Protein Uptake and Cytoplasmic Access in Animal Cells

Deurs, Bo van; Hansen, Steen Ingemann; Olsnes, Sjur; Sandvig, Kirsten

doi:10.1007/978-1-4615-2898-2_4

Cited by 6 publications

(9 citation statements)

References 168 publications

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“…Similar results are obtained by using cell fractionation performed on cells incubated with radioactively labeled toxin [8,15]. It should be mentioned that gold-labeled ricin is not transported to the TGN [29]; this conjugate is exclusively routed to the lysosomes. Also, multivalent conjugates of ricin and HRP were similarly routed to lysosomes [29].…”

Section: Nansport To the Tram-golgi Networksupporting

confidence: 73%

“…By using EM one can visualize transport of toxin-HRP conjugates to the TGN, and quantifi- cation by immunogold-labeling shows that 5-10% of the endocytosed toxin actually enters the TGN in 1 h [29]. Similar results are obtained by using cell fractionation performed on cells incubated with radioactively labeled toxin [8,15].…”

Section: Nansport To the Tram-golgi Networkmentioning

confidence: 62%

“…Since there is evidence that ricin and Shiga toxin (and a number of other toxins as well) are transported to the trans-Golgi network as a necessary step on their way to the cytosol [7,29,31] this transport has been studied by several methods. By using EM one can visualize transport of toxin-HRP conjugates to the TGN, and quantifi- cation by immunogold-labeling shows that 5-10% of the endocytosed toxin actually enters the TGN in 1 h [29].…”

Section: Nansport To the Tram-golgi Networkmentioning

confidence: 99%

“…It should be mentioned that gold-labeled ricin is not transported to the TGN [29]; this conjugate is exclusively routed to the lysosomes. Also, multivalent conjugates of ricin and HRP were similarly routed to lysosomes [29]. Thus, the valency clearly affects the routing, and it is therefore important to use monovalent conjugates.…”

Section: Nansport To the Tram-golgi Networkmentioning

confidence: 99%

“…At lower temperature (below lVC), when toxin transport to this organelle is inhibited [29,32], the cells are protected against ricin and Shiga toxin [29] but not against diphteria toxin, which is believed to enter the cytosol from endosomes upon acidification [33]. Also, hybridoma cells producing anti-&in antibody are protected against the toxin, presumably because ricin meets the antibody in the Golgi apparatus [34].…”

Section: Nansport To the Tram-golgi Networkmentioning

confidence: 99%

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Endocytosis and intracellular sorting of ricin and Shiga toxin

Sandvig

Deurs

1994

FEBS Letters

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AkstraetRicin and Shiga toxin belong to a group of protein toxins with targets in the cytosol. These toxins consist of one moiety that binds the toxin molecule to cell surface receptors, and another enzymatically active moiety that enters the cytosol after endocytic uptake of the toxin. The toxins are of current interest in relation to disease and the construction of immunotoxins. Moreover, they have proven useful to investigate mechanisms of endocytosis and to follow intracellular pathways of transport. Some of the recent results obtained with ricin and Shiga toxin are discussed.

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Section: Nansport To the Tram-golgi Networksupporting

confidence: 73%

Section: Nansport To the Tram-golgi Networkmentioning

confidence: 62%

Section: Nansport To the Tram-golgi Networkmentioning

confidence: 99%

Section: Nansport To the Tram-golgi Networkmentioning

confidence: 99%

Section: Nansport To the Tram-golgi Networkmentioning

confidence: 99%

See 3 more Smart Citations

Endocytosis and intracellular sorting of ricin and Shiga toxin

Sandvig

Deurs

1994

FEBS Letters

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Endosomal ricin transport: involvement of Rab4- and Rab5-positive compartments

Moisenovich

Tonevitsky

Maljuchenko

et al. 2004

Histochem Cell Biol

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Transport of the ribosome-inactivating protein ricin through endosomes was studied in A431 cells expressing Rab5-, Rab4-, and Rab11-GFP. It was shown that Rab5- and Rab4-positive functional domains of early endosomes are involved in ricin transport. Ricin enters cells by both clathrin-dependent and clathrin-independent mechanisms. The main pool of internalized toxin accumulates in early endosomes and remains associated with them for a long time. In contrast to earlier observations, current observations indicate that the majority of ricin avoids transport to lysosomes. The low level of ricin association with Rab11 as well as with transferrin accumulated in the pericentriolar recycling compartment shows that the compartment is not responsible for keeping ricin away from degradation in lysosomes. Escape from degradation in lysosomes is assumed to result from the potentiality of ricin to form assemblies within compartments.

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Passive delivery of protein drugs through transdermal route

Chaulagain

Jain

Tiwari

et al. 2018

Artificial Cells, Nanomedicine, and Biotechnology

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Skin is the largest external organ in the human body but its use for therapeutic purposes has been minimal. Stratum corneum residing on the uppermost layer of the skin provides a tough barrier to transport the drugs across the skin. Very small group of drugs sharing Lipinski properties, i.e. drugs having molecular weight not larger than 500 Da, having high lipophilicity and optimum polarity are fortunate enough to be used on skin therapeutics. But, at a time where modern therapeutics is slowly shifting from use of small molecular drugs towards the use of macromolecular therapeutic agents such as peptides, proteins and nucleotides in origin, skin therapeutics need to be evolved accordingly to cater the delivery of these agents. Physical technologies like iontophoresis, laser ablation, micro-needles and ultrasound, etc. have been introduced to enhance skin permeability. But their success is limited due to their complex working mechanisms and involvement of certain irreversible skin damage in some or other way. This review therefore explores the delivery strategies for transport of mainly peptide and protein drugs that do not involve any injuries (non-invasive) to the skin termed as passive delivery techniques. Chemical enhancers, nanocarriers, certain biological peptides and miscellaneous approaches like prodrugs are also thoroughly reviewed for their applications in protein delivery.

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Protein Uptake and Cytoplasmic Access in Animal Cells

Cited by 6 publications

References 168 publications

Endocytosis and intracellular sorting of ricin and Shiga toxin

Endocytosis and intracellular sorting of ricin and Shiga toxin

Endosomal ricin transport: involvement of Rab4- and Rab5-positive compartments

Passive delivery of protein drugs through transdermal route

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