Analysis of lectin-dependent recognition of desialylated erythrocytes by Kupffer cells

Schlepper-Schäfer, Jutta; Kolb-Bachofen, Victoria; Kolb, Hubert

doi:10.1042/bj1860827

Cited by 76 publications

(20 citation statements)

References 23 publications

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“…The peritoneal macrophage receptor closely resembles the hepatic lectin first described in [8,9] and a lectin found on Kupffer cells [6,7]. In each case the receptor recognizes both galactosyl and glucosyl residues 1791 and its activity is calcium-dependent.…”

Section: Discussionmentioning

confidence: 80%

“…In each case the receptor recognizes both galactosyl and glucosyl residues 1791 and its activity is calcium-dependent. Inhibition of ATP production, however, only affected receptor activity of peritoneal macrophages but not of hepatocytes [lo] or liver macrophages [7].…”

Section: Discussionmentioning

confidence: 99%

“…Gamma globulin fractions of goat and rabbit anti-rat ~muno~obu~n antisera (Nordic, Tilburg) were prepared by precipitation with sodium sulfate and absorbed twice with a mixture of untreated and desialylated rat erythrocytes [7]. Antisera reacted with H-chains of IgG and L-chains of all Ig ciasses,…”

Section: Cell Adhesion Assaymentioning

confidence: 99%

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Presence of a lectin‐like receptor for D‐galactose on rat peritoneal macrophages

Nagamura

Kolb

1980

FEBS Letters

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Section: Discussionmentioning

confidence: 80%

Section: Discussionmentioning

confidence: 99%

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Presence of a lectin‐like receptor for D‐galactose on rat peritoneal macrophages

Nagamura

Kolb

1980

FEBS Letters

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“…Subsequent studies demonstrated characteristic differences between the macrophage galactose receptor and the hepatic lectin in carbohydrate specificity as well as in the number and complexity of polypeptide subunits. However, Kupffer cell lectin had a greater affinity to GalNAc than to galactoside with a multivalent effect, indicating that the carbohydrate specificity of Kupffer cell lectin was similar to that of hepatic ASGPR (51,52). Kupffer cell lectin could be recognized by 6-O-phospho-D-glucose and glucosyl-BSA.…”

Section: Table I Inhibition Of Hepatocyte Adhesion To the Pv6gna Surfmentioning

confidence: 99%

Specific Binding of Glucose-derivatized Polymers to the Asialoglycoprotein Receptor of Mouse Primary Hepatocytes

Kim¹,

Goto²,

Akaike³

2001

Journal of Biological Chemistry

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In this study, we designed a novel amphiphilic poly-(p-Nvinylbenzyl-D-glucuronamide) (PV6Gna) modified at the 6-OH position of glucose for hepatocyte recognition to address the mechanism of the interaction between mouse primary hepatocytes and the PV6Gna. PV6Gna bound to lectins specific for glucose but not galactose as did other glucose-derivatized polymers. However, hepatocyte adhesion onto the PV6Gna surface was inhibited in the presence of galactose and its analogues but not in the presence of glucose and its analogues. We also showed that hepatocyte adhesion to the PV6Gna surface was inhibited dose dependently by asialofetuin (ASF). Interactions between soluble PV6Gna and hepatocytes were inhibited by GalNAc, ASF, and EGTA in flow cytometry analysis using fluorescein isothiocyanate-conjugated PV6Gna. Hepatocyte adhesion to the PV6Gna surface was inhibited more effectively by GalNAc than by methyl ␤-D-galactose. In flow cytometry analysis and cell adhesion assay, ASF competed for the inhibition of interaction between PV6Gna and hepatocytes 0.5-4 ؋ 10 5

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“…Hepatic binding protein [56,57] Binds circulating desialated erythrocytes and glycoproteins in rat and rabbit liver. Galactose specific Nevertheless, those molecules which have so far been characterized and experimentally demonstrated to be involved in intercellular recognition and adhesion fall naturally into the two categories delineated, that is they are either membrane-anchored factors or extracellular factors which, it is suggested, bridge between cells or receptors.…”

Section: Fab Disrupts Histogenesis Of Embryonic Retina In Organ Culturementioning

confidence: 99%

Factors mediating cell—cell recognition and adhesion

1980

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Analysis of lectin-dependent recognition of desialylated erythrocytes by Kupffer cells

Cited by 76 publications

References 23 publications

Presence of a lectin‐like receptor for D‐galactose on rat peritoneal macrophages

Presence of a lectin‐like receptor for D‐galactose on rat peritoneal macrophages

Specific Binding of Glucose-derivatized Polymers to the Asialoglycoprotein Receptor of Mouse Primary Hepatocytes

Factors mediating cell—cell recognition and adhesion

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