• Media type: E-Article
  • Title: How adhesion/growth-regulatory galectins-1 and -3 attain cell specificity : case study defining their target on neuroblastoma cells (SK-N-MC) and marked affinity regulation by affecting microdomain organization of the membrane
  • Contributor: Kopitz, Jürgen [VerfasserIn]; Bergmann, Marion [VerfasserIn]; Gabius, Hans-Joachim [VerfasserIn]
  • imprint: 28 July 2010
  • Published in: International Union of Biochemistry and Molecular Biology: IUBMB life ; 62(2010), 8 vom: Aug., Seite 624-628
  • Language: English
  • DOI: 10.1002/iub.358
  • ISSN: 1521-6551
  • Identifier:
  • Keywords: ganglioside ; glucosylceramide synthesis ; glycolipid ; lectin ; rafts
  • Origination:
  • Footnote:
  • Description: Galectins are potent effectors with conspicuous cell-type-specific activity profile. Its occurrence poses the question on the nature of the underlying biochemical determinants, in human SK-N-MC neuroblastoma cells involved in negative growth regulation. Since increase of surface presentation of ganglioside GM1 and homodimeric galectin-1 precedes growth inhibition, a direct interaction is suggested. We thus examined cell binding depending on glucosylceramide synthesis. It was drastically reduced by N-butyldeoxynojirimycin and threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol, adding decisive evidence for the assumed galectin/ganglioside binding. Glycoproteins do not compensate ganglioside depletion which was verified by measuring lipid-bound sialic acid. Binding affinity is significantly lowered by disrupting microdomain integrity, also effective for the competitive inhibitor galectin-3. This was caused by cell treatment with either 2-hydroxypropyl-β-cyclodextrin or filipin III. In this cell system, target specificity and topology of ligand presentation act together to enable high-affinity binding. © 2010 IUBMB IUBMB Life, 62(8): 624-628, 2010.
  • Access State: Open Access