Activity of lysosomal exoglycosidases in human gliomas.
There is a lot of data suggesting that modifications of cell glycoconjugates may be important in progression of cancer. In the present work we studied activities of lysosomal exoglycosidases: beta-hexosaminidase and its isoenzymes A and B, beta-galactosidase and alpha-mannosidase, in human gliomas. Enzyme activity was determined spectrophotometrically based on the release of p-nitrophenol from p-nitrophenyl-derivative of appropriate sugars. The activities of the exoglycosidases tested were significantly higher in malignant glial tumors than in control tissue (normal brain tissue) and non-glial tumors. The highest activities of exoglycosidases were observed in high-grade gliomas, and a positive correlation of enzyme activities and degree of malignancy was noted. Our results suggest that lysosomal exoglycosidases may participate in the progression and dynamical development of glial tumors.
Wielgat
P
P
Department of Pharmaceutical Biochemistry, Medical University of Bialystok, ul. Mickiewicza 2A , 15-089, Bialystok, Poland. pwielg@amb.edu.pl
Walczuk
U
U
Szajda
S
S
Bień
M
M
Zimnoch
L
L
Mariak
Z
Z
Zwierz
K
K
D001932:Brain Neoplasms / Q000201:enzymology* / Q000473:pathology; D018450:Disease Progression; D015972:Gene Expression Regulation, Neoplastic; D005910:Glioma / Q000201:enzymology* / Q000473:pathology; D006026:Glycoside Hydrolases / Q000378:metabolism; D006801:Humans; D007527:Isoenzymes / Q000378:metabolism; D043323:alpha-Mannosidase / Q000378:metabolism*; D001616:beta-Galactosidase / Q000378:metabolism*; D001619:beta-N-Acetylhexosaminidases / Q000378:metabolism*
D007527:Isoenzymes; D006026:Glycoside Hydrolases; D001616:beta-Galactosidase; D043323:alpha-Mannosidase; D001619:beta-N-Acetylhexosaminidases