title: Lysosomal exoglycosidases and cathepsin D in colon adenocarcinoma.
abstract: BACKGROUND
  Changes in the structure of membrane glycoconjugates and activity of glycosidases and proteases are important in tumor formation.
  
  
  OBJECTIVE
  The aim of the study was to compare the specific activity of lysosomal exoglycosidases: N-acetyl-β-D-hexosaminidase (HEX), its isoenzymes A (HEX A) and B (HEX B), β-D-galactosidase (GAL), α-fucosidase (FUC), and α-mannosidase (MAN) with the activity of cathepsin D (CD) in serum, urine, and carcinoma tissue of patients with colon adenocarcinoma.
  
  
  METHODS
  The specific activity of HEX, HEX A, HEX B, GAL, FUC, MAN, and CD was assayed in serum, urine, and carcinoma tissue of 12 patients with colon adenocarcinoma.
  
  
  RESULTS
  Lysosomal exoglycosidases and CD have similar specific activity in colon adenocarcinoma tissue and urine, which is higher than their activity in serum (with the exception of the highest specific activity of CD in urine). A positive correlation was observed between the specific activity of CD and that of HEX, HEX A, FUC, and MAN in the carcinoma tissue and urine as well as between CD and GAL in the urine of patients with colon adenocarcinoma. Negative correlations were observed between protein levels and the specific activity of HEX, HEX A, FUC, MAN, and CD in the carcinoma tissue and urine, and between protein levels and GAL in urine.
  
  
  CONCLUSIONS
  Increased degradation and remodeling of glycoconjugates in the colon adenocarcinoma tissue is reflected by increased specific activity of exoglycosidases and CD. The results suggest a strong effect of exoglycosidase action on tissue degradation and a potential role of exoglycosidases in the initiation of proteolysis.
authors.affiliation: Department of Psychiatry, Medical University of Bialystok, Białystok, Poland. napoleonwas@yahoo.com
authors.forename: Napoleon
authors.initials: N
authors.lastname: Waszkiewicz
authors.forename: Beata
authors.initials: B
authors.lastname: Zalewska-Szajda
authors.forename: Sławomir D
authors.initials: SD
authors.lastname: Szajda
authors.forename: Alina
authors.initials: A
authors.lastname: Kępka
authors.forename: Magdalena
authors.initials: M
authors.lastname: Waszkiewicz
authors.forename: Wiesława
authors.initials: W
authors.lastname: Roszkowska-Jakimiec
authors.forename: Marzena
authors.initials: M
authors.lastname: Wojewódzka-Żeleźniakowicz
authors.forename: Anna J
authors.initials: AJ
authors.lastname: Milewska
authors.forename: Jacek
authors.initials: J
authors.lastname: Dadan
authors.forename: Agata
authors.initials: A
authors.lastname: Szulc
authors.forename: Krzysztof
authors.initials: K
authors.lastname: Zwierz
authors.forename: Jerzy R
authors.initials: JR
authors.lastname: Ladny
mesh_terms: D000230:Adenocarcinoma / Q000201:enzymology* / Q000378:metabolism; D000368:Aged; D000369:Aged, 80 and over; D014408:Biomarkers, Tumor / Q000378:metabolism*; D002402:Cathepsin D / Q000378:metabolism*; D003110:Colonic Neoplasms / Q000201:enzymology* / Q000378:metabolism; D005260:Female; D054818:Hexosaminidase A / Q000378:metabolism; D054819:Hexosaminidase B / Q000378:metabolism; D006801:Humans; D007527:Isoenzymes / Q000378:metabolism; D008247:Lysosomes / Q000378:metabolism*; D008297:Male; D008875:Middle Aged; D011237:Predictive Value of Tests; D012680:Sensitivity and Specificity; D044967:Serum / Q000378:metabolism; D043323:alpha-Mannosidase / Q000378:metabolism; D001616:beta-Galactosidase / Q000378:metabolism; D001619:beta-N-Acetylhexosaminidases / Q000378:metabolism
chemical_list: D014408:Biomarkers, Tumor; D007527:Isoenzymes; D001616:beta-Galactosidase; D043323:alpha-Mannosidase; D054818:Hexosaminidase A; D054819:Hexosaminidase B; D001619:beta-N-Acetylhexosaminidases; D002402:Cathepsin D