Leucocyte migration inhibition in vitro with inhibitors of aspartic and sulphhydryl proteinases. 1984

E Lauritzen, and S Møller, and J Leerhoy

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.

UI MeSH Term Description Entries
D007611 Aprotinin A single-chain polypeptide derived from bovine tissues consisting of 58 amino-acid residues. It is an inhibitor of proteolytic enzymes including CHYMOTRYPSIN; KALLIKREIN; PLASMIN; and TRYPSIN. It is used in the treatment of HEMORRHAGE associated with raised plasma concentrations of plasmin. It is also used to reduce blood loss and transfusion requirements in patients at high risk of major blood loss during and following open heart surgery with EXTRACORPOREAL CIRCULATION. (Reynolds JEF(Ed): Martindale: The Extra Pharmacopoeia (electronic version). Micromedex, Inc, Englewood, CO, 1995) BPTI, Basic Pancreatic Trypsin Inhibitor,Basic Pancreatic Trypsin Inhibitor,Bovine Kunitz Pancreatic Trypsin Inhibitor,Kallikrein-Trypsin Inactivator,Kunitz Pancreatic Trypsin Inhibitor,Trypsin Inhibitor, Basic, Pancreatic,Trypsin Inhibitor, Kunitz, Pancreatic,Antilysin,Bovine Pancreatic Trypsin Inhibitor,Contrical,Contrykal,Dilmintal,Iniprol,Kontrikal,Kontrykal,Pulmin,Traskolan,Trasylol,Zymofren,Inactivator, Kallikrein-Trypsin,Kallikrein Trypsin Inactivator
D007962 Leukocytes White blood cells. These include granular leukocytes (BASOPHILS; EOSINOPHILS; and NEUTROPHILS) as well as non-granular leukocytes (LYMPHOCYTES and MONOCYTES). Blood Cells, White,Blood Corpuscles, White,White Blood Cells,White Blood Corpuscles,Blood Cell, White,Blood Corpuscle, White,Corpuscle, White Blood,Corpuscles, White Blood,Leukocyte,White Blood Cell,White Blood Corpuscle
D009504 Neutrophils Granular leukocytes having a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes. LE Cells,Leukocytes, Polymorphonuclear,Polymorphonuclear Leukocytes,Polymorphonuclear Neutrophils,Neutrophil Band Cells,Band Cell, Neutrophil,Cell, LE,LE Cell,Leukocyte, Polymorphonuclear,Neutrophil,Neutrophil Band Cell,Neutrophil, Polymorphonuclear,Polymorphonuclear Leukocyte,Polymorphonuclear Neutrophil
D010436 Pepstatins N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin.
D011480 Protease Inhibitors Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES). Antiprotease,Endopeptidase Inhibitor,Endopeptidase Inhibitors,Peptidase Inhibitor,Peptidase Inhibitors,Peptide Hydrolase Inhibitor,Peptide Hydrolase Inhibitors,Peptide Peptidohydrolase Inhibitor,Peptide Peptidohydrolase Inhibitors,Protease Antagonist,Protease Antagonists,Antiproteases,Protease Inhibitor,Antagonist, Protease,Antagonists, Protease,Hydrolase Inhibitor, Peptide,Hydrolase Inhibitors, Peptide,Inhibitor, Endopeptidase,Inhibitor, Peptidase,Inhibitor, Peptide Hydrolase,Inhibitor, Peptide Peptidohydrolase,Inhibitor, Protease,Inhibitors, Endopeptidase,Inhibitors, Peptidase,Inhibitors, Peptide Hydrolase,Inhibitors, Peptide Peptidohydrolase,Inhibitors, Protease,Peptidohydrolase Inhibitor, Peptide,Peptidohydrolase Inhibitors, Peptide
D002402 Cathepsin D An intracellular proteinase found in a variety of tissue. It has specificity similar to but narrower than that of pepsin A. The enzyme is involved in catabolism of cartilage and connective tissue. EC 3.4.23.5. (Formerly EC 3.4.4.23).
D002403 Cathepsins A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES. Cathepsin
D002464 Cell Migration Inhibition Phenomenon of cell-mediated immunity measured by in vitro inhibition of the migration or phagocytosis of antigen-stimulated LEUKOCYTES or MACROPHAGES. Specific CELL MIGRATION ASSAYS have been developed to estimate levels of migration inhibitory factors, immune reactivity against tumor-associated antigens, and immunosuppressive effects of infectious microorganisms. Chemotaxis Inhibition,Chemotaxis Inhibitions,Inhibition, Chemotaxis,Inhibitions, Chemotaxis
D004791 Enzyme Inhibitors Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction. Enzyme Inhibitor,Inhibitor, Enzyme,Inhibitors, Enzyme
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man

Related Publications

E Lauritzen, and S Møller, and J Leerhoy
December 1985, Biochemical Society transactions,
E Lauritzen, and S Møller, and J Leerhoy
January 1998, Advances in experimental medicine and biology,
E Lauritzen, and S Møller, and J Leerhoy
October 1974, The Australian journal of experimental biology and medical science,
E Lauritzen, and S Møller, and J Leerhoy
January 1992, Scandinavian journal of clinical and laboratory investigation. Supplementum,
E Lauritzen, and S Møller, and J Leerhoy
January 1975, The Orthopedic clinics of North America,
E Lauritzen, and S Møller, and J Leerhoy
January 1998, Advances in experimental medicine and biology,
E Lauritzen, and S Møller, and J Leerhoy
May 1989, The Biochemical journal,
E Lauritzen, and S Møller, and J Leerhoy
June 1976, Scandinavian journal of immunology,
E Lauritzen, and S Møller, and J Leerhoy
February 1959, Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.),
E Lauritzen, and S Møller, and J Leerhoy
January 1988, Advances in experimental medicine and biology,
Copied contents to your clipboard!