• The sequence of 14 NH2-terminal amino acid residues of the molecule showed 93% identity to rat MBP-A and complete identity to the translated cDNA sequences for mouse MBP-A and mouse Ra-reactive factor component P28b (RaRF P28b) published previously [10].

Other interactions of Masp1

• Organization of two genes encoding cytotoxic T lymphocyte-specific serine proteases CCPI and CCPII [7].

Analytical, diagnostic and therapeutic context of Masp1

• Western blot analysis indicated that PO25 LPS bound to Ra-reactive factor (RaRF), the complex of mannan-binding lectins (MBL) and MBL-associated serine proteases [6].

References