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- Scopus: eid_2-s2.0-0019297732
- PMID: 7217459
- WOS: WOS:A1980LC39900003
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Article: Inhibition of cholera toxin activation of the adenylate cyclase system in intact HeLa cells
Title | Inhibition of cholera toxin activation of the adenylate cyclase system in intact HeLa cells |
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Authors | |
Issue Date | 1980 |
Citation | Journal Of Cyclic Nucleotide Research, 1980, v. 6 n. 5, p. 359-367 How to Cite? |
Abstract | Cholera toxin treatment activates the adenylate cyclase in intact HeLa cells. However, pretreatment of the cells with chemicals known to inhibit receptor internalization and lysosomal processing blocks the toxin include methylamine, ammonium chloride, chloroquine and dansylcadaverine. These chemicals did not affect either the binding of ( 125I)-cholera toxin to HeLa cells nor the ability of A 1 peptide to activate the adenylate cyclase in plasma membrane preparations. We conclude that these chemicals act on the processing of the toxin subsequent to its binding and that internalization and lysosomal processing mediate the release of the active fragment from cholera toxin, which activates the adenylate cyclase system. |
Persistent Identifier | http://hdl.handle.net/10722/167451 |
ISSN | |
ISI Accession Number ID |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lin, MC | en_US |
dc.contributor.author | Taniuchi, M | en_US |
dc.date.accessioned | 2012-10-08T03:07:10Z | - |
dc.date.available | 2012-10-08T03:07:10Z | - |
dc.date.issued | 1980 | en_US |
dc.identifier.citation | Journal Of Cyclic Nucleotide Research, 1980, v. 6 n. 5, p. 359-367 | en_US |
dc.identifier.issn | 0095-1544 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/167451 | - |
dc.description.abstract | Cholera toxin treatment activates the adenylate cyclase in intact HeLa cells. However, pretreatment of the cells with chemicals known to inhibit receptor internalization and lysosomal processing blocks the toxin include methylamine, ammonium chloride, chloroquine and dansylcadaverine. These chemicals did not affect either the binding of ( 125I)-cholera toxin to HeLa cells nor the ability of A 1 peptide to activate the adenylate cyclase in plasma membrane preparations. We conclude that these chemicals act on the processing of the toxin subsequent to its binding and that internalization and lysosomal processing mediate the release of the active fragment from cholera toxin, which activates the adenylate cyclase system. | en_US |
dc.language | eng | en_US |
dc.relation.ispartof | Journal of Cyclic Nucleotide Research | en_US |
dc.subject.mesh | Adenylate Cyclase - Metabolism | en_US |
dc.subject.mesh | Ammonium Chloride - Pharmacology | en_US |
dc.subject.mesh | Cadaverine - Analogs & Derivatives - Pharmacology | en_US |
dc.subject.mesh | Chloroquine - Pharmacology | en_US |
dc.subject.mesh | Cholera Toxin - Antagonists & Inhibitors - Metabolism | en_US |
dc.subject.mesh | Enzyme Activation - Drug Effects | en_US |
dc.subject.mesh | G(M1) Ganglioside | en_US |
dc.subject.mesh | Hela Cells | en_US |
dc.subject.mesh | Humans | en_US |
dc.subject.mesh | Methylamines - Pharmacology | en_US |
dc.subject.mesh | Receptors, Cell Surface | en_US |
dc.subject.mesh | Receptors, Immunologic - Antagonists & Inhibitors | en_US |
dc.title | Inhibition of cholera toxin activation of the adenylate cyclase system in intact HeLa cells | en_US |
dc.type | Article | en_US |
dc.identifier.email | Lin, MC:mcllin@hkucc.hku.hk | en_US |
dc.identifier.authority | Lin, MC=rp00746 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.pmid | 7217459 | - |
dc.identifier.scopus | eid_2-s2.0-0019297732 | en_US |
dc.identifier.volume | 6 | en_US |
dc.identifier.issue | 5 | en_US |
dc.identifier.spage | 359 | en_US |
dc.identifier.epage | 367 | en_US |
dc.identifier.isi | WOS:A1980LC39900003 | - |
dc.identifier.scopusauthorid | Lin, MC=7404816359 | en_US |
dc.identifier.scopusauthorid | Taniuchi, M=6701625278 | en_US |
dc.identifier.issnl | 0095-1544 | - |