Inhibition of bleomycin-induced cell death in rat alveolar macrophages and human lung epithelial cells by ambroxol.

The mitochondrial permeability transition is recognized to be involved in toxic and oxidative forms of cell injury. In the present study, we investigated the effect of ambroxol against the cytotoxicity of bleomycin (BLM) by looking at the effect on the mitochondrial membrane permeability in alveolar macrophages and lung epithelial cells. Alveolar macrophages or lung epithelial cells exposed to BLM revealed the loss of cell viability and increase in caspase-3 activity.

Production of macrophage inflammatory protein (MIP)-1alpha and MIP-1beta by human polymorphonuclear neutrophils stimulated with Porphyromonas endodontalis lipopolysaccharide.

This study was undertaken to investigate the capacity of polymorphonuclear neutrophils (PMNs) to secrete Macrophage Inflammatory Protein (MIP)-1alpha and MIP-1beta after stimulation with Porphyromonas endodontalis lipopolysaccharide (LPS). Escherichia coli LPS was used as a positive control. Venous blood was collected and PMNs were isolated from healthy volunteers.

Effect of R-(-)-deprenyl and harmaline on dopamine- and peroxynitrite-induced membrane permeability transition in brain mitochondria.

The present study examined the effect of MAO inhibitors, deprenyl and harmaline, on the membrane permeability transition in brain mitochondria. Deprenyl, harmaline, and antioxidant enzymes (SOD and catalase) attenuated alteration of the swelling, membrane potential, cytochrome c release, and Ca2+ transport in mitochondria treated with dopamine. In contrast, deprenyl and harmaline did not reduce the peroxynitrite-induced change in membrane permeability.

Identification of glyceraldehyde-3-phosphate dehydrogenase by protein sequencing in the rat postsynaptic density fraction.

Although many abundant proteins of the postsynaptic density (PSD) are known, most of the less abundant and minor PSD proteins await identification. In this work we attempted to identify a 37 kDa protein, which represented less than 1% of the total n-octyl glucoside (NOG)-insoluble proteins, by protein sequencing. To enrich the target protein, the NOG-insoluble fraction was first electrophoresed in 6% SDS-polyacrylamide gels, and the proteins smaller than 45 kDa compressed in the gel from were electroeluted and subsequently reseparated in 10% SDS-gels.