Sulfation in the Golgi Lumen of Madin-Darby Canine Kidney Cells Is Inhibited by Brefeldin A and Depends on a Factor Present in the Cytoplasm and on Golgi Membranes

Fjeldstad, Katja; Pedersen, Mona Elisabeth; Vuong, Tram Thu; Kolset, Svein Olav; Nordstrand, Line Mari; Prydz, Kristian

doi:10.1074/jbc.m206365200

Cited by 19 publications

(15 citation statements)

References 45 publications

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“…Thus, we analyzed the role of changes in sulfation on the proliferation and differentiation potential of mouse embryonic spinal cord NPC using NaClO 3 as a potent inhibitor of eukaryotic sulfation reactions. Low concentrations of NaClO 3 (2 mM to 5 mM) preferentially inhibit sulfation of CS-GAGs, whereas higher concentrations (15 mM to 30 mM) are required to inhibit sulfation of HS-GAGs as well [39]. We used a concentration of 30 mM, to assure an almost complete sulfation blockage of both CS-GAGs and HS-GAGs.…”

Section: Discussionmentioning

confidence: 99%

Normal sulfation levels regulate spinal cord neural precursor cell proliferation and differentiation

et al. 2012

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BackgroundSulfated glycosaminoglycan chains are known for their regulatory functions during neural development and regeneration. However, it is still unknown whether the sulfate residues alone influence, for example, neural precursor cell behavior or whether they act in concert with the sugar backbone. Here, we provide evidence that the unique 473HD-epitope, a representative chondroitin sulfate, is expressed by spinal cord neural precursor cells in vivo and in vitro, suggesting a potential function of sulfated glycosaminoglycans for spinal cord development.ResultsThus, we applied the widely used sulfation inhibitor sodium chlorate to analyze the importance of normal sulfation levels for spinal cord neural precursor cell biology in vitro. Addition of sodium chlorate to spinal cord neural precursor cell cultures affected cell cycle progression accompanied by changed extracellular signal-regulated kinase 1 or 2 activation levels. This resulted in a higher percentage of neurons already under proliferative conditions. In contrast, the relative number of glial cells was largely unaffected. Strikingly, both morphological and electrophysiological characterization of neural precursor cell-derived neurons demonstrated an attenuated neuronal maturation in the presence of sodium chlorate, including a disturbed neuronal polarization.ConclusionsIn summary, our data suggest that sulfation is an important regulator of both neural precursor cell proliferation and maturation of the neural precursor cell progeny in the developing mouse spinal cord.

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Section: Discussionmentioning

confidence: 99%

Normal sulfation levels regulate spinal cord neural precursor cell proliferation and differentiation

et al. 2012

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“…However, a little-cited pleiotropic effect of BFA is the complete inhibition of the Golgi uptake of the activated substrate of TPST, PAPS (adenosine 3′-phosphate 5′-phosphosulfate) [51] and a total abrogation of protein sulfation [52]. The fact that the TPSTs continue to act upon their substrates in the presence of Exo2, as shown in the present paper and elsewhere [18], may therefore reflect either their relocation to the ER membrane or the action of TPST in the fragmented TGN, although we cannot detect its presence in the TGN in the experiments described here (Figure 8).…”

Section: Discussionmentioning

confidence: 99%

The secretion inhibitor Exo2 perturbs trafficking of Shiga toxin between endosomes and the trans-Golgi network

Spooner

Watson

Smith

et al. 2008

Biochemical Journal

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The small-molecule inhibitor Exo2 {4-hydroxy-3-methoxy-(5,6,7,8-tetrahydrol[1]benzothieno[2,3-d]pyrimidin-4-yl)hydraz-one benzaldehyde} has been reported to disrupt the Golgi apparatus completely and to stimulate Golgi–ER (endoplasmic reticulum) fusion in mammalian cells, akin to the well-characterized fungal toxin BFA (brefeldin A). It has also been reported that Exo2 does not affect the integrity of the TGN (trans-Golgi network), or the direct retrograde trafficking of the glycolipid-binding cholera toxin from the TGN to the ER lumen. We have examined the effects of BFA and Exo2, and found that both compounds are indistinguishable in their inhibition of anterograde transport and that both reagents significantly disrupt the morphology of the TGN in HeLa and in BS-C-1 cells. However, Exo2, unlike BFA, does not induce tubulation and merging of the TGN and endosomal compartments. Furthermore, and in contrast with its effects on cholera toxin, Exo2 significantly perturbs the delivery of Shiga toxin to the ER. Together, these results suggest that the likely target(s) of Exo2 operate at the level of the TGN, the Golgi and a subset of early endosomes, and thus Exo2 provides a more selective tool than BFA for examining membrane trafficking in mammalian cells.

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“…Cultivation of cells in sulfate-free medium and addition of sodium chlorate inhibits effective sulfation of CSPGs and HSPGs in a dose-dependent manner. It has been reported that low concentrations of chlorate (3-5 mM) reduced mainly sulfation of CSPG, while higher chlorate concentrations (10 mM) are needed for inhibition of HSPG sulfation (Fjeldstad et al, 2002). Furthermore, inhibition of sulfation of HSPGs was shown to significantly decrease infection with vaccinia virus (Chung et al, 1998) and inhibits adeno-associated virus 2 infection (Qiu et al, 2000) in vitro.…”

Section: Role Of Sulfation Of Hepatocellular Proteoglycans For Hbv Inmentioning

confidence: 99%

Role of glycosaminoglycans for binding and infection of hepatitis B virus

Leistner

Gruen-Bernhard

Glebe³

2007

Cell Microbiol

133

148

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SummaryMany parts of the life cycle of hepatitis B virus (HBV) infection of hepatocytes have been unravelled, but the attachment and entry process leading to infection is largely unknown. Using primary Tupaia hepatocyte cultures as an in vitro infection system, we determined that HBV uses cell-surface heparan sulfate proteoglycans as low-affinity receptor, because HBV infection was inhibited by heparin (IC50: 5 mg ml -1 ) or other higher-sulfated polymers, but not by lowersulfated glycosaminoglycans, such as chondroitin sulfate. Pretreatment of primary hepatocytes with heparinase decreased viral binding and inhibited HBV infection completely. Interestingly, after preS1-dependent viral binding at 16°C to the cell surface, subsequent infection could still be inhibited by HBV preS1-lipopeptides, but not by heparin any more, suggesting a shift of the virus to a high-affinity receptor. In summary, we suggest following multistep attachment process: in vivo, HBV is initially trapped within the liver in the space of Dissé by heparan sulfate proteoglycans. Thereafter, HBV binds via its preS1 attachment site and the N-terminal myristic acid to a yet unknown, high-affinity receptor that confers uptake in a yet unknown compartment.

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Sulfation in the Golgi Lumen of Madin-Darby Canine Kidney Cells Is Inhibited by Brefeldin A and Depends on a Factor Present in the Cytoplasm and on Golgi Membranes

Cited by 19 publications

References 45 publications

Normal sulfation levels regulate spinal cord neural precursor cell proliferation and differentiation

Normal sulfation levels regulate spinal cord neural precursor cell proliferation and differentiation

The secretion inhibitor Exo2 perturbs trafficking of Shiga toxin between endosomes and the trans-Golgi network

Role of glycosaminoglycans for binding and infection of hepatitis B virus

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