scholarly journals Transport of phagosomal components to an endosomal compartment.

1992 ◽  
Vol 267 (1) ◽  
pp. 126-132
Author(s):  
A Pitt ◽  
L S Mayorga ◽  
A L Schwartz ◽  
P D Stahl
Keyword(s):  
Endosomal Compartment

scholarly journals Endocytic pathways in polarized Caco-2 cells: identification of an endosomal compartment accessible from both apical and basolateral surfaces.

1990 ◽  
Vol 110 (2) ◽  
pp. 337-348 ◽  
Author(s):  
E J Hughson ◽  
C R Hopkins
Keyword(s):  
Cell Line ◽  
Concanavalin A ◽  
Transferrin Receptor ◽  
Apical Surface ◽  
Double Labeling ◽  
Endocytic Compartment ◽  
Endosomal Compartment ◽  
Apical Cytoplasm ◽  
Peroxidase Conjugate ◽  
Endocytic Pathways

The enterocyte-like cell line Caco-2 forms a polarized epithelium when grown on filters. We have investigated the interaction of endocytic pathways from the apical and basolateral surfaces. The transferrin receptor was an appropriate marker for the basolateral route; uptake of radiolabeled transferrin was highly polarized, and recycling of this ligand back to the basolateral surface occurred with an efficiency of 95%, even after prolonged incubations with transferrin. Using a transferrin-peroxidase conjugate to delineate the morphological pathway, we have identified an early endocytic compartment in the basolateral cytoplasm of the cells. Longer incubations revealed a deeper endocytic compartment in the apical cytoplasm. Concanavalin A complexed to gold was used to simultaneously label the apical endocytic route. After 60 min, extensive mixing of the two labels was seen in endocytic elements throughout the apical cytoplasm, including in the Golgi area, but never in the basal cytoplasm. Using a second double labeling procedure in which antitransferrin receptor antibody complexed to gold was applied to the basolateral surface for up to 2 h and free peroxidase applied to the apical surface for shorter periods, we demonstrated that this apical marker rapidly (within 5 min) reached endosomes containing antibody-gold. Our results indicate that, in Caco-2 cells, the endocytic pathways from the apical and basolateral surfaces meet in an endosomal compartment from which transferrin can still be recycled.

The endosomal compartment of rat hepatocytes

1985 ◽  
Vol 159 (1) ◽  
pp. 113-126 ◽  
Author(s):  
Alec Robert ◽  
Jean-Louis Carpentier ◽  
Emmanuel Van Obberghen ◽  
Bertrand Canivet ◽  
Phillip Gorden ◽  
...  
Keyword(s):  
Rat Hepatocytes ◽  
Endosomal Compartment

scholarly journals Syntaxin 7, a Novel Syntaxin Member Associated with the Early Endosomal Compartment

1998 ◽  
Vol 273 (1) ◽  
pp. 375-380 ◽  
Author(s):  
Siew Heng Wong ◽  
Yue Xu ◽  
Tao Zhang ◽  
Wanjin Hong
Keyword(s):  
Endosomal Compartment

scholarly journals Intracellular Trafficking of Adeno-Associated Virus Vectors: Routing to the Late Endosomal Compartment and Proteasome Degradation

2001 ◽  
Vol 75 (4) ◽  
pp. 1824-1833 ◽  
Author(s):  
Anne-Marie Douar ◽  
Karine Poulard ◽  
Daniel Stockholm ◽  
Olivier Danos
Keyword(s):  
Intracellular Trafficking ◽  
Fluorescent Protein ◽  
Growth Factor Receptor ◽  
Brefeldin A ◽  
Transduction Efficiency ◽  
Single Stranded Dna ◽  
Adeno Associated Virus ◽  
Surface Receptors ◽  
Endosomal Compartment ◽  
Green Fluorescent

ABSTRACT The early steps of adeno-associated virus (AAV) infection involve attachment to a variety of cell surface receptors (heparan sulfate, integrins, and fibroblast growth factor receptor 1) followed by clathrin-dependent or independent internalization. Here we have studied the subsequent intracellular trafficking of AAV particles from the endosomal compartment to the nucleus. Human cell lines were transduced with a recombinant AAV (rAAV) carrying a reporter gene (luciferase or green fluorescent protein) in the presence of agents that affect trafficking. The effects of bafilomycin A1, brefeldin A, and MG-132 were measured. These drugs act at the level of endosome acidification, early-to-late endosome transition, and proteasome activity, respectively. We observed that the transducing virions needed to be routed as far as the late endosomal compartment. This behavior was markedly different from that observed with adenovirus particles. Antiproteasome treatments with MG-132 led to a 50-fold enhancement in transduction efficiency. This effect was accompanied by a 10-fold intracellular accumulation of single-stranded DNA AAV genomes, suggesting that the mechanism of transduction enhancement was different from the one mediated by a helper adenovirus, which facilitates the conversion of the rAAV single-stranded DNA genome into its replicative form. MG-132, a drug currently in clinical use, could be of practical use for potentializing rAAV-mediated delivery of therapeutic genes.

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