Cross-linking of galectin 3, a galactose-binding protein of mammalian cells, by tissue-type transglutaminase.
The 30 kDa beta-galactoside-binding protein of baby hamster kidney (BHK) cells [Mehul et al. (1994), J. Biol. Chem. 269, 18250-18258] homologous to galectin 3, a widely distributed mammalian lectin, has been found to be a substrate for tissue type transglutaminase, as shown by the incorporation in a calcium- and time-dependent manner of 5-(biotinamido) pentylamine in the presence of guinea pig liver transglutaminase. The amino-terminal domain of hamster galectin 3, which is a repetitive sequence rich in glutamine, tyrosine, glycine and proline, is also an excellent substrate. A single lysine residue in the N-terminal domain is an essential requirement for transglutaminase-mediated oligomerization, and two equivalent glutamine residues present in identical sequence repeats within this domain appear to be involved as amine acceptors in cross-linking reactions. Transglutaminase-mediated cross-linking of galectin 3 to itself or to matrix components may be one mechanism for stabilisation of a multivalent binding form of the lectin in cell secretions or in extracellular matrices.
Mehul
B
B
National Institute for Medical Research, Ridgeway, London, UK.
Bawumia
S
S
Hughes
R C
RC
D000595:Amino Acid Sequence; D000818:Animals; D000943:Antigens, Differentiation / Q000378:metabolism*; D001483:Base Sequence; D006224:Cricetinae; D003432:Cross-Linking Reagents; D017931:DNA Primers / Q000737:chemistry; D016326:Extracellular Matrix Proteins / Q000378:metabolism; D037502:Galectin 3; D006168:Guinea Pigs; D066298:In Vitro Techniques; D008099:Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011994:Recombinant Proteins; D011503:Transglutaminases / Q000378:metabolism*
D000943:Antigens, Differentiation; D003432:Cross-Linking Reagents; D017931:DNA Primers; D016326:Extracellular Matrix Proteins; D037502:Galectin 3; D011994:Recombinant Proteins; D011503:Transglutaminases