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

Matlin, Karl S.; Bainton, Dorothy F.; Pesonen, Marja; Louvard, Daniel; Genty, Nicole; Simons, Kai

doi:10.1083/jcb.97.3.627

Cited by 104 publications

(58 citation statements)

References 38 publications

(38 reference statements)

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“…BFA did stimulate to some extent cellular accumulation of HRP in highly confluent MDCK cells grown on plastic (not shown). Under these conditions the plasma membrane facing the medium bears resemblance to the apical membrane of truly polarized MDCK cells (22).…”

Section: Ultrastructural Analysis Of Endosomes and Lysosomes In Bfa-tmentioning

confidence: 99%

Effects of brefeldin A on endocytosis, transcytosis and transport to the Golgi complex in polarized MDCK cells.

Prydz

Hansen

Sandvig

et al. 1992

The Journal of Cell Biology

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Abstract. We have studied the effects of brefeldin A (BFA) on endocytosis and intracellular traffic in polarized MDCK cells by using the galactose-binding protein toxin ricin as a membrane marker and HRP as a marker of fluid phase transport. We found that BFA treatment rapidly increased apical endocytosis of both ricin and HRP, whereas basolateral endocytosis was unaffected, as was endocytosis of HRP in the poorly polarized carcinoma cell lines HEp-2 and T47D. Tubular endosomes were induced by BFA both apically and basolaterally in some MDCK cells, comparable with those seen in HEp-2 and T47D cells. In addition, in MDCK cells, BFA induced formation of small (<300 nm) vesicles, labeled both after apical and basolateral uptake of HRP, as well as some very large (>700 nm) vacuoles, which were only labeled when HRP was present in the apical medium. In contrast, neither in MDCK nor in HEp-2 or T47D cells, did BFA have any effect on lysosomal morphology. Moreover, transcytosis in the basolateral-apical direction was stimulated both for HRP and ricin. Other vesicular transport routes were less affected or unaffected by BFA treatment. Two closely related structural analogues of BFA (B16 and B21), unable to produce the changes in Golgi and endosomal morphology seen after BFA treatment in a number of different cell lines, were also unable to mimic the effects of BFA on MDCK ceils. well documented effect of the fungal metabolite brefeldin A (BFA) ~ on mammalian ceils is rapid dissociation of proteins associated with the cytosolic face of the Golgi apparatus (7-9), and a subsequent retrograde movement of components of the cis-, medial, and trans-Golgi stacks back into the ER (6,10,17,18,24). However, markers of the trans-Golgi network (TGN), do not move along to the ER upon BFA treatment (5,6,18,32).Recently, it was reported that BFA transforms the morphology of endosomes, lysosomes, and the TGN in normal rat kidney (NRK) cells into more tubular structures (19,44). Studies on the distribution of the TGN 38-protein have shown that BFA treatment may also give a more compact TGN 38 immunofluorescence around the microtubule organizing center (19,28).Two kidney epithelial cell lines (PtK and MDCK) have Golgi stacks that appear to be morphologically resistant to BFA (15,16,32). However, BFA treatment does cause formation of tubular endosomes in both cell lines, suggesting that the effect of BFA on endosomes is not directly coupled to the effect on the Golgi apparatus (15,19).In MDCK cells there are two distinct populations of early endosomes localized close to the apical and the basolateral surface domains, respectively. Markers of apical and baso-1. Abbreviations used in this paper: BFA, brefeldin A; TGN, trans-Golgi network; TER, transepithelial resistance. lateral endocytosis are therefore initially separated, before they enter mannose-6-phosphate receptor-rich late endosomes and lysosomes shared by the two pathways (3,26,42). Early apical and early basolateral endosomes display differences in their fusion machineries and in t...

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Section: Ultrastructural Analysis Of Endosomes and Lysosomes In Bfa-tmentioning

confidence: 99%

Effects of brefeldin A on endocytosis, transcytosis and transport to the Golgi complex in polarized MDCK cells.

Prydz

Hansen

Sandvig

et al. 1992

The Journal of Cell Biology

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“…Further, studies on epithelial cells showed that GSL [12][13][14] and glycosylphosphatidylinositol (GPI)-anchored proteins [15,16] were preferentially target to the apical membrane. Moreover, biologically active membrane proteins were found to be associated with surrounding GSLs [17].…”

Section: Gsl-enriched Microdomains: From Caveolae To Raft To Glycosmentioning

confidence: 99%

“…1. First observations of polarized sorting of GSL [12][13][14] and glycoproteins [15,16] in epithelial cells. 2.…”

Section: Supplementary Materialsmentioning

confidence: 99%

Functional role of glycosphingolipids and gangliosides in control of cell adhesion, motility, and growth, through glycosynaptic microdomains

