Cross‐linking of galectin 3, a galactose‐binding protein of mammalian cells, by tissue‐type transglutaminase
1995; Wiley; Volume: 360; Issue: 2 Linguagem: Inglês
10.1016/0014-5793(95)00100-n
ISSN1873-3468
AutoresBruno Méhul, Sulemana Bawumia, R. Colin Hughes,
Tópico(s)Signaling Pathways in Disease
ResumoThe 30 kDa β‐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 mammlian 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 dhis 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 stablisation of a multivalent binding form of the lectin in cell secretions or in extracellular matrices.
Referência(s)