The binding of fucose-containing glycoproteins by hepatic lectins. Re-examination of the clearance from blood and the binding to membrane receptors and pure lectins

M. A. Lehrman, S. V. Pizzo, M. J. Imber, R. L. Hill

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

The nature of the hepatic receptors that bind glycoproteins through fucose at the non-reducing termini of oligosaccharides in glycoproteins has been examined by three different approaches. First, the clearance from blood of intravenously injected glycoproteins was examined in mice with the aid of neoglycoproteins of bovine serum albumin (BSA). The clearance of fucosyl-BSA was rapid and was not strongly inhibited by glycoproteins that inhibit clearance mediated by the galactose or the mannose/N-acetylglucosamine receptors of liver. The clearance of Fucα1,3(Galβ1,4)GlcNAc-BSA (where Fuc is fucose) was inhibited weakly by either Fuc-BSA or Galβ1,4GlcNAc-BSA but strongly by a mixture of the two neoglycoproteins, suggesting that its clearance was mediated by hepatic galactose receptors as well as by a fucose-binding receptor. Second, the binding of neoglycoproteins to a membrane fraction of mouse liver was examined. Fuc-BSA binding to membranes was Ca2+ dependent but was not inhibited by glycoproteins that would inhibit the galactose or the mannose/N-acetylglucosamine receptors. In addition, the binding of Fuc-BSA and Galβ1,4,GlcNAc-BSA differed as a function of pH, in accord with binding of Fuc-BSA through fucose-specific hepatic receptors. Finally, the binding of neoglycoproteins to the pure galactose lectin from rat liver was examined. Neither Fuc-BSA nor Fucα1,2Galβ1,4GlcNAc-BSA bound the galactose lectin, although Fucα1,3(Galβ-1,4)GlcNAc-BSA bound avidly. Taken together, these studies suggest that a fucose-binding receptor that differs from the galactose and the mannose/N-acetylglucosamine receptors may exist in rat and mouse liver.

Original languageEnglish (US)
Pages (from-to)7412-7418
Number of pages7
JournalJournal of Biological Chemistry
Volume261
Issue number16
StatePublished - 1986

Fingerprint

Mitogen Receptors
Asialoglycoprotein Receptor
Fucose
Bovine Serum Albumin
Lectins
Glycoproteins
Blood
Membranes
Galactose
Liver
Rats
Oligosaccharides

ASJC Scopus subject areas

  • Biochemistry

Cite this

The binding of fucose-containing glycoproteins by hepatic lectins. Re-examination of the clearance from blood and the binding to membrane receptors and pure lectins. / Lehrman, M. A.; Pizzo, S. V.; Imber, M. J.; Hill, R. L.

In: Journal of Biological Chemistry, Vol. 261, No. 16, 1986, p. 7412-7418.

Research output: Contribution to journalArticle

@article{592458960c014deaa2c57f5459da5a29,
title = "The binding of fucose-containing glycoproteins by hepatic lectins. Re-examination of the clearance from blood and the binding to membrane receptors and pure lectins",
abstract = "The nature of the hepatic receptors that bind glycoproteins through fucose at the non-reducing termini of oligosaccharides in glycoproteins has been examined by three different approaches. First, the clearance from blood of intravenously injected glycoproteins was examined in mice with the aid of neoglycoproteins of bovine serum albumin (BSA). The clearance of fucosyl-BSA was rapid and was not strongly inhibited by glycoproteins that inhibit clearance mediated by the galactose or the mannose/N-acetylglucosamine receptors of liver. The clearance of Fucα1,3(Galβ1,4)GlcNAc-BSA (where Fuc is fucose) was inhibited weakly by either Fuc-BSA or Galβ1,4GlcNAc-BSA but strongly by a mixture of the two neoglycoproteins, suggesting that its clearance was mediated by hepatic galactose receptors as well as by a fucose-binding receptor. Second, the binding of neoglycoproteins to a membrane fraction of mouse liver was examined. Fuc-BSA binding to membranes was Ca2+ dependent but was not inhibited by glycoproteins that would inhibit the galactose or the mannose/N-acetylglucosamine receptors. In addition, the binding of Fuc-BSA and Galβ1,4,GlcNAc-BSA differed as a function of pH, in accord with binding of Fuc-BSA through fucose-specific hepatic receptors. Finally, the binding of neoglycoproteins to the pure galactose lectin from rat liver was examined. Neither Fuc-BSA nor Fucα1,2Galβ1,4GlcNAc-BSA bound the galactose lectin, although Fucα1,3(Galβ-1,4)GlcNAc-BSA bound avidly. Taken together, these studies suggest that a fucose-binding receptor that differs from the galactose and the mannose/N-acetylglucosamine receptors may exist in rat and mouse liver.",
author = "Lehrman, {M. A.} and Pizzo, {S. V.} and Imber, {M. J.} and Hill, {R. L.}",
year = "1986",
language = "English (US)",
volume = "261",
pages = "7412--7418",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "16",

