Glycobiology Advance Access published online on September 26, 2003
Glycobiology, doi:10.1093/glycob/cwh002
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© 2003 Oxford University Press
ORIGINAL ARTICLES
1 Department of Experimental Pathology, "F. Addarii" Institute of Oncology, University of Bologna, Bologna, Italy
Revised on September 2, 2003
Accepted on September 2, 2003
Expression of
-galactoside
2,6 sialyltransferase (ST6Gal.I) and of
2,6-sialylated glycoconjugates in normal human liver, hepatocarcinoma and cirrhosis
2 Pathology Unit, "F. Addarii" Institute of Oncology, University of Bologna, Bologna, Italy
-galactoside
2,6 sialyltransferase (ST6Gal.I) mediates the addition of
2,6-linked sialic acid to glycoproteins. ST6Gal.I is strongly expressed by the liver and is upregulated in several cancers, but little is known of its regulation in human liver diseases. We have investigated the expression of ST6Gal.I and of its product, the
2,6 sialylated lactosamine, in normal human liver, hepatocarcinoma (HCC) and cirrhosis. We found that both ST6Gal.I activity and mRNA can undergo up- or downregulation in different HCC patients. At the mRNA level, the groups of specimens showing the highest expression were HCC of grade 2, HCC developed without preexisting cirrhosis and HCC of male patients. The lectin from Sambucus nigra (SNA) reveals a significative overexpression of
2,6-sialylated glycoconjugates in HCC tissue homogenates and their intracellular accumulation in HCC histological sections, even though in a few cases the extent of
2,6-sialylation dramatically decreases. Transcription of the gene occurs through at least two different promoters, resulting in two differentially expressed mRNA species. RNA in situ hybridization reveals that the ST6Gal.I mRNA can be expressed at a quantitatively heterogeneous level among the neoplastic cells. Neither ST6Gal.I expression nor
2,6-sialylation are altered in cirrhosis. These data indicate that neoplastic transformation, but not cirrhosis, can alter the process of
2,6 sialylation of liver glycoproteins.![]()
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