The metastatic potential of rat prostate tumor variant R3327-MatLyLu is correlated with an increased activity of N-acetylglucosaminyl transferase III and V.
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.
Easton
E W
EW
Department of Medical Chemistry, Vrije Universiteit, Amsterdam, The Netherlands.
Blokland
I
I
Geldof
A A
AA
Rao
B R
BR
van den Eijnden
D H
DH
D000818:Animals; D002240:Carbohydrate Sequence; D002853:Chromatography, Liquid; D005964:Glucosyltransferases / Q000378:metabolism*; D007527:Isoenzymes / Q000378:metabolism*; D008297:Male; D008969:Molecular Sequence Data; D017351:N-Acetylglucosaminyltransferases; D009362:Neoplasm Metastasis; D011471:Prostatic Neoplasms / Q000201:enzymology / Q000473:pathology*; D051381:Rats
D007527:Isoenzymes; D005964:Glucosyltransferases; D017351:N-Acetylglucosaminyltransferases; C037649:N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase