Lactoferrin binding to the rat asialoglycoprotein receptor requires the receptor’s lectin properties
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Lactoferrin binding to the rat asialoglycoprotein receptor requires the receptor's lectin properties.
Lactoferrin binds to rat hepatic lectin 1 (RHL1), the major subunit of the asialoglycoprotein (ASGP) receptor, with high affinity, by a galactose-independent mechanism. To better understand the molecular basis of this novel interaction, we compared the binding of lactoferrin and asialo-orosomucoid (ASOR) to isolated rat hepatocytes and to purified ASGP receptors as a function of pH, Ca(2+) and ...
متن کاملDifferential ligand binding by two subunits of the rat liver asialoglycoprotein receptor.
The rat liver asialoglycoprotein receptor consists of two types of subunits, a predominant polypeptide designated rat hepatic lectin 1 (RHL-1) and a minor polypeptide, RHL-2/3, that comes in two differentially glycosylated forms. The exact stoichiometry and arrangement of the subunits in the RHL oligomer are not known. The carbohydrate-recognition domain of RHL-2/3 has been prepared by limited ...
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The galactophilic lectin expressed on the surface of cultured Hodgkin's cells, recently described by this laboratory, has binding characteristics similar to those of the hepatic asialoglycoprotein receptor (HBP), and has been recognized as a Mr 55,000 (p55) membrane glycoprotein by a polyclonal antiserum to rat HBP. This study confirms the close structural relationship between the two lectins s...
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We recently reported that the dissociation of internalized receptor-1261-asialo-orosomucoid (ASOR) complexes by isolated hepatocytes is a biphasic process; most complexes dissociate rapidly but 25-50% dissociate slowly (Oka, J. A., and Weigel, P. H. J. Biol. Chern. 258, 10253-10262). Cells were allowed to endocytose a pulse of surface-bound '''I-ASOR, and were washed and then incubated at 37 "C...
متن کاملIdentification and quantification of the rat hepatocyte asialoglycoprotein receptor.
The asialoglycoprotein receptor from rat liver was purified by solubilization and affinity chromatography on asialoorosomucoid-Sepharose. The preparation yielded four distinct polypeptides of Mr 40,000-120,000. We prepared a monoclonal antibody that both immunoprecipitates solubilized receptor activity and blocks the binding of galactose-terminal glycoproteins to immobilized receptor. The monoc...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 2000
ISSN: 0264-6021
DOI: 10.1042/0264-6021:3480113