}

TY - JOUR

T1 - The binding of fucose-containing glycoproteins by hepatic lectins. Re-examination of the clearance from blood and the binding to membrane receptors and pure lectins

AU - Lehrman, M. A.

AU - Pizzo, S. V.

AU - Imber, M. J.

AU - Hill, R. L.

PY - 1986

Y1 - 1986

N2 - The nature of the hepatic receptors that bind glycoproteins through fucose at the non-reducing termini of oligosaccharides in glycoproteins has been examined by three different approaches. First, the clearance from blood of intravenously injected glycoproteins was examined in mice with the aid of neoglycoproteins of bovine serum albumin (BSA). The clearance of fucosyl-BSA was rapid and was not strongly inhibited by glycoproteins that inhibit clearance mediated by the galactose or the mannose/N-acetylglucosamine receptors of liver. The clearance of Fucα1,3(Galβ1,4)GlcNAc-BSA (where Fuc is fucose) was inhibited weakly by either Fuc-BSA or Galβ1,4GlcNAc-BSA but strongly by a mixture of the two neoglycoproteins, suggesting that its clearance was mediated by hepatic galactose receptors as well as by a fucose-binding receptor. Second, the binding of neoglycoproteins to a membrane fraction of mouse liver was examined. Fuc-BSA binding to membranes was Ca2+ dependent but was not inhibited by glycoproteins that would inhibit the galactose or the mannose/N-acetylglucosamine receptors. In addition, the binding of Fuc-BSA and Galβ1,4,GlcNAc-BSA differed as a function of pH, in accord with binding of Fuc-BSA through fucose-specific hepatic receptors. Finally, the binding of neoglycoproteins to the pure galactose lectin from rat liver was examined. Neither Fuc-BSA nor Fucα1,2Galβ1,4GlcNAc-BSA bound the galactose lectin, although Fucα1,3(Galβ-1,4)GlcNAc-BSA bound avidly. Taken together, these studies suggest that a fucose-binding receptor that differs from the galactose and the mannose/N-acetylglucosamine receptors may exist in rat and mouse liver.

AB - The nature of the hepatic receptors that bind glycoproteins through fucose at the non-reducing termini of oligosaccharides in glycoproteins has been examined by three different approaches. First, the clearance from blood of intravenously injected glycoproteins was examined in mice with the aid of neoglycoproteins of bovine serum albumin (BSA). The clearance of fucosyl-BSA was rapid and was not strongly inhibited by glycoproteins that inhibit clearance mediated by the galactose or the mannose/N-acetylglucosamine receptors of liver. The clearance of Fucα1,3(Galβ1,4)GlcNAc-BSA (where Fuc is fucose) was inhibited weakly by either Fuc-BSA or Galβ1,4GlcNAc-BSA but strongly by a mixture of the two neoglycoproteins, suggesting that its clearance was mediated by hepatic galactose receptors as well as by a fucose-binding receptor. Second, the binding of neoglycoproteins to a membrane fraction of mouse liver was examined. Fuc-BSA binding to membranes was Ca2+ dependent but was not inhibited by glycoproteins that would inhibit the galactose or the mannose/N-acetylglucosamine receptors. In addition, the binding of Fuc-BSA and Galβ1,4,GlcNAc-BSA differed as a function of pH, in accord with binding of Fuc-BSA through fucose-specific hepatic receptors. Finally, the binding of neoglycoproteins to the pure galactose lectin from rat liver was examined. Neither Fuc-BSA nor Fucα1,2Galβ1,4GlcNAc-BSA bound the galactose lectin, although Fucα1,3(Galβ-1,4)GlcNAc-BSA bound avidly. Taken together, these studies suggest that a fucose-binding receptor that differs from the galactose and the mannose/N-acetylglucosamine receptors may exist in rat and mouse liver.

UR - http://www.scopus.com/inward/record.url?scp=0022900906&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022900906&partnerID=8YFLogxK

M3 - Article

VL - 261

SP - 7412

EP - 7418

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 16

ER -