Leucocyte migration inhibition in vitro with inhibitors of aspartic and sulphhydryl proteinases.
The human leucocyte migration in the leucocyte migration under agarose technique ( LMAT ) was investigated with specific inhibitors of aspartic, sulphhydryl , metallo- and serine proteinases. The general aspartic proteinase inhibitor pepstatin and the highly specific competitive cathepsin D inhibitor, N-gly-glu-gly-phe-leu-gly-D-phe-leu suppressed leucocyte migration at concentrations of 20-200 mumol/l and 30-59 mumol/l, respectively. The suphhydryl enzyme inactivator, N-ethylmaleimide suppressed leucocyte migration at concentrations of 100-200 mumol/l. Several inhibitors of serine- and metallo enzymes were tested, but none had any effect on leucocyte mobility, although the metal binding agent 8-hydroxyquinoline was strongly inhibitory to cell migration, the significance of which is discussed.
D007611:Aprotinin / Q000494:pharmacology; D001224:Aspartic Acid; D002402:Cathepsin D; D002403:Cathepsins / Q000037:antagonists & inhibitors; D002464:Cell Migration Inhibition; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D006801:Humans; D007962:Leukocytes / Q000276:immunology*; D009504:Neutrophils / Q000276:immunology; D010436:Pepstatins / Q000494:pharmacology; D011480:Protease Inhibitors; D013438:Sulfhydryl Compounds
D004791:Enzyme Inhibitors; D010436:Pepstatins; D011480:Protease Inhibitors; D013438:Sulfhydryl Compounds; D001224:Aspartic Acid; D007611:Aprotinin; D002403:Cathepsins; D002402:Cathepsin D