Intracellular site of asialoglycoprotein receptor-ligand uncoupling: Double-label immunoelectron microscopy during receptor-mediated endocytosis

Geuze, Hans J.; Slot, Jan W.; Strous, Ger J.; Lodish, Harvey F.; Schwartz, Alan L.

doi:10.1016/0092-8674(83)90518-4

Cited by 776 publications

(429 citation statements)

References 35 publications

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“…Antibodies We used affinity-purified well characterized rabbit antibodies against ASGP-13 ( Schwartz et al, 1981;Geuze et al, 1963a), MP-R (Geuze et al, submitted), SC (free and bound) (ISA-R) (Ortans et al, 1979). fetuin (Geuze et al, 1963a), the heavy chain of IgA (Orlans et al.…”

Section: Methodsmentioning

confidence: 99%

“…1961). Background labeling as judged from sections labeled with anti-rat pancreas amylase and interference between the labeling steps was neglrgible (Geuze et al, 1963a).…”

Section: Animals and Tissuementioning

confidence: 98%

“…Experimental rats were treated as detailed previously (Geuze et al, 1963a). These animals recerved a continuous tail-vein infusion of ASF at 106 ag/ min.…”

Section: Animals and Tissuementioning

confidence: 99%

See 2 more Smart Citations

Intracellular receptor sorting during endocytosis: Comparative immunoelectron microscopy of multiple receptors in rat liver

Geuze¹,

Slot²,

Strous³

et al. 1984

Cell

Self Cite

356

198

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Section: Methodsmentioning

confidence: 99%

“…1961). Background labeling as judged from sections labeled with anti-rat pancreas amylase and interference between the labeling steps was neglrgible (Geuze et al, 1963a).…”

Section: Animals and Tissuementioning

confidence: 98%

See 1 more Smart Citation

Intracellular receptor sorting during endocytosis: Comparative immunoelectron microscopy of multiple receptors in rat liver

Geuze¹,

Slot²,

Strous³

et al. 1984

Cell

Self Cite

356

198

View full text Add to dashboard Cite

“…Additionaly, the stained glycoproteins within the epithelial cells of the vas deferens might correspond either to structural proteins or to proteins reabsorbed from the lumen and contained in endosomes and endolysosomes [4][5]. Endosomes have been shown to be involved in the sorting and recycling of receptors and ligands via small tubular extensions [22].…”

Section: Discussionmentioning

confidence: 99%

Untitled

Arenas

Madrid

Bethencourt

et al. 1998

Glycoconjugate Journal

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“…After internalization of the ligand-receptor complex and the formation of endosomes, ligands and their receptors are dissociated and segregated (Brown et al, 1983;Geuze et al, 1983;Presky & Schonbrunn, 1986). Numerous reports have demonstrated degradation of ligands and ligand-receptor complexes by the action of several enzymes (King et al, 1980;Heldin et al, 1982;Walker & Burgress, 1987).…”

Section: Discussionmentioning

confidence: 99%

Characterization of ligand binding and processing by gastrin-releasing peptide receptors in a small-cell lung cancer cell line

Cardona

Bleehen

Reeve

1992

Biochemical Journal

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The ligand-binding properties of the gastrin-releasing peptide (GRP) receptor and the cellular processing of GRP have been studied in the small-cell lung cancer (SCLC) cell line COR-L42. Scatchard analysis of GRP receptor expression indicated a single class of high-affinity receptors (Kd 1.5 nM) and approx. 6700 receptors/cell. GRP bound to its receptor with a K1 of 2.4 nm. The bombesin-related peptides neuromedin B (NMB) and phyllolitorin also bound to GRP receptors with K, values of 22.7 and 59.1 nm respectively. Binding of 125I-GRP to COR-L42 cells increased rapidly at 37°C, achieved a maximum at 10 min and declined rapidly thereafter. At 4°C, maximum binding was achieved at 30 min and the subsequent decline in cell-associated radioactivity was slower than that seen at 37 'C. Acid/salt extraction, to separate surface-bound ligand from internalized GRP, indicated that after receptor binding 125I-GRP was rapidly internalized. To determine the pathway of 125I-GRP degradation, binding studies were carried out with the lysosomotropic agent chloroquine (5 mM), and with phosphoramidon (10,UM), an inhibitor of the membrane-bound enzyme (EC 3.4.24.11).Both agents markedly inhibited the degradation of GRP, indicating that this process involves a lysosomal pathway and a phosphoramidon-sensitive pathway, possibly involving the EC 3.4.24.11 enzyme. GRP receptor down-regulation was observed following a 10 min exposure to 100 nM-GRP. With longer pretreatment times the number of binding sites recovered to 80 % of control values. Treatment with S mM-chloroquine plus GRP or cycloheximide (10,ig/ml) plus GRP demonstrated that the majority of GRP receptors are recycled. NMB and phyllolitorin pretreatment did not influence the subsequent binding of 125I-GRP, suggesting that these peptides do not down-regulate GRP receptors.

show abstract

Intracellular site of asialoglycoprotein receptor-ligand uncoupling: Double-label immunoelectron microscopy during receptor-mediated endocytosis

Cited by 776 publications

References 35 publications

Intracellular receptor sorting during endocytosis: Comparative immunoelectron microscopy of multiple receptors in rat liver

Intracellular receptor sorting during endocytosis: Comparative immunoelectron microscopy of multiple receptors in rat liver

Untitled

Characterization of ligand binding and processing by gastrin-releasing peptide receptors in a small-cell lung cancer cell line

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