Galectin-3, a beta-galactoside-binding animal lectin, binds to neural recognition molecules.
In this study, we have investigated the ability of galectin-3, a beta-galactoside-binding animal lectin, to interact in vitro with different neural tissue-derived glycoproteins involved in cell-cell and cell-substrate adhesion. Galectin-3 interacted to varying degrees with the cell recognition molecules L1, the myelin-associated glycoprotein, and the neural cell adhesion molecule and the extracellular matrix molecules tenascin-C and tenascin-R but not with collagen type I. Binding of galectin-3 to the different glycoproteins tested was carbohydrate dependent and could be specifically inhibited by the addition of lactose and, to a lesser extent, galactose.
Probstmeier
R
R
Department of Neurobiology, Swiss Federal Institute of Technology, Zürich.
Montag
D
D
Schachner
M
M
D000818:Animals; D000943:Antigens, Differentiation / Q000378:metabolism*; D015816:Cell Adhesion Molecules, Neuronal / Q000378:metabolism*; D016326:Extracellular Matrix Proteins / Q000378:metabolism; D005697:Galactosides / Q000378:metabolism*; D037502:Galectin 3; D006023:Glycoproteins / Q000378:metabolism; D007700:Kinetics; D037102:Lectins / Q000378:metabolism*; D009185:Myelin Proteins / Q000378:metabolism; D018992:Myelin-Associated Glycoprotein; D009419:Nerve Tissue Proteins / Q000378:metabolism; D019063:Tenascin
D000943:Antigens, Differentiation; D015816:Cell Adhesion Molecules, Neuronal; D016326:Extracellular Matrix Proteins; D005697:Galactosides; D037502:Galectin 3; D006023:Glycoproteins; D037102:Lectins; D009185:Myelin Proteins; D018992:Myelin-Associated Glycoprotein; D009419:Nerve Tissue Proteins; D019063:Tenascin; C007816:beta-galactoside