Influence of a glycosaminoglycan polysulfate (Arteparon) on lysosomal enzyme release from human polymorphonuclear leukocytes.
In order to study the mechanism of action of a sulfated glycosaminoglycan (Arteparon) its influence upon the release of lysosomal enzymes from human polymorphonuclear leukocytes (PMNL) was investigated. Several fractions of tested glycosaminoglycan were used, differing in molecular weight (from 3,000 to 17,000). Human PMNL were incubated with zymosan particles opsonized with autologous serum. Preincubation with separate glycosaminoglycan fractions in concentrations 10(-3) M and 10(-4) M for 1 hr resulted in a significant activity decrease of released beta glucuronidase, neutral proteinase and myeloperoxidase. The concentration 10(-5) M was less active. Determination of total enzyme activities were made after cells (either incubated with tested glycosaminoglycan fractions for 1 hr or without incubation) were lysed by six freeze-thaw cycles. Sulfated glycosaminoglycan fractions inhibited all total enzyme activities. These results suggest direct inhibitory effect of tested drugs on lysosomal enzymes based on an interaction between inhibitor and enzyme.
D010450:Endopeptidases / Q000378:metabolism; D005966:Glucuronidase / Q000378:metabolism; D006025:Glycosaminoglycans / Q000494:pharmacology*; D006801:Humans; D007962:Leukocytes / Q000187:drug effects*; D008247:Lysosomes / Q000187:drug effects / Q000201:enzymology*; D009504:Neutrophils / Q000187:drug effects / Q000201:enzymology; D009195:Peroxidase / Q000378:metabolism
D006025:Glycosaminoglycans; C010034:Arteparon; D009195:Peroxidase; D005966:Glucuronidase; D010450:Endopeptidases