Effect of sodium thiomalate on immune complex-induced release of lysosomal enzymes from human polymorphonuclear leucocytes.
The extracellular release of beta-glucuronidase and beta-N-acetylglucosaminidase from normal human polymorphonuclear leucocytes initiated with bovine serum albumin/anti-bovine serum albumin immune complex (15 micrograms/ml) was significantly inhibited (p less than 0.01) by pretreatment with increasing concentrations (10(-8) M, 10(-7) M, 10(-6) M and 10(-5) M) of sodium thiomalate in a time- and dose-related fashion. Also, beta-glucuronidase and beta-N-acetylglucosaminidase exhibited similar responses to the effects of bovine serum albumin/anti-bovine serum albumin or sodium thiomalate. In contrast, neither bovine serum albumin/anti-bovine serum albumin nor sodium thiomalate provoked appreciable leakage of the cytoplasmic enzyme, lactate dehydrogenase. This indicates that cell integrity remains intact under the experimental conditions described.
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D000118:Acetylglucosaminidase / Q000097:blood* / Q000378:metabolism; D000936:Antigen-Antibody Complex; D002470:Cell Survival; D005966:Glucuronidase / Q000097:blood* / Q000378:metabolism; D006052:Gold Sodium Thiomalate / Q000494:pharmacology*; D006596:Hexosaminidases / Q000097:blood*; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D008247:Lysosomes / Q000187:drug effects / Q000201:enzymology*; D009504:Neutrophils / Q000187:drug effects / Q000201:enzymology*
D000936:Antigen-Antibody Complex; D006052:Gold Sodium Thiomalate; D006596:Hexosaminidases; D005966:Glucuronidase; D000118:Acetylglucosaminidase