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Gene Review

Mbl2  -  mannose-binding lectin (protein C) 2

Rattus norvegicus

Synonyms: Ab2-001, Ab2-011, MBP-C, Mannan-binding protein, Mannose-binding protein C, ...
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Disease relevance of Mbl2

  • The rat core-specific lectin (CSL) or mannan-binding protein is synthesized and secreted by rat hepatocytes and H-4-II-E hepatoma cells [1].

High impact information on Mbl2

  • The results indicate that phosphorylation of MBP-C (i) extends the cross bridges from the backbone of the filament and (ii) increases their degree of order and/or alters their orientation [2].
  • We isolated natural thick filaments from cardiac muscle and, using electron microscopy and optical diffraction, determined the effect of phosphorylation of MBP-C on cross bridges [2].
  • The activity of MBP-A in a hemolytic complement fixation assay using mannan-coated sheep erythrocytes was approximately 20-fold greater than the activity of MBP-C [3].
  • Complexes of MBP-C with methyl glycosides of mannose, N-acetylglucosamine, and fucose were prepared by soaking MBP-C crystals in solutions containing these sugars [4].
  • A lectin, previously designated the Man/GlcNAc-specific lectin or mannan-binding protein, is found in rat liver and plasma [5].

Biological context of Mbl2

  • Computer analysis of several lectins for sequence homology suggested that the COOH-terminal quarter of the MBP is associated with the calcium binding as well as carbohydrate recognition [6].
  • The nucleotide sequence of the cDNA determined by the dideoxy method revealed the complete amino acid sequence of the MBP (226 residues) [6].
  • cDNA clones encoding rat liver mannan-binding protein (MBP), a lectin specific for mannose and N-acetylglucosamine, were isolated from a rat liver cDNA library carried in lambda gt 11, by screening with affinity purified polyclonal rabbit anti-rat liver MBP antibodies [6].
  • From these and other data, we postulate that the binding site of MBP-C has an extended area of interaction, probably the size of a mannotriose, while MBP-A interacts essentially with one mannose residue [7].
  • The isolated binding protein shares come common properties with liver mannan-binding protein: requirement of Ca2+ for the binding and high affinity for mannan [8].

Anatomical context of Mbl2


Associations of Mbl2 with chemical compounds

  • A complex formed between free galactose and MBP-C reveals a similar mode of binding, with the anomeric hydroxyl group serving as one of the Ca2+ ligands [4].
  • The NH2-terminal residue of the MBP, glutamic acid, was preceded by a predominantly hydrophobic stretch of 18 amino acids, which was assumed to be a signal peptide [6].
  • We found that the liver-type MBP CRD of rat (MBP-C) bound methyl glycosides of certain mannobioses and -trioses, which are part of the mannose-rich N-glycoside, more tightly than methyl alpha-mannopyranoside [7].
  • The mannobiose and -triose most strongly bound to MBP-C CRD were Man alpha (1-2)Man alpha-OMe and Man alpha (1-2)Man alpha (1-6)Man alpha-OMe, respectively [7].
  • The apparent ubiquitous distribution of mannan-binding protein in mammalian liver is consistent with the proposal that the binding protein is the cellular receptor mediating the hepatic uptake of glycoproteins terminated with mannose and/or N-acetylglucosamine residues [9].

Other interactions of Mbl2

  • These structures explain how MBPs recognize a wide range of monosaccharides and suggest how fine specificity differences between MBP-A and MBP-C may be achieved [4].

Analytical, diagnostic and therapeutic context of Mbl2

  • The structural basis of carbohydrate recognition by rat liver mannose-binding protein (MBP-C) has been explored by determining the three-dimensional structure of the C-type carbohydrate-recognition domain (CRD) of MBP-C using x-ray crystallography [4].
  • The rate of sedimentation of MBP-C and its mobility on gel filtration suggest a highly elongated molecule [10].
  • Analytical ultracentrifugation experiments indicate that MBP-C is trimeric, with a weight-averaged molecular mass of approx. 77 kDa [10].
  • A rat liver mannan-binding protein was isolated by affinity chromatography on invertase--Sepharose by a modification of the method of Kawasaki, Etoh & Yamashina [(1978) Biochem. Biophys. Res. Commun. 81, 1018-1024] and by a new method involving chromatography on mannose-Sepharose [11].


  1. Post-translational modifications of the core-specific lectin. Relationship to assembly, ligand binding, and secretion. Colley, K.J., Baenziger, J.U. J. Biol. Chem. (1987) [Pubmed]
  2. Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle. Weisberg, A., Winegrad, S. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  3. Molecular determinants of oligomer formation and complement fixation in mannose-binding proteins. Wallis, R., Drickamer, K. J. Biol. Chem. (1999) [Pubmed]
  4. Structural analysis of monosaccharide recognition by rat liver mannose-binding protein. Ng, K.K., Drickamer, K., Weis, W.I. J. Biol. Chem. (1996) [Pubmed]
  5. Synthesis, processing, and secretion of the core-specific lectin by rat hepatocytes and hepatoma cells. Brownell, M.D., Colley, K.J., Baenziger, J.U. J. Biol. Chem. (1984) [Pubmed]
  6. Primary structure of rat liver mannan-binding protein deduced from its cDNA sequence. Oka, S., Itoh, N., Kawasaki, T., Yamashina, I. J. Biochem. (1987) [Pubmed]
  7. Difference in binding-site architecture of the serum-type and liver-type mannose-binding proteins. Lee, R.T., Lee, Y.C. Glycoconj. J. (1997) [Pubmed]
  8. Mannan-binding protein in lymphoid tissues of rats. Kawasaki, T., Mizuno, Y., Masuda, T., Yamashina, I. J. Biochem. (1980) [Pubmed]
  9. Isolation and characterization of a mannan-binding protein from rat liver. Mizuno, Y., Kozutsumi, Y., Kawasaki, T., Yamashina, I. J. Biol. Chem. (1981) [Pubmed]
  10. Asymmetry adjacent to the collagen-like domain in rat liver mannose-binding protein. Wallis, R., Drickamer, K. Biochem. J. (1997) [Pubmed]
  11. Isolation and characterization of a mannose/N-acetylglucosamine/fucose-binding protein from rat liver. Townsend, R., Stahl, P. Biochem. J. (1981) [Pubmed]
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