Defined geometry of binding between triantennary glycopeptide and the asialoglycoprotein receptor of rat heptocytes

Kevin G Rice; Ora A Weisz; Thomas Barthel; Reiko T Lee; Yuan C Lee

doi:10.1016/S0021-9258(17)44770-3

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Defined geometry of binding between triantennary glycopeptide and the asialoglycoprotein receptor of rat heptocytes

Journal article

Open access

Peer reviewed

Defined geometry of binding between triantennary glycopeptide and the asialoglycoprotein receptor of rat heptocytes

Kevin G Rice, Ora A Weisz, Thomas Barthel, Reiko T Lee and Yuan C Lee

The Journal of biological chemistry, Vol.265(30), pp.18429-18434

10/25/1990

DOI: 10.1016/S0021-9258(17)44770-3

PMID: 2211711

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Abstract

Three derivatives of a triantennary glycopeptide, each containing a single uniquely located 6-amino-galactose residue at either position 6', 6, or 8, were modified at the 6-amino group by attachment of a photolyzable reagent and radiolabeled by iodination of tyrosine. These were allowed to bind to the asialoglycoprotein receptor of isolated rat hepatocytes and photolyzed for affinity labeling. (formula; see text) Each probe specifically labeled either the major (RHL1) or minor (RHL2/3) subunits which comprise the receptor. A photolyzable group attached to galactose residue 6 6' specifically radiolabeled RHL1, whereas a photolyzable group attached to galactose 8 specifically labeled RHL2/3. Photoaffinity labeling of a soluble rat hepatic lectin preparation demonstrated that the minor subunits (RHL2/3) were no longer labeled by the triantennary probe with a photolyzable group at galactose 8. The inhibitory potency of a variety of complex glycopeptides against radiolabeled ligand binding to both rat hepatocytes and soluble lectin are in agreement with photoaffinity results that galactose 8 of triantennary glycopeptide is of unique importance by binding solely to the minor subunits (RHL2/3) of the asialoglycoprotein receptor on hepatocytes. Conversely, galactose residues 6 and 6' bind specifically to the major subunit (RHL1), indicating a precise binding geometry between the trivalent ligand and lectin.

Ligands

Photochemistry

Affinity Labels

Carbohydrate Sequence

Molecular Weight

Asialoglycoprotein Receptor

Liver - metabolism

Molecular Sequence Data

Rats

Structure-Activity Relationship

Asialoglycoproteins - metabolism

Glycopeptides - metabolism

Animals

Receptors, Immunologic - ultrastructure

Molecular Structure

In Vitro Techniques

Receptors, Immunologic - metabolism

Details

Title: Subtitle: Defined geometry of binding between triantennary glycopeptide and the asialoglycoprotein receptor of rat heptocytes
Creators: Kevin G Rice - Department of Biology, Johns Hopkins University, Baltimore, Maryland
Ora A Weisz
Thomas Barthel
Reiko T Lee
Yuan C Lee
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.265(30), pp.18429-18434
DOI: 10.1016/S0021-9258(17)44770-3
PMID: 2211711
NLM abbreviation: J Biol Chem
ISSN: 0021-9258
eISSN: 1083-351X
Publisher: United States
Grant note: DK09970 / NIDDK NIH HHS GM13013-01 BI4 / NIGMS NIH HHS
Language: English
Date published: 10/25/1990
Academic Unit: Pharmaceutical Sciences and Experimental Therapeutics; Craniofacial Anomalies Research Center; Medicinal and Natural Products Chemistry
Record Identifier: 9984065320902771

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