Literature DB >> 7396839

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

J Schlepper-Schäfer, V Kolb-Bachofen, H Kolb.   

Abstract

Kupffer cells isolated from the rat liver are able to bind neuraminidase-treated rat erythrocytes via a D-galactose-specific receptor on the cell surface. Binding of desialylated erythrocytes was inhibited by several mono- and oligo-saccharides related to D-galactose, but not by unrelated sugars. However, after phosphorylation at position 6 D-glucose was as good an inhibitor as D-galactose. Two synthetic glycoproteins, D-galactosyl-albumin and, at a higher concentration, D-glucosyl-albumin, strongly inhibit cell contacts. Lectin-mediated binding of desialylated erythrocytes is dependent on the presence of Ca2'ons, but independent of ATP formation and cell motility. It is concluded that binding of desialylated erythrocytes by rat Kupffer cells is mediated by a Ca2-dependent D-galactosyl/D-glucosyl-recognition system.

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Year:  1980        PMID: 7396839      PMCID: PMC1161719          DOI: 10.1042/bj1860827

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  22 in total

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Authors:  D Aminoff; W F Bruegge; W C Bell; K Sarpolis; R Williams
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Review 8.  The role of surface carbohydrates in the hepatic recognition and transport of circulating glycoproteins.

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Review 9.  Blood-group and Forssman antigenic determinants shared between microbes and mammalian cells.

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Authors:  A R Spurr
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  9 in total

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5.  Does the D-galactose receptor on Kupffer cells recycle?

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Review 6.  Endogenous galactoside-binding lectins: a new class of functional tumor cell surface molecules related to metastasis.

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7.  Carbohydrate-structure-dependent recognition of desialylated serum glycoproteins in the liver and leucocytes. Two complementary systems.

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9.  Tumor cell surface beta 1-4-linked galactose binds to lectin(s) on microvascular endothelial cells and contributes to organ colonization.

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  9 in total

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