salicylates and thiophenol

Salicylideneamino-2-thiophenol (Sal) regulated the redox status and the expression of chemokines induced by tert-butyl hydroperoxide (t-BHP). Sal (100 microM) increased reduced/oxidized glutathione (GSH/GSSG) ratios and thiol (SH) levels by 210 and 157%, respectively, and decreased reactive oxygen species (ROS) levels by 60% in t-BHP-treated macrophages. The inductions of regulated upon activation, normal T-cell expressed and secreted (RANTES), monocyte chemoattractant protein-1 (MCP-1), interleukin-8 (IL-8) and hypoxia inducible factor-1alpha (HIF-1alpha) by t-BHP (10 microM) were decreased to 250, 80, 80 and 500% by Sal (100 microM), respectively. In the Sal signaling pathway, c-Jun N-terminal kinases (JNK), extracellular signal-regulated kinases (ERK) and p38 signaling protein modulation were decreased by 67, 69 and 119%, respectively, by Sal at 100 microM. Sal (100 microM) also altered cytosol and nuclear NF-kappaB protein expression by 169 and 5%, respectively. Sal also attenuated NF-kappaB nuclear binding activity. Sal thus has a protective effect against t-BHP-induced inflammation and that this, in part, is due to the inhibition of the production of RANTES, MCP-1, IL-8 and HIF-1alpha via the modulation of the NF-kappaB and mitogen-activated protein kinase (MAPK) pathways.

Topics: Animals; Chemokine CCL2; Chemokine CCL5; Gene Expression Regulation; Glutathione; Hypoxia-Inducible Factor 1, alpha Subunit; Inflammation; Interleukin-8; Macrophages, Peritoneal; Mitogen-Activated Protein Kinases; NF-kappa B; Phenols; Rats; RNA, Messenger; Salicylates; Salicylic Acid; Sulfhydryl Compounds; tert-Butylhydroperoxide

The base induced addition of benzenethiol to 2-cyclohexen-1-one and its 4,4-, 5,5- and 6,6-dimethyl derivatives is catalysed by a salophen-uranyl based metallocleft 2 in chloroform solution with high turnover efficiency and low product inhibition. Analysis of rate data coupled with equilibrium measurements for complexation of the catalyst with the enone reactants and addition products shows that the catalytic mechanism involves the three main steps typical of single-substrate enzymatic processes, namely substrate binding and recognition, transformation of the bound substrate, and release of the reaction product. Unlike the reference salophen-uranyl 1, catalyst 2 is endowed with a structured binding site responsible for a high degree of substrate specificity among the investigated enones, due to recognition of their shape and size.

Topics: Antinematodal Agents; Binding Sites; Binding, Competitive; Catalysis; Cyclohexanones; Enzymes; Kinetics; Organometallic Compounds; Phenols; Salicylates; Substrate Specificity; Sulfhydryl Compounds; Titrimetry; Uranium

Topics: Anti-Bacterial Agents; Benzene; Benzene Derivatives; Cresols; Phenols; Salicylates; Sulfhydryl Compounds