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- W3130388995 abstract "3446 β1,6-N-acetylgulcosaminyltransferase V (GnT-V) expression, assessed via β1,6-branched oligosaccharide formation, is common in human cancer and is correlated with metastasis and poor survival. GnT-V has multiple glycoprotein substrates and thereby exerts global effects on cancer progression, characteristic of a master regulator of metastasis. Yet little is known of GnT-V expression within tumors at the tissue and cellular levels. Here we report histochemical analyses comparing GnT-V and β1,6-branched oligosaccharides in malignant melanoma (n = 24 cases). We were surprised to find distinct patterns of GnT-V expression that differed between cases. Methods. GnT-V and β1,6-branched oligosaccharides were compared in formalin-fixed, paraffin-embedded tumor specimens. Tumor sections were stained with anti-GnT-V, with the lectin LPHA (β1,6-branched oligosaccharides), and in some cases with antibodies to the Golgi complex. Stains were analyzed by light microscopy. Results. All tumors stained with GnT-V. On the cellular level GnT-V stained large perinuclear structures consistent with the Golgi complex and also showed cytoplasmic staining. Thus although GnT-V is known to be enzymatically active in the Golgi complex, the protein was not localized solely to this structure. On the tissue level three staining patterns were seen. 1) The most common was uniform GnT-V staining throughout the tumor with a correspondence between GnT-V protein and β1,6-branched oligosaccharides. Thus in this pattern most if not all tumor cells were induced for GnT-V synthesis and enzymatic activity. 2) In a second pattern GnT-V protein was restricted to certain nests or areas of the tumor where again there was a correspondence with β1,6-branched oligosaccharides. This pattern indicated different tumor cell phenotypes for GnT-V synthesis or degradation. 3) In a third pattern, GnT-V stained throughout the tumor but in this case β1,6-branched oligosaccharides were restricted to certain nests or areas. This indicted selective activation or inhibition of GnT-V enzymatic activity. Conclusions. These findings reveal for the first time that GnT-V synthesis and enzymatic activity are subject to multiple levels of regulation. This information should help pave the way to a fuller understanding of GnT-V expression —a key factor in tumor invasion and metastasis." @default.
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- W3130388995 date "2006-04-15" @default.
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- W3130388995 title "Increased lysosomal burden correlates with the metastatic potential of human breast cancer xenografts" @default.
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