ABSTRACT
OBJECTIVE: To investigate the effects of musk-1, a glucoprotein component isolated from the water extract of musk, on some functions of rat polymorphonuclear leukocytes activated by IL-8 in vitro. METHOD: An in vitro incubation system was used. Superoxide anion production was determined by cytochrome C reduction. beta-glucuronidase and lysozyme release was quantitated by enzyme reactions in which phenolph-thaleinglucuronic acid and Micrococcus Lysodeikticus were as the substrates, respectively. RESULTS: In comparison with control, musk-1 at concentration 1-100 micrograms.ml-1 can increase superoxide anion production by 91.7%-291%, and decrease beta-glucuronidase and lysozyme release by 2.2%-58.1% and 3.9%-39.8%, respectively. CONCLUSION: Inhibition of lysosomel enzyme release might be considered as one of mechanisms of antiinflammatory action of musk.
Subject(s)
Anti-Inflammatory Agents, Non-Steroidal/pharmacology , Fatty Acids, Monounsaturated/pharmacology , Glucuronidase/metabolism , Materia Medica/pharmacology , Neutrophils/metabolism , Animals , Female , Male , Muramidase/metabolism , Oxygen/metabolism , Rats , Rats, WistarABSTRACT
Proteins, with the large variety of chemical groups they present at their molecular surface, are a class of molecules which can be very informative on most of the possible solute-solvent interactions. Hen egg white lysozyme has been used as a probe to investigate the complex solvent dynamics occurring at the protein surface, by analysing the results obtained from Nuclear Magnetic Resonance, X-ray diffractometry and Molecular Dynamics simulations. A consistent overall picture for the dynamics of water molecules close to the protein is obtained, suggesting that a rapid exchange occurs, in a picosecond timescale, among all the possible hydration surface sites both in solution and the solid state, excluding the possibility that solvent molecules can form liquid-crystal-like supramolecular adducts, which have been proposed as a molecular basis of 'memory of water'.