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lec-1  -  Protein LEC-1

Caenorhabditis elegans

 
 
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High impact information on galectin

  • Sugar binding properties of the two lectin domains of the tandem repeat-type galectin LEC-1 (N32) of Caenorhabditis elegans. Detailed analysis by an improved frontal affinity chromatography method [1].
  • Physical mapping by yeast artificial chromosome polytene filter hybridization revealed that the 32-kDa galectin gene is located on chromosome II [2].
  • Although such an insertion pattern has never been observed in the vertebrate galectin genes, it seems to be common in C. elegans tandem repeat-type galectin genes, as predicted by the C. elegans genome project (Coulson, A., and the C. elegans Genome Consortium (1996) Biochem. Soc. Trans. 24, 289-291) [2].
  • Two dimeric galectins are expressed during fruiting body formation which are 83% identical to each other in amino acid sequence and conserve all key residues shared by members of the galectin family [3].
  • The subsequent study revealed that the 32-kDa lectin is a member of the galectin family [4].
 

Biological context of galectin

  • The cDNA sequence, exhibiting a tandem repeat structure and designated Hco-gal-2, showed significant levels of similarity with galectins from several species of nematode as well as mammalian galectin type 4 [5].
  • A cDNA encoding a beta-galactoside-binding lectin (galectin) was identified by immunoscreening a Haemonchus contortus cDNA library with antisera from lambs vaccinated with a membrane protein complex (H-gal-GP) derived from the parasites' gut [5].
  • These results suggest that one of the fundamental roles of the galectin may be as a component of the durable outer barrier, as in the case of the morphogenesis of chick embryonic skin [6].
  • The 32-kDa galectin (LEC-1) of the nematode Caenorhabditis elegans (C elegans) is composed of two tandemly repeated homologous sequences, each containing a carbohydrate-recognition domain (CRD) [7].
 

Associations of galectin with chemical compounds

  • Further, to examine the practical validity of the method, we extracted membrane proteins from C. elegans with 1% Triton X-100, and isolated specific glycopeptides by use of the same galectin column [8].
 

Analytical, diagnostic and therapeutic context of galectin

  • Native galectin was preferentially extracted from the H-gal-GP complex and also from an insoluble membrane fraction prepared from adult worms using lactose-agarose affinity chromatography [5].

References

  1. Sugar binding properties of the two lectin domains of the tandem repeat-type galectin LEC-1 (N32) of Caenorhabditis elegans. Detailed analysis by an improved frontal affinity chromatography method. Arata, Y., Hirabayashi, J., Kasai , K. J. Biol. Chem. (2001) [Pubmed]
  2. Structure of the 32-kDa galectin gene of the nematode Caenorhabditis elegans. Arata, Y., Hirabayashi, J., Kasai, K. J. Biol. Chem. (1997) [Pubmed]
  3. Fungal galectins, sequence and specificity of two isolectins from Coprinus cinereus. Cooper, D.N., Boulianne, R.P., Charlton, S., Farrell, E.M., Sucher, A., Lu, B.C. J. Biol. Chem. (1997) [Pubmed]
  4. Purification and molecular characterization of a novel 16-kDa galectin from the nematode Caenorhabditis elegans. Hirabayashi, J., Ubukata, T., Kasai, K. J. Biol. Chem. (1996) [Pubmed]
  5. Cloning and characterization of a beta-galactoside-binding protein (galectin) from the gut of the gastrointestinal nematode parasite Haemonchus contortus. Newlands, G.F., Skuce, P.J., Knox, D.P., Smith, S.K., Smith, W.D. Parasitology (1999) [Pubmed]
  6. An immunohistochemical study of the 32-kDa galectin (beta-galactoside-binding lectin) in the nematode Caenorhabditis elegans. Arata, Y., Akimoto, Y., Hirabayashi, J., Kasai, K., Hirano, H. Histochem. J. (1996) [Pubmed]
  7. Effects of substitution of conserved amino acid residues on the sugar-binding property of the tandem-repeat 32-kDa galectin of the nematode Caenorhabditis elegans. Arata, A., Sekiguchi, M., Hirabayashi, J., Kasai, K. Biol. Pharm. Bull. (2001) [Pubmed]
  8. Glycome project: concept, strategy and preliminary application to Caenorhabditis elegans. Hirabayashi, J., Arata, Y., Kasai, K. Proteomics (2001) [Pubmed]
 
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