Differential expression of an alpha-galactosyl-containing trisaccharide on high- and low-malignant murine sarcoma cells: identification and regulation.
Past studies have shown that carbohydrate residues reactive with the Griffonia simplicifolia isolectin B4 (GS I-B4) are present on the surface of highly-malignant murine sarcoma cells but are lacking or expressed in much lower amounts on the surface of low-malignant cells isolated from the same parent tumors (Am J Pathol 111: 27; J Nat Cancer Inst 71: 1281). In the present study it is shown that an antibody which recognizes the trisaccharide Galalpha1-3Galbeta1-4GlcNAc- is reactive with the highly-malignant cells but is non-reactive with the low-malignant cells. Further studies show that the high-malignant cells not only bind GS 1-B4 but also bind Evonymus europaea lectin (which like GS I-B4 recognizes terminal galactose in alpha1-3 linkage) and Erythina crystagalli lectin (which recognizes sub-terminal galactose in the beta1-4 linkage--e.g., Galbeta1-4GlcNAc). In contrast, the low malignant cells bind Erythina crystagalli lectin as efficiently as the high malignant cells but do not bind (or bind much smaller amounts of) either GS I-B4 or Evonymus europaea lectin. The present studies also show that there is no significant difference between high- and low-malignant cells in expression of alpha-galactosidase activity. In contrast, the high-malignant cells express high levels of alpha-galactosyl transferase activity while this enzyme is virtually undetectable in low-malignant cells. Taken together, these studies indicate that differential expression of a single monosaccharide residue distinguishes high- and low-malignant murine sarcoma cells. These studies also identify a mechanism to account for surface carbohydrate differences between the high- and low-malignant cells.
Varani
James
J
Departments of Pathology, The University of Michigan Medical School, Ann Arbor 48109, USA. varani@umich.edu
Petryniak
Jerzy
J
Takagaki
Masaru
M
Dame
Michael K
MK
Petryniak
Bronislawa
B
Goldstein
Irwin J
IJ
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D000951:Antigens, Neoplasm / Q000032:analysis* / Q000276:immunology / Q000378:metabolism; D023181:Antimicrobial Cationic Peptides; D014408:Biomarkers, Tumor / Q000032:analysis* / Q000276:immunology / Q000378:metabolism; D015152:Blotting, Northern; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D005700:Galactosyltransferases / Q000032:analysis / Q000235:genetics; D037102:Lectins / Q000378:metabolism; D051379:Mice; D008807:Mice, Inbred BALB C; D008969:Molecular Sequence Data; D009361:Neoplasm Invasiveness; D009363:Neoplasm Proteins / Q000032:analysis / Q000235:genetics; D037121:Plant Lectins; D010940:Plant Proteins / Q000494:pharmacology; D012333:RNA, Messenger / Q000032:analysis; D012334:RNA, Neoplasm / Q000032:analysis; D012513:Sarcoma, Experimental / Q000737:chemistry* / Q000473:pathology; D014312:Trisaccharides / Q000032:analysis* / Q000276:immunology / Q000378:metabolism; D000519:alpha-Galactosidase / Q000494:pharmacology
D000911:Antibodies, Monoclonal; D000951:Antigens, Neoplasm; D023181:Antimicrobial Cationic Peptides; D014408:Biomarkers, Tumor; C047161:Evonymous europa lectin; C045475:Griffonia simplicifolia lectins; D037102:Lectins; D009363:Neoplasm Proteins; D037121:Plant Lectins; D010940:Plant Proteins; D012333:RNA, Messenger; D012334:RNA, Neoplasm; D014312:Trisaccharides; C045629:erythrina lectin; D005700:Galactosyltransferases; C047006:N-acetyllactosaminide alpha-1,3-galactosyltransferase; D000519:alpha-Galactosidase