Hall, Heike and Deutzmann, Rainer and Timpl, Rupert and Vaughan, Lloyd and Schmitz, Brigitte and Schachner, Melitta (1997) HNK-1 carbohydrate-mediated cell adhesion to laminin-1 is different from heparin-mediated and sulfatide-mediated cell adhesion. EUROPEAN JOURNAL OF BIOCHEMISTRY, 246 (1). pp. 233-242. ISSN 0014-2956
Full text not available from this repository.Abstract
The sulfated HNK-1 carbohydrate present on glycolipids and on several neural recognition molecules has been shown to mediate the adhesion of murine small cerebellar neurons and astrocytes to the extracellular matrix molecule laminin-1. In this study, we characterized the binding of the HNK-1 carbohydrate to laminin-1 extracted from the Engelbreth-Holm-Swarm (EHS) sarcoma and distinguished it unequivocally from binding sites for other sulfated carbohydrates. Electron microscopic analysis of rotary shadowed complexes of laminin-1 and a HNK-1 neoglycoprotein revealed a major binding site on the G domain that comprises the C-terminal globule of the laminin alpha 1 chain. The HNK-1 carbohydrate also interacted with placental laminin isoforms containing an alpha chain variant. It bound to the proteolytic laminin-1 fragment EX comprising the domains G1-G3, but not to fragment E3 that carries the major heparin binding site on domains G4-G5. No binding was observed to the short arm containing fragments E1XNd or P1. Binding studies with native or denatured laminin E8 fragments and proteolytic or recombinant fragments of the G domain localized the HNK-1 carbohydrate binding site to domain G2. The binding could be clearly distinguished from binding sites for other sulfated carbohydrates such as heparin and sulfatides. Further, the binding could not be abolished by reduction and alkylation or by urea treatment of laminin-1 and was independent of the native conformation of laminin-1 and of Ca2+. The G2 domain is also involved in the adhesion of HNK-1 carbohydrate expressing early postnatal cerebellar neurons and is different from heparin- and sulfatide-mediated cell adhesion to laminin-1. HNK-1 carbohydrate-mediated cell adhesion appears, however, to be dependent on the native conformation of laminin-1 indicating a more complex cellular recognition process.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | MYELIN-ASSOCIATED GLYCOPROTEIN; MONOCLONAL-ANTIBODY HNK-1; A-CHAIN; BINDING DOMAIN; B-CHAINS; N-CAM; SULFOGLUCURONYL GLYCOLIPIDS; L2/HNK-1 CARBOHYDRATE; BASEMENT-MEMBRANES; SURFACE-ANTIGENS; HNK-1 carbohydrate; laminin; heparin; sulfatide; cell adhesion |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie I > Prof. Dr. Rainer Deutzmann |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 27 Apr 2023 09:16 |
| Last Modified: | 27 Apr 2023 09:16 |
| URI: | https://pred.uni-regensburg.de/id/eprint/50818 |
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