Effects of db-cAMP and theophylline on Concanavalin A binding site distribution on transformed and protease-treated cell lines
Identifieur interne : 001037 ( Istex/Curation ); précédent : 001036; suivant : 001038Effects of db-cAMP and theophylline on Concanavalin A binding site distribution on transformed and protease-treated cell lines
Auteurs : Joan Z. Borysenko [États-Unis] ; Th. E. Ukena [États-Unis] ; M. J. Karnovsky [États-Unis]Source :
- Experimental Cell Research [ 0014-4827 ] ; 1977.
English descriptors
- Teeft :
- Acad, Binding site distribution, Brief trypsinization, Cabs distribution, Cars distribution, Cell cycle, Cell edges, Cell lines, Cell shape, Cells show, Chinese hamster ovary cells, Cona, Cona binding, Dbcamp treatment, High concentrations, Intracellular camp levels, Many microvilli, Microtubular protein, Microtubule, Microvilli, Morphological reversion, Mouse embryo fibroblasts, Natl, Normal cells, Proc, Proc natl acad, Proteolytic activity, Scanning micrograph, Sodium butyrate, Surface distribution, Theophylline, Theophylline treatment, Tufts university school, Ukena.
Abstract
Abstract: We have examined the effects of N6, O2-dibutyryl 3′: 5′ adenosine-cyclic monophosphate (db-cAMP) and theophylline treatment on the surface distribution of Concanavalin A-binding sites (CABS) on 3T3 cells, SV40-transformed 3T3 cells (SV3T3) and a line of SV40-transformed mouse embryo fibroblasts (VLM). Overnight incubation of VLM cells in medium containing db-cAMP and theophylline completely eliminated the lectin-induced clustering of CABS observed on many transformed cell lines. Similar treatment of SV3T3 cells caused a partial inhibition of clustering. A clone of 3T3 cells that did not normally show lectin-induced clustering could be caused to patch by brief trypsinization. Induction of clustering on these cells after trypsinization was likewise prevented by db-cAMP and theophylline.
Url:
DOI: 10.1016/0014-4827(77)90407-4
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Karnovsky</name><affiliation wicri:level="1"><mods:affiliation>Department of Pathology, Harvard Medical School, Boston, MA 02115, USA</mods:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology, Harvard Medical School, Boston, MA 02115</wicri:regionArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Experimental Cell Research</title><title level="j" type="abbrev">YEXCR</title><idno type="ISSN">0014-4827</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1977">1977</date><biblScope unit="volume">107</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="253">253</biblScope><biblScope unit="page" to="260">260</biblScope></imprint><idno type="ISSN">0014-4827</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0014-4827</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acad</term><term>Binding site distribution</term><term>Brief trypsinization</term><term>Cabs distribution</term><term>Cars distribution</term><term>Cell cycle</term><term>Cell edges</term><term>Cell lines</term><term>Cell shape</term><term>Cells show</term><term>Chinese hamster ovary cells</term><term>Cona</term><term>Cona binding</term><term>Dbcamp treatment</term><term>High concentrations</term><term>Intracellular camp levels</term><term>Many microvilli</term><term>Microtubular protein</term><term>Microtubule</term><term>Microvilli</term><term>Morphological reversion</term><term>Mouse embryo fibroblasts</term><term>Natl</term><term>Normal cells</term><term>Proc</term><term>Proc natl acad</term><term>Proteolytic activity</term><term>Scanning micrograph</term><term>Sodium butyrate</term><term>Surface distribution</term><term>Theophylline</term><term>Theophylline treatment</term><term>Tufts university school</term><term>Ukena</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: We have examined the effects of N6, O2-dibutyryl 3′: 5′ adenosine-cyclic monophosphate (db-cAMP) and theophylline treatment on the surface distribution of Concanavalin A-binding sites (CABS) on 3T3 cells, SV40-transformed 3T3 cells (SV3T3) and a line of SV40-transformed mouse embryo fibroblasts (VLM). Overnight incubation of VLM cells in medium containing db-cAMP and theophylline completely eliminated the lectin-induced clustering of CABS observed on many transformed cell lines. Similar treatment of SV3T3 cells caused a partial inhibition of clustering. A clone of 3T3 cells that did not normally show lectin-induced clustering could be caused to patch by brief trypsinization. Induction of clustering on these cells after trypsinization was likewise prevented by db-cAMP and theophylline.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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