capsazepine has been researched along with Pneumonia* in 2 studies
2 other study(ies) available for capsazepine and Pneumonia
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Regulation of MMP-9 by a WIN-binding site in the monocyte-macrophage system independent from cannabinoid receptors.
The cannabinoid system is known to be involved in the regulation of inflammatory processes. Therefore, drugs targeting cannabinoid receptors are considered as candidates for anti-inflammatory and tissue protective therapy. We demonstrated that the prototypical cannabinoid agonist R(+)WIN55,212-2 (WIN) reduced the secretion of matrix metalloproteinase-9 (MMP-9) in a murine model of cigarette-smoke induced lung inflammation. In experiments using primary cells and cell lines of the monocyte-macrophage-system we found that binding of the cannabinoid-receptor agonist WIN to a stereo-selective, specific binding site in cells of the monocyte-macrophage-system induced a significant down-regulation of MMP-9 secretion and disturbance of intracellular processing, which subsequently down-regulated MMP-9 mRNA expression via a ERK1/2-phosphorylation-dependent pathway. Surprisingly, the anti-inflammatory effect was independent from classical cannabinoid receptors. Our experiments supposed an involvement of TRPV1, but other yet unidentified sites are also possible. We conclude that cannabinoid-induced control of MMP-9 in the monocyte-macrophage system via a cannabinoid-receptor independent pathway represents a general option for tissue protection during inflammation, such as during lung inflammation and other diseases associated with inflammatory tissue damage. Topics: Animals; Benzoxazines; Binding Sites; Bone Resorption; Bronchoalveolar Lavage Fluid; Capsaicin; Cell Differentiation; Disease Models, Animal; Extracellular Signal-Regulated MAP Kinases; Gene Expression Regulation, Enzymologic; Glycosylation; Humans; Macrophages; Matrix Metalloproteinase 9; Mice; Microglia; Monocytes; Morpholines; Naphthalenes; Osteoclasts; Phosphorylation; Pneumonia; PPAR gamma; Receptors, Cannabinoid; rho GTP-Binding Proteins; Signal Transduction; TRPV Cation Channels | 2012 |
Role of substance P in hydrogen sulfide-induced pulmonary inflammation in mice.
We have shown earlier that H(2)S acts as a mediator of inflammation. In this study, we have investigated the involvement of substance P and neurogenic inflammation in H(2)S-induced lung inflammation. Intraperitoneal administration of NaHS (1-10 mg/kg), an H(2)S donor, to mice caused a significant increase in circulating levels of substance P in a dose-dependent manner. H(2)S alone could also cause lung inflammation, as evidenced by a significant increase in lung myeloperoxidase activity and histological evidence of lung injury. The maximum effect of H(2)S on substance P levels and on lung inflammation was observed 1 h after NaHS administration. At this time, a significant increase in lung levels of TNF-alpha and IL-1beta was also observed. In substance P-deficient mice, the preprotachykinin-A knockout mice, H(2)S did not cause any lung inflammation. Furthermore, pretreatment of mice with CP-96345 (2.5 mg/kg ip), an antagonist of the neurokinin-1 (NK(1)) receptor, protected mice against lung inflammation caused by H(2)S. However, treatment with antagonists of NK(2), NK(3), and CGRP receptors did not have any effect on H(2)S-induced lung inflammation. Depleting neuropeptide from sensory neurons by capsaicin (50 mg/kg sc) significantly reduced the lung inflammation caused by H(2)S. In addition, pretreatment of mice with capsazepine (15 mg/kg sc), an antagonist of the transient receptor potential vanilloid-1, protected mice against H(2)S-induced lung inflammation. These results demonstrate a key role of substance P and neurogenic inflammation in H(2)S-induced lung injury in mice. Topics: Air Pollutants; Animals; Anti-