Inhibition and reversal of capping by cytochalasin B, yinblastine and colchicine

Petris, S. de

doi:10.1038/250054a0

Cited by 186 publications

(74 citation statements)

References 15 publications

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“…Binding and aggregation of label could cause and maintain the interaction of the binding sites with this network. This network could then either transfer the message to other parts of the cell or itself direct the rearrangement, de Petris (14) has suggested that such a network could be provided by microfilaments because of the effects of cytochalasin B on label-induced rearrangement. He and others (44,56) have found a cooperative inhibitory effect of cytochalasin B and colchicine on capping, indicating that a microtubule system may be involved as well.…”

Section: Discussionmentioning

confidence: 99%

Reversibility of cell surface label rearrangement.

Brown¹,

Revel²

1976

The Journal of Cell Biology

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Cell surface labeling can cause rearrangements of randomly distributed membrane components. Removal of the label bound to the cell surface allows the membrane components to return to their original random distribution, demonstrating that label is necessary to maintain as well as to induce rearrangements. With scanning electron microscopy, the rearrangement of concanavalin A (con A) and ricin binding sites on LA-9 cells has been followed by means of hemocyanin, a visual label. The removal of con A from its binding sites at the cell surface with alpha-methyl mannoside, and the return of these sites to their original distribution are also followed in this manner.There are labeling differences with con A and ricin. Under some conditions, however, the same rearrangements are seen with both lectins. The disappearance of labeled sites from areas of ruffling activity is a major feature of the rearrangements seen. Both this ruffling activity and the rearrangement of label are sensitive to cytochalasin B, and ruffling activity, perhaps along with other cytochalasin-sensitire structure, may play a role in the rearrangements of labeled sites.Evidence from a number of laboratories indicates that the application of label to cell surfaces causes a rearrangement of randomly distributed membrane molecules (12,15,20,30,35,43,51,53). Rearrangement is not a general membrane phenomenon, but involves only the labeled sites; surface molecules which do not interact with the label remain in a random, homogeneous distribution (29). It is not known how the interaction between label and receptor causes rearrangement.Two components can be recognized during label-induced rearrangement (12,35,53,55): the formation of clusters of label; and the preferential relocation of label to certain areas on the cell and away from others, e.g., capping. It has been proposed that the first component, clustering, results from crosslinking of surface sites by multivalent label molecules, since univalent antibody fragments appear uniformly distributed on the cell surface (16,35,53). Stackpole et al. (50), however, have demonstrated that clustering can occur even with strictly univalent reagents. They suggest that interaction of label with its binding sites may cause an alteration which thermodynamically favors aggregation. The second component of rearrangement must involve more than crosslinking or aggregation of labeled molecules in the plane of the membrane; it requires energy (12,15,20,35,53,57) and must therefore be directed by some activity of the cell.In this communication we follow the rearrangements at the cell surface obtained with two different lectins and show that the label-receptor interaction is necessary for the maintenance as well as the induction of rearrangements. Mechanisms consistent with our findings whereby label-receptor THE JOURNAL OF CELL BIOLOGY 9 VOLUME 68, 1976 9 pages 629-641 629

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Section: Discussionmentioning

confidence: 99%

Reversibility of cell surface label rearrangement.

Brown¹,

Revel²

1976

The Journal of Cell Biology

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“…The inhibition of amiloride-sensitive Na ϩ channels produced by influenza is not attributable, however, to a redistribution of membrane proteins (''capping'') such as occurs in lymphocytes after exposure to concanavalin A (35). Capping in lymphocytes after exposure to concanavalin A and other agents that crosslink receptors is inhibited by microfilament inhibitors such as cytochalasin D (36,37), whereas the inhibitory effect of influenza virus on Na ϩ channels is not. This is, to our knowledge, the first report of any viral or microbial pathogen that regulates amiloride-sensitive Na ϩ channels.…”

Section: ϫ2mentioning

confidence: 99%

Influenza virus inhibits amiloride-sensitive Na⁺channels in respiratory epithelia

Kunzelmann

Beesley

King

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

108

124

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Many pathogens causing diarrhea do so by modulating ion transport in the gut. Respiratory pathogens are similarly associated with disturbances of fluid balance in the respiratory tract, although it is not known whether they too act by altering epithelial ion transport. Here we show that influenza virus A͞PR͞8͞34 inhibits the amiloride-sensitive Na ؉ current across mouse tracheal epithelium with a half-time of about 60 min. We further show that the inhibitory effect of the influenza virus is caused by the binding of viral hemagglutinin to a cell-surface receptor, which then activates phospholipase C and protein kinase C. Given the importance of epithelial Na ؉ channels in controlling the amount of fluid in the respiratory tract, we suggest that down-regulation of Na ؉ channels induced by influenza virus may play a role in the fluid transport abnormalities that are associated with influenza infections.hemagglutinin ͉ protein kinase C ͉ ENaC ͉ phospholipase C

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“…microfilaments) and monomeric form, has, however, yet to be clearly defined. In the case of lymphocytes, microfilaments have been implicated in various cell surface-mediated phenomena including the capping of surface immunoglobulin [2][3][4][5], lectin-induced mitogenicity [6,7] and lymphocyte-mediated cytotoxicity [8,9]. One possible explanation for the apparent linkage between cell surface events and cytoplasmic microfilaments would be a specific interaction between the filaments and the cell surface (plasma) membrane.…”

Section: Introductionmentioning

confidence: 99%

Actin associated with purified lymphocyte plasma membrane

Barber

Crumpton

1976

FEBS Letters

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Inhibition and reversal of capping by cytochalasin B, yinblastine and colchicine

Cited by 186 publications

References 15 publications

Reversibility of cell surface label rearrangement.

Reversibility of cell surface label rearrangement.

Influenza virus inhibits amiloride-sensitive Na⁺channels in respiratory epithelia

Actin associated with purified lymphocyte plasma membrane

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Inhibition and reversal of capping by cytochalasin B, yinblastine and colchicine

Cited by 186 publications

References 15 publications

Reversibility of cell surface label rearrangement.

Reversibility of cell surface label rearrangement.

Influenza virus inhibits amiloride-sensitive Na+channels in respiratory epithelia

Actin associated with purified lymphocyte plasma membrane

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Influenza virus inhibits amiloride-sensitive Na⁺channels in respiratory epithelia