The metastatic potential of rat prostate tumor variant R3327-MatLyLu is correlated with an increased activity of N-acetylglucosaminyl transferase III and V.

Abstract

Enzyme activities of N-acetylglucosaminyltransferase (GlcNAc-Tase) I-V involved in N-linked complex-type carbohydrate synthesis were determined in a non-metastatic hormone-dependent rat prostate tumor (R3327-H) and a related, hormone-independent variant metastasizing to lymph nodes and lungs (R3327-MatLyLu). In the metastasizing variant a significantly increased activity of both GlcNAc-Tase III and GlcNAc-Tase V was observed, whereas the activities of GlcNAc-Tase I and II were essentially unchanged. The increase in activity of GlcNAc-Tase III is particularly noteworthy since it indicates that elevated expression of this enzyme cannot be considered as an exclusive marker of hepatic malignancy.

• Authors: E W Easton, I Blokland, A A Geldof, B R Rao, D H van den Eijnden
• Journal: FEBS letters (FEBS Lett) Vol. 308 Issue 1 Pg. 46-9 (Aug 10 1992) ISSN: 0014-5793 [Print] England
• PMID: 1386579 (Publication Type: Journal Article)

Chemical References

• Isoenzymes
• Glucosyltransferases
• N-Acetylglucosaminyltransferases
• N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase

Topics

• Animals
• Carbohydrate Sequence
• Chromatography, Liquid
• Glucosyltransferases (metabolism)
• Isoenzymes (metabolism)
• Male
• Molecular Sequence Data
• N-Acetylglucosaminyltransferases
• Neoplasm Metastasis
• Prostatic Neoplasms (enzymology, pathology)
• Rats