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The metastatic potential of rat prostate tumor variant R3327‐MatLyLu is correlated with an increased activity of N ‐acetylglucosaminyl transferase III and V
Author(s) -
Easton Ellen W.,
Blokland Irene,
Geldof Albert A.,
Rao B.Ramanath,
van den Eijnden Dirk H.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81047-p
Subject(s) - malignancy , transferase , prostate , enzyme , chemistry , hormone , medicine , cancer research , endocrinology , biology , pathology , biochemistry , cancer
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.