Effects of receptor-specific antibody on the uptake of desialylated glycoproteins in the isolated perfused rat liver

R. J. Stockert, U. Gartner, A. G. Morell, Allan W. Wolkoff

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

Removal of the terminal sialic acid residues from most mammalian glycoproteins results in their rapid transfer from the circulation into the liver. In vitro, these desialylated glycoproteins bind to a specific membrane-associated hepatic lectin which has a ubiquitous distribution within the liver cell. In the present study, infusion of a specific antibody to the purified lectin into the portal vein of an isolated perfused rat liver prior to injection of radiolabeled asialoorosomucoid or bilirubin reduced the rate of influx of asialoorosomucoid into the liver by over 80%, while the influx of bilirubin was unchanged. Although uptake of asialoorosomucoid remained blocked for at least 90 min after excess antibody was removed from the perfusion system, the total hepatic content of functional binding protein was nearly normal. These results indicate that interaction with specific cell surface lectin is essential for removal of asialoorosomucoid from the circulation. During the 90 min following infusion of antibody, no functional lectin is restored to the surface of hepatocytes.

Original languageEnglish (US)
Pages (from-to)3830-3831
Number of pages2
JournalJournal of Biological Chemistry
Volume255
Issue number9
StatePublished - 1980

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Asialoglycoproteins
Liver
Rats
Lectins
Antibodies
Bilirubin
Asialoglycoprotein Receptor
Liver Circulation
N-Acetylneuraminic Acid
Portal Vein
Hepatocytes
Glycoproteins
Carrier Proteins
Perfusion
Membranes
Injections
asialoorosomucoid

ASJC Scopus subject areas

  • Biochemistry

Cite this

Effects of receptor-specific antibody on the uptake of desialylated glycoproteins in the isolated perfused rat liver. / Stockert, R. J.; Gartner, U.; Morell, A. G.; Wolkoff, Allan W.

In: Journal of Biological Chemistry, Vol. 255, No. 9, 1980, p. 3830-3831.

Research output: Contribution to journalArticle

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AB - Removal of the terminal sialic acid residues from most mammalian glycoproteins results in their rapid transfer from the circulation into the liver. In vitro, these desialylated glycoproteins bind to a specific membrane-associated hepatic lectin which has a ubiquitous distribution within the liver cell. In the present study, infusion of a specific antibody to the purified lectin into the portal vein of an isolated perfused rat liver prior to injection of radiolabeled asialoorosomucoid or bilirubin reduced the rate of influx of asialoorosomucoid into the liver by over 80%, while the influx of bilirubin was unchanged. Although uptake of asialoorosomucoid remained blocked for at least 90 min after excess antibody was removed from the perfusion system, the total hepatic content of functional binding protein was nearly normal. These results indicate that interaction with specific cell surface lectin is essential for removal of asialoorosomucoid from the circulation. During the 90 min following infusion of antibody, no functional lectin is restored to the surface of hepatocytes.

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