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Gene Review

Masp1  -  mannan-binding lectin serine peptidase 1

Mus musculus

Synonyms: AW048060, CCPII, Complement factor MASP-3, Complement-activating component of Ra-reactive factor, Crarf, ...
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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


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].


  1. The C4 and C2 but not C1 components of complement are responsible for the complement activation triggered by the Ra-reactive factor. Ji, Y.H., Matsushita, M., Okada, H., Fujita, T., Kawakami, M. J. Immunol. (1988) [Pubmed]
  2. Substrate specificities of the protease of mouse serum Ra-reactive factor. Ogata, R.T., Low, P.J., Kawakami, M. J. Immunol. (1995) [Pubmed]
  3. A 100-kDa protein in the C4-activating component of Ra-reactive factor is a new serine protease having module organization similar to C1r and C1s. Takayama, Y., Takada, F., Takahashi, A., Kawakami, M. J. Immunol. (1994) [Pubmed]
  4. Localization of the genes for the 100-kDa complement-activating components of Ra-reactive factor (CRARF and Crarf) to human 3q27-q28 and mouse 16B2-B3. Takada, F., Seki, N., Matsuda, Y., Takayama, Y., Kawakami, M. Genomics (1995) [Pubmed]
  5. A new member of the C1s family of complement proteins found in a bactericidal factor, Ra-reactive factor, in human serum. Takada, F., Takayama, Y., Hatsuse, H., Kawakami, M. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  6. Role of the complement-lectin pathway in anaphylactoid reaction induced with lipopolysaccharide in mice. Swierzko, A.S., Cedzyński, M., Kirikae, T., Nakano, M., Klink, M., Kirikae, F., Ziółkowski, A., Vinogradov, E.V., Kawakami, M. Eur. J. Immunol. (2003) [Pubmed]
  7. Organization of two genes encoding cytotoxic T lymphocyte-specific serine proteases CCPI and CCPII. Lobe, C.G., Upton, C., Duggan, B., Ehrman, N., Letellier, M., Bell, J., McFadden, G., Bleackley, R.C. Biochemistry (1988) [Pubmed]
  8. Presence of a serine protease in the complement-activating component of the complement-dependent bactericidal factor, RaRF, in mouse serum. Takahashi, A., Takayama, Y., Hatsuse, H., Kawakami, M. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  9. Activation of the C4 and C2 components of complement by a proteinase in serum bactericidal factor, Ra reactive factor. Ji, Y.H., Fujita, T., Hatsuse, H., Takahashi, A., Matsushita, M., Kawakami, M. J. Immunol. (1993) [Pubmed]
  10. Purification and characterization of mannan-binding protein from mouse serum. Holt, P., Holmskov, U., Thiel, S., Teisner, B., Højrup, P., Jensenius, J.C. Scand. J. Immunol. (1994) [Pubmed]
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