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.
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.
Ono
M
M
Pacific Northwest Research Institute, 720 Broadway, Seattle, Washington 98122-4327, USA.
Handa
K
K
Withers
D A
DA
Hakomori
S
S
D000818:Animals; D015703:Antigens, CD / Q000737:chemistry / Q000502:physiology*; D016466:CHO Cells; D002448:Cell Adhesion / Q000502:physiology*; D002465:Cell Movement / Q000502:physiology*; D006224:Cricetinae; D005353:Fibronectins / Q000502:physiology; D006028:Glycosphingolipids / Q000502:physiology; D006031:Glycosylation; D022781:Hepatocytes / Q000502:physiology; D051861:Kangai-1 Protein; D007797:Laminin / Q000502:physiology; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000502:physiology*; D011487:Protein Conformation; D011518:Proto-Oncogene Proteins; D015398:Signal Transduction
D015703:Antigens, CD; D005353:Fibronectins; D006028:Glycosphingolipids; D051861:Kangai-1 Protein; D007797:Laminin; D008562:Membrane Glycoproteins; D011518:Proto-Oncogene Proteins