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Characterization of a 21 amino acid peptide sequence of the laminin G2 domain that is involved in HNK-1 carbohydrate binding and cell adhesion

Hall, Heike ; Vorherr, Thomas ; Schachner, Melitta

In: Glycobiology, 1995, vol. 5, no. 4, p. 435-441

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    Title
    • Characterization of a 21 amino acid peptide sequence of the laminin G2 domain that is involved in HNK-1 carbohydrate binding and cell adhesion
    Author
    • Hall, Heike. Present address: Department of Experimental Pathology, Guy's Hospital London Bridge, London SE1 9RT, UK
    • Vorherr, Thomas. Department of Hoffmann La Roche PRPC 15/4, 4002 Basel, Switzerland
    • Schachner, Melitta. Department of Neurobiology, Swiss Federal Institute of Technology, Hönggerberg, 8093 Zürich, Switzerland, PRPC 15/4, 4002 Basel, Switzerland, London Bridge, London SE1 9RT, UK
    Document Type
    • Postprint
    OAI-PMH Identifier
    • oai:doc.rero.ch:297739
    Summary
    The N-linked HNK-1 carbohydrate expressed by several recognition molecules mediates the adhesion of early postnatal cerebellar neurons to the G2 domain of the terminal globular domain of the laminin α1 chain (H.Hall et al., submitted). To define this binding site more precisely, G2-derived synthetic peptides were used for binding and competition studies. Peptide 5-G2, comprising the amino acid residues 3431-3451 of G2, inhibited the interaction between the HNK-1-carrying glycolipid and laminin in a concentrationdependent and saturable manner. Peptides which overlap only partially with this sequence interfered less. Peptides comprising other amino acid sequences from G2, and peptides derived from G1 and G3 or a scrambled version of peptide 5-G2, did not show significant effects. Direct binding of peptide 5-G2 to the HNK-1 glycolipid was also demonstrated. Furthermore, peptide 5-G2 interfered in a concentration-dependent and saturable manner with the adhesion of early postnatal cerebellar neurons to laminin. These observations indicate that amino acid residues 3431-3451 of the laimnin G2 domain are involved in HNK-1 carbohydratemediated cell adhesion