The binding of asialo-glycoprotein to isolated Golgi apparatus

Riordan, John R.; Mitchell, Laura L.; Slavik, M.

doi:10.1016/0006-291x(74)90465-3

Cited by 15 publications

(5 citation statements)

References 16 publications

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“…First, information on the binding of this glycoprotein by plasma membrane preparations is limited (6,31). Second, the glycan structures of fetuin are well known (22,(32)(33)(34) been reported.…”

Section: Discussionmentioning

confidence: 98%

Multivalent interaction between asialofetuin and plasma membrane preparations from the rat liver

Debanne¹,

Regoeczi²,

Hatton³

1980

Can. J. Biochem.

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Binding of bovine asialofetuin by rat liver plasma membranes was studied using different techniques for the separation of the free and bound forms of the glycoprotein and also different approaches to measure nonspecific binding. The membrane preparations had the electron microscopic appearance of a mixture of lamellae and vesicles and their lipid:protein ratios and marker enzyme profiles fell within the range of values available from the literature. The binding capacity was approximately 15 pmol of asialofetuin per milligram of membrane protein. Scatchard plots of the values obtained over a wide range of concentrations (4.8--12.6 micrograms asialofetuin per 30 micrograms membrane protein) after incubation at 22 degrees C showed pronounced nonlinearity which, in combination with evaluations according to other theoretical models, was referable to heterogeneity of binding. In sharp contrast, after incubation at 4 degrees C the Scatchard plot was linear. This difference is interpreted as the expression of a functional, rather than a chemical, heterogeneity in asialofetuin binding. The underlying mechanism is thought to be competition of galactose groups for binding sites with the result that the number of bonds varies between the galactose groups of a bound asialofetuin molecular and the hepatic lectin, depending on the concentration of the glycoprotein in the incubation mixture.

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Section: Discussionmentioning

confidence: 98%

Multivalent interaction between asialofetuin and plasma membrane preparations from the rat liver

Debanne¹,

Regoeczi²,

Hatton³

1980

Can. J. Biochem.

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“…It is not clear whether the native a-lactalbumin has some exposed galactose residues or a-lactalbumin peptide interacts with the lectin. Hudgin and Ashwe1l 26 ) and Riordan et al 27 ) reported that bovine a-lactalbumin,though it is not a glycoprotein, is bound by the hepatic binding protein.…”

Section: Binding Activity Of Rat Mammary Gland Lectin For Milk Glycopmentioning

confidence: 94%

Partial Purification and Characterization of Rat Mammary Gland Lectin

Takeuchi

Yoshikawa

Sasaki

et al. 1982

Agricultural and Biological Chemistry

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“…This finding, together with the observed invariance of the receptors' turnover rate during protracted asialoglycoprotein catabolism (9), suggested a recycling mechanism whereby HBP is spared the degradative fate of internalized asialoglycoprotein. Analysis of mechanisms by which HBP is reutilized is compounded by its presence in other intracellular membranes (38)(39)(40). Depending on the method of assay, the intracellular pool of HBP is from 50 to 90% of the total cell concentration of receptor.…”

Section: Receptor Recyclingmentioning

confidence: 99%

Hepatic Binding Protein: The Galactose-Specific Receptor of Mammalian Hepatocytes

1983

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The membranes of the liver cell have been described as a protein mosaic within a lipid bilayer. Among the various pieces in this design are receptor proteins capable of recognizing and binding specific ligands. These receptors define much of the differentiated state of hepatocytes providing them with many specific functions. One of the most extensively studied of these receptor proteins is the hepatic binding protein or HBP. This membrane glycoprotein is responsible for the endocytosis of galactose-terminating glycoproteins leading to their lysosomal catabolism. While no physiologic function has yet been ascribed to HBP, its study has provided many insights into the biology and pathobiology of the liver. DISCOVERYThe path that led to discovery of HBP began with the development of a novel procedure to incorporate tritium selectively into the galactosyl residues of serum glycoprotein (1). Since most serum glycoproteins' carbohydrate moieties terminate in sialic acid, this residue was enzymatically removed to expose the penultimate galactose. The desialylated glycoproteins were then treated with galactose oxidase to yield an active aldehyde group in their galactosyl residues which could be reduced with tritiated borohydride. Application of this procedure to the serum copper-protein, ceruloplasmin, yielded a preparation which was indistinguishable from the native protein except, of course, for the absence of sialic acid. However, when this desialylated glycoprotein was injected, it no longer was viable in the circulation (2).The penultimate galactosyl residues, exposed by removal of sialic acid, were shown to be the critical determinants of this rapid clearance phenomena (3, 4). Enzymatic oxidation or removal of the terminal galactosyl residues significantly prolonged the intravascular survival of desialylated ceruloplasmin. The unique nature of this model was extended beyond galactose-directed clearance by the observation that sequestration of desiAddress reprint requests to: Richard J. Stockert, Ph.D., Ullmann, Room 517,

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The binding of asialo-glycoprotein to isolated Golgi apparatus

Cited by 15 publications

References 16 publications

Multivalent interaction between asialofetuin and plasma membrane preparations from the rat liver

Multivalent interaction between asialofetuin and plasma membrane preparations from the rat liver

Partial Purification and Characterization of Rat Mammary Gland Lectin

Hepatic Binding Protein: The Galactose-Specific Receptor of Mammalian Hepatocytes

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