Alpha-2,6-sialylation of L-PHA reactive oligosaccharides and expression of N-acetylglucosaminyltransferase V in human diffuse large B cell lymphoma.
Cell surface sialylation and beta1-6 branching of L-PHA reactive oligosaccharides play an important role in metastatic capacities of various tumor cell lines. We analyzed the expression and sialylation of L-PHA reactive oligosaccharides in human diffuse large B cell lymphoma (DLBCL). DLBCL was grouped into three types; i). Group A, non-reactive type with no expression of L-PHA reactive oligosaccharides, ii). Group B, sialylated type with expression of sialylated L-PHA reactive oligosaccharides and iii). Group C, non-sialylated type with expression of non-sialylated L-PHA reactive oligosaccharides. To clarify the linkage of sialic acid residues in L-PHA reactive oligosaccharides of Group B cases, L-PHA lectin histochemistry after treatment with two different neuraminidases was performed. In all Group B cases, L-PHA binding reactivity was found after treatment with Vibrio cholerae neuraminidase. But not after treatment with Newcastle disease virus neuraminidase. These data indicate that alpha2,6-linked sialic acid residues were predominantly involved in sialylation of L-PHA reactive oligosaccharides of Group B. To clarify the relationship between expression of N-acetylglucosaminyltransferase V (GnT-V), which catalyzes beta1-6 branching of L-PHA reactive oligosaccharides, and L-PHA reactivities in DLBCL, we investigated the expression of GnT-V using immunohistochemical methods. Most of the Group B and C cases expressed GnT-V while 33% of Group A cases showed no expression of GnT-V. These data suggest that expression of GnT-V is not always correlated with the expression of L-PHA reactive glycoconjugates. Furthermore, survival of patients in Group A which showed no expression of GnT-V was significantly shorter than that of patients in Group C which expressed GnT-V. Therefore, loss of non-sialylated L-PHA reactive oligosaccharides due to lack of expression of GnT-V in lymphoma cells may be associated with aggressiveness of DLBCL.
Suzuki
Osamu
O
Fukushima Medical University, School of Medicine, Department of Pathology, Fukushima 960-1295, Japan. osuzuki@cc.fmu.ac.jp
Nozawa
Yoshihiro
Y
Kawaguchi
Takanori
T
Abe
Masafumi
M
D001710:Biotin / Q000494:pharmacology; D006801:Humans; D007150:Immunohistochemistry; D037102:Lectins / Q000737:chemistry / Q000378:metabolism; D008223:Lymphoma / Q000201:enzymology / Q000378:metabolism; D016393:Lymphoma, B-Cell / Q000378:metabolism / Q000401:mortality / Q000473:pathology*; D008228:Lymphoma, Non-Hodgkin / Q000378:metabolism / Q000401:mortality / Q000473:pathology; D008956:Models, Chemical; D017351:N-Acetylglucosaminyltransferases / Q000737:chemistry*; D019158:N-Acetylneuraminic Acid / Q000378:metabolism; D009439:Neuraminidase / Q000494:pharmacology; D009522:Newcastle disease virus / Q000201:enzymology; D009844:Oligosaccharides / Q000737:chemistry*; D011485:Protein Binding; D012799:Sialyltransferases / Q000378:metabolism*; D013997:Time Factors; D014734:Vibrio cholerae / Q000201:enzymology; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase
D037102:Lectins; D009844:Oligosaccharides; D001710:Biotin; D017351:N-Acetylglucosaminyltransferases; C052254:alpha-1,6-mannosylglycoprotein beta 1,6-N-acetylglucosaminyltransferase; D012799:Sialyltransferases; D009439:Neuraminidase; D019158:N-Acetylneuraminic Acid; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase