calcimycin has been researched along with montelukast* in 2 studies
2 other study(ies) available for calcimycin and montelukast
| Article | Year |
|---|---|
Role of cysteinyl leukotrienes in the proliferation and the migration of murine vascular smooth muscle cells in vivo and in vitro.
Topics: Acetates; Animals; Anti-Bacterial Agents; Calcimycin; Cell Movement; Cell Proliferation; Cells, Cultured; Cyclopropanes; Cysteine; Femoral Artery; Leukotriene Antagonists; Leukotrienes; Lipopolysaccharides; Macrophages; Male; Mice; Mice, Inbred C57BL; Models, Animal; Muscle, Smooth, Vascular; Myocytes, Smooth Muscle; Neovascularization, Physiologic; Quinolines; Sulfides; Wound Healing | 2007 |
Novel inhibitory effect on 5-lipoxygenase activity by the anti-asthma drug montelukast.
5-Lipoxygenase is the key enzyme in the biosynthesis of leukotrienes, powerful lipid mediators involved in inflammation, cell-cell communication, and other important physiological and pathological conditions. Particularly, cysteinyl-leukotrienes have been recognized as playing a significant role in the pathophysiology of asthma and potent and effective Cys-LT1 receptor antagonists have been developed for the treatment of this illness. Here we report that montelukast, a structural Cys-LT1 receptor antagonist, also exerts a substantial and apparently direct inhibitory effect on 5-lipoxygenase activity in vitro, at concentrations in the lower micromolar range, which are of potential therapeutic relevance. Thus, when human mast cells HMC-1 were stimulated with the Ca ionophore A23187 in the presence of montelukast (up to 100 microM) a substantial decline in 5-lipoxygenase biosynthesis was observed. Similar results were obtained in the rat mast cell-like RBL-1 cell model (IC50 congruent with 2.5 microM) and in human polymorphonuclear leukocytes. Moreover, montelukast directly inhibited human recombinant 5-lipoxygenase. Kinetic experiments revealed that the inhibition was of the non-competitive type, suggesting that montelukast binds a yet undefined allosteric site on 5-lipoxygenase. 5-Lipoxygenase inhibition by montelukast appears to be highly selective since the drug had no effects on other enzymes of the leukotriene cascade, viz. LTC4 synthase and LTA hydrolase. Topics: Acetates; Allosteric Site; Animals; Anti-Asthmatic Agents; Asthma; Calcimycin; Calcium; Catalysis; Cell Line; Cell Line, Tumor; Cell Survival; Cells, Cultured; Chromatography, High Pressure Liquid; Cyclopropanes; Dexamethasone; Dose-Response Relationship, Drug; HL-60 Cells; Humans; Inhibitory Concentration 50; Kinetics; Leukotriene B4; Leukotriene C4; Lipoxygenase Inhibitors; Mast Cells; Neutrophils; Protein Binding; Quinolines; Rats; Recombinant Proteins; Sulfides | 2004 |