The galactose-specific recognition system of mammalian liver: The route of ligand internalization in rat hepatocytes

Wall, Doris A.; Wilson, Glynn; Hubbard, Ann L.

doi:10.1016/0092-8674(80)90116-6

Cited by 471 publications

(242 citation statements)

References 35 publications

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“…The coated vesicles were rapidly uncoated and fused with the tubules in the sinusoidal portions of hepatocytes. Such processes are consistent with those found in rat hepatocytes during the endocytosis of proteins destined for excretion into bile (IgA) (32,38) and for degradation in lysosomes (asialoglycoprotein) (36,43).…”

Section: Discussionsupporting

confidence: 70%

Cytochemical examination of the compartments involved in the transcellular transport of horseradish peroxidase in rat hepatocytes.

Mori

Yamaguchi

Oyamada

et al. 1990

Cell Struct. Funct.

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ABSTRACT,horseradish peroxidase (HRP, 10 mg/100 g body weight) was intravenously injected into rats in order to investigate the nature of the compartmens involved in the transcellular transport of the protein through hepatocytes into bile. Double cytochemistry for HRPand the marker enzymesfor cytoplasmic orgattelles was used. HRPwas shown to be taken up by hepatocytes via vesicles at the sinusoidal surface, some of which were positive for 5 -nucleotiddse activity. HRPwas then found in the smooth-surfaced vesicles and tubules which were negative in 5 -nucleotidase, glucose 6-phosphatase, thiamine pyrophosphatase and acid phosphatase activity, suggesting that the tubular structures are neither the endoplasmic reticulum, the Golgi apparatus nor lysosomes. Biochemical studies revealed that the lead procedures used for the double cytochemistry did not inhibit the peroxidatic activity of HRP, and conversely that HRPdid not interfere with the marker enzyme activity. Such cytochemical observations seemed to be supported by the observation that administration of monensin (3.5 mg/100 g) and chloroquine (5 mg/100 g), which markedly aletered the structure of the Golgi apparatus and lysosomes, respectively, slightly altered the biliary excretion of HRPbut not to a significant extent.

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Section: Discussionsupporting

confidence: 70%

Cytochemical examination of the compartments involved in the transcellular transport of horseradish peroxidase in rat hepatocytes.

Mori

Yamaguchi

Oyamada

et al. 1990

Cell Struct. Funct.

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“…Others have also observed the endocytosis of probes and liga~ds into vacuoles morphologically similar to those described here (12,45,48). In particular Van Deurs et al (42) reported that cationized ferritin initially entered electronlucent endocytic vacuoles and "light" multivesicular bodies containing some vesicular profiles, and only later could been seen in "dark" multivesicular bodies and dense bodies.…”

Section: Endocytosismentioning

confidence: 81%

Transepithelial transport of a viral membrane glycoprotein implanted into the apical plasma membrane of Madin-Darby canine kidney cells. I. Morphological evidence.

Matlin¹,

Bainton²,

Pesonen³

et al. 1983

The Journal of Cell Biology

104

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The G protein of vesicular stomatitis virus was implanted in the apical plasma membrane of Madin-Darby canine kidney cells by low pH-dependent fusion of the viral envelope with the cellular membrane. The amount of fusion as determined by removal of unfused virions, either by tryptic digestion or by EDTA treatment at 0°C, was 22-24% of the cell-bound virus radioactivity. Upon incubation of cells after implantation, the amount of G protein as detected by immunofluorescence diminished on the apical membrane and appeared within 30 min on the basolateral membrane. At the same time some G protein fluorescence was also seen in intracellular vacuoles. The observations by immunofluorescence were confirmed and extended by electron microscopy. Using immunoperoxidase localization, G protein was seen to move into irregularly shaped vacuoles (endosomes) and multivesicular bodies and to appear on the basolateral plasma membrane. These results suggest that the apical and basolateral domains of Madin-Darby canine kidney cells are connected by an intracellular route.In most cells the plasma membrane is continuously endocytosed (36) and the loss of surface membrane must be balanced by retrieval of membrane from inside the cell. Membrane recycling poses a special problem in epithelial cells because the plasma membrane is polarized; it is divided into apical and basolateral domains with distinct protein and lipid compositions (35). If the plasma membrane is continuously recycling, an important question is how the apical and basolateral domains preserve their unique compositions. If the apical and the basolateral recycling routes are separated, randomization of the cell surface would of course be prevented. If, however, they connect at some point in the cell, continuous sorting of apical and basolateral proteins would have to take place.In an attempt to map the membrane traffic routes to and from the cell surface in epithelial cells, we are using the MadinDarby canine kidney (MDCK) cell line as our experimental system (7, 16). These cells display both structural and functional polarity when grown in culture (24, 32). The microvillar

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“…The high specificity (91 ± 7%) of the chemically synthesised NGA-ligand binding to normal liver tissue has provided the basis for studying changes in receptor density in cancer patients with or without liver metastasis. It is known that, once bound at the surface by HBP, glycoproteins are internalised and transported to prelysosomal vesicles where the majority of the ligand-receptor complex dissociates by a change to an acid pH (Wall et al, 1980). Thereafter, the receptor recycles to the plasma mem-brane (cell surface) while the ligand is degraded in the lysosomal compartment (Haimes et al, 1981).…”

Section: Discussionmentioning

confidence: 99%

Decreased hepatic function in patients with hepatoma or liver metastasis monitored by a hepatocyte specific galactosylated radioligand

Virgolini

Müller²,

Klepetko³

et al. 1990

Br J Cancer

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The galactose-specific recognition system of mammalian liver: The route of ligand internalization in rat hepatocytes

Cited by 471 publications

References 35 publications

Cytochemical examination of the compartments involved in the transcellular transport of horseradish peroxidase in rat hepatocytes.

Cytochemical examination of the compartments involved in the transcellular transport of horseradish peroxidase in rat hepatocytes.

Transepithelial transport of a viral membrane glycoprotein implanted into the apical plasma membrane of Madin-Darby canine kidney cells. I. Morphological evidence.

Decreased hepatic function in patients with hepatoma or liver metastasis monitored by a hepatocyte specific galactosylated radioligand

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