Differential expression of an alpha-galactosyl-containing trisaccharide on high- and low-malignant murine sarcoma cells: identification and regulation.

Abstract

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.

• Authors: James Varani, Jerzy Petryniak, Masaru Takagaki, Michael K Dame, Bronislawa Petryniak, Irwin J Goldstein
• Journal: Clinical & experimental metastasis (Clin Exp Metastasis) Vol. 19 Issue 1 Pg. 1-8 ( 2002) ISSN: 0262-0898 [Print] Netherlands
• PMID: 11918078 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Antibodies, Monoclonal
• Antigens, Neoplasm
• Antimicrobial Cationic Peptides
• Biomarkers, Tumor
• Evonymous europa lectin
• Griffonia simplicifolia lectins
• Lectins
• Neoplasm Proteins
• Plant Lectins
• Plant Proteins
• RNA, Messenger
• RNA, Neoplasm
• Trisaccharides
• erythrina lectin
• Galactosyltransferases
• N-acetyllactosaminide alpha-1,3-galactosyltransferase
• alpha-Galactosidase

Topics

• Animals
• Antibodies, Monoclonal (immunology)
• Antigens, Neoplasm (analysis, immunology, metabolism)
• Antimicrobial Cationic Peptides
• Biomarkers, Tumor (analysis, immunology, metabolism)
• Blotting, Northern
• Carbohydrate Conformation
• Carbohydrate Sequence
• Galactosyltransferases (analysis, genetics)
• Lectins (metabolism)
• Mice
• Mice, Inbred BALB C
• Molecular Sequence Data
• Neoplasm Invasiveness
• Neoplasm Proteins (analysis, genetics)
• Plant Lectins
• Plant Proteins (pharmacology)
• RNA, Messenger (analysis)
• RNA, Neoplasm (analysis)
• Sarcoma, Experimental (chemistry, pathology)
• Trisaccharides (analysis, immunology, metabolism)
• alpha-Galactosidase (pharmacology)