Todeschini

Hakomori

2008

Biochimica et Biophysica Acta (BBA) - General Subjects

381

257

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At cell surface microdomains, glycosyl epitopes, carried either by glycosphingolipids, N-or O-linked oligosaccharides, are recognized by carbohydrate-binding proteins or complementary carbohydrates. In both cases, the carbohydrate epitopes may be clustered with specific signal transducers, tetraspanins, adhesion receptors or growth factor receptors. Through this framework, carbohydrates can mediate cell signaling leading to changes in cellular phenotype. Microdomains involved in carbohydrate-dependent cell adhesion inducing cell activation, motility, and growth are termed "glycosynapse". In this review a historical synopsis of glycosphingolipids-enriched microdomains study leading to the concept of glycosynapse is presented. Examples of glycosynapse as signaling unit controlling the tumor cell phenotype are discussed in three contexts:(i) Cell-to-cell adhesion mediated by glycosphingolipids-to-glycosphingolipids interaction between interfacing glycosynaptic domains, through head-to-head (trans) carbohydrate-to-carbohydrate interaction.(ii) Functional role of GM3 complexed with tetraspanin CD9, and interaction of such complex with integrins, or with fibroblast growth factor receptor, to control tumor cell phenotype and its reversion to normal cell phenotype.(iii) Inhibition of integrin-dependent Met kinase activity by GM2/tetraspanin CD82 complex in glycosynaptic microdomain.Data present here suggest that the organizational status of glycosynapse strongly affects cellular phenotype influencing tumor cell malignancy.

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“…To generate radioactively labeled retrovirus for binding studies, purification of retrovirus is required. We addressed this requirement by applying a method previously described for the purification of vesicular stomatitis virus (17) that uses ultracentrifugation and a sucrose-step gradient to purify viral particles within the interphase of the gradient. First, localization of infectious retrovirus in the different fractions of the gradient after centrifugation was analyzed.…”

Section: Fibronectin Fragments Have Been Shown To Improve Retrovirus mentioning

confidence: 99%

Heparin Inhibits Retrovirus Binding to Fibronectin as Well as Retrovirus Gene Transfer on Fibronectin Fragments

Carstanjen

Dutt

Möritz

2001

J Virol

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Fibronectin fragments have been shown to improve retrovirus gene transfer efficiency by binding retrovirus and target cells. Using a novel virus adhesion assay, we confirmed binding of type C oncoretrovirus vectors to the heparin II domain of fibronectin and demonstrated inhibition of viral binding and gene transfer by heparin.Fibronectin (FN) fragments have been shown to improve retrovirus gene transfer into primitive hematopoietic cells, including murine (9, 20) and primate (10) long-term repopulating stem cells or human cells repopulating immunodeficient NOD-SCID or BNX mice (7,12). The technology has also been applied successfully to clinical studies (1, 5). The underlying biological mechanism has at least partly been resolved, as it was demonstrated that FN binds not only hematopoietic target cells (26, 27) but also recombinant retrovirus particles (9, 18). For this reason, colocalization of retrovirus and target cells on the FN fragments has been proposed as the mechanism responsible for improved retrovirus transduction of hematopoietic cells in the presence of FN (9, 18). The putative site for retrovirus binding is localized within type III repeats 12 to 14 of FN, containing the high-affinity heparin II (Hep-II) domain ( Fig. 1) (11,29). FN fragments combining the Hep-II domain with domains allowing integrin-mediated cell binding, such as the central cell binding domain or the type III repeatconnecting segment region ( Fig. 1), are most active in enhancing retrovirus gene transfer efficiency (9).Given the importance of the Hep-II -domain in this colocalization model, we were interested in investigating heparin as a potential inhibitor of retrovirus binding and, consequently, retrovirus transduction on FN fragments. Inhibitory effects of heparin and other sulfated polysaccharides on infection have been reported for other enveloped viruses, such as human immunodeficiency virus type 1 (6), cytomegalovirus (2), and Rous sarcoma virus (25). During lentivirus infection, heparin seems to interfere with intracellular events necessary for viral replication (6), whereas in the case of Rous sarcoma virus, negatively charged sulfated proteoglycans inhibit infection most likely through electrostatic inhibition of viral adsorption to the cell surface (25).So far, most studies investigating the binding of retrovirus to FN have applied indirect methods using transduction efficiency for NIH 3T3 fibroblasts, which were added to FN-bound virus, as the readout (9, 18). More-direct evidence of retrovirusbinding to FN was provided by studies demonstrating binding of the retrovirus envelope protein gp70 using enzyme-linked immunosorbent assay technology (14). For the studies presented here, a radioactive virus binding assay, that allows direct and quantitative detection of virus bound to FN and is independent of downstream steps of infection was developed. This seems warranted, as viral infection is a multistep process and competitors of viral binding might also interfere with other downstream events in the viral infectious cyc...

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

Cited by 104 publications

References 38 publications

Effects of brefeldin A on endocytosis, transcytosis and transport to the Golgi complex in polarized MDCK cells.

Effects of brefeldin A on endocytosis, transcytosis and transport to the Golgi complex in polarized MDCK cells.

Functional role of glycosphingolipids and gangliosides in control of cell adhesion, motility, and growth, through glycosynaptic microdomains

Heparin Inhibits Retrovirus Binding to Fibronectin as Well as Retrovirus Gene Transfer on Fibronectin Fragments

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