Glycosylation effect on membrane domain (GEM) involved in cell adhesion and motility: a preliminary note on functional alpha3, alpha5-CD82 glycosylation complex in ldlD 14 cells

Biochem Biophys Res Commun. 2000 Dec 29;279(3):744-50. doi: 10.1006/bbrc.2000.4030.


Laminin (LN)- or fibronectin (FN)-dependent adhesion in Krieger's ldlD 14 (D14) cells is enhanced significantly in the presence vs absence, of galactose (Gal), whereas LN- or FN-induced haptotactic cell motility is barely affected unless cells express CD82 by its gene transfection (cells termed D14/CD82). The effect of CD82 on LN- or FN-induced motility is based on its ability to associate with alpha3 or alpha5 integrin to form a complex associated with a low-density lipid membrane domain (termed GEM or GSD). Complex formation is greatly affected by N-glycosylation of both integrin and CD82, as well as by concurrent GM3 ganglioside synthesis. The effect of glycosylation on alpha5-CD82 complex was also studied in D14 cells expressing mutant CD82, defective in all three N-glycosylation sites. LN-induced motility was greatly inhibited, whereas FN-induced motility was enhanced, with complete N-glycosylation in D14/CD82 cells in Gal-added medium, whereby alpha5-CD82 complex formation did not occur or occurred at a minimal level. Both LN- and FN-induced motility were inhibited when N-glycosylation was impaired, or N-glycosylation of CD82 was deleted, whereby alpha5-CD82 complex formation occurred strongly. Thus, glycosylation profoundly affects interaction of integrin with CD82, leading to significant inhibition or promotion of cell motility.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Antigens, CD / chemistry
  • Antigens, CD / physiology*
  • CHO Cells
  • Cell Adhesion / physiology*
  • Cell Movement / physiology*
  • Cricetinae
  • Fibronectins / physiology
  • Glycosphingolipids / physiology
  • Glycosylation
  • Hepatocytes / physiology
  • Kangai-1 Protein
  • Laminin / physiology
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / physiology*
  • Protein Conformation
  • Proto-Oncogene Proteins*
  • Signal Transduction


  • Antigens, CD
  • Fibronectins
  • Glycosphingolipids
  • Kangai-1 Protein
  • Laminin
  • Membrane Glycoproteins
  • Proto-Oncogene Proteins