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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-3-23
pubmed:abstractText
Cell-surface glycoproteins are regarded as candidates for involvement in the spread of tumor cells. N-linked beta1-6 branched oligosaccharides may contribute directly to the malignant or metastatic phenotypes of tumor cells. Increased beta1-6 branching has been associated with an increased level of N-acetylglucosaminyltransferase V (GlcNAc transferase V), the glycosyltransferase that initiates the beta1-6 branching. In this report, 33 pathologically verified hepatocellular carcinoma (HCC) specimens, six non-cancerous tissues surrounding HCC and five normal liver specimens have been studied. We have quantified N-linked beta1-6 branched oligosaccharides indirectly by measuring GlcNac transferase V activity. The average GlcNac transferase V activities in hepatocellular carcinoma (HCC), noncancerous tissues surrounding HCC and normal liver tissues were 324.2 +/- 269.8, 84.8 +/- 20.7 and 7.0 +/- 6.2 pmol product h(-1) mg protein(-1) (P < 0.05) respectively. In addition, the activity was correlated with the TNM classification of HCC. The average activities of GlcNAc transferase V in stages T1, T2-3 and T4 were 77.6 +/- 57.8, 369.0 +/- 294.7 and 329.9 +/- 205.9 pmol product h(-1) mg protein h(-1) respectively (P < 0.05), showing that the activity of the enzyme in advanced HCC was higher than that in early HCC. Our preliminary results indicated that GlcNAc transferase V activity increased in human HCC and was correlated with its progression.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0171-5216
pubmed:author
pubmed:issnType
Print
pubmed:volume
124
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
27-30
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Elevated activity of N-acetylglucosaminyltransferase V in human hepatocellular carcinoma.
pubmed:affiliation
Gene Research Center and Department of Biochemistry, Shanghai Medical University, PR China.
pubmed:publicationType
Journal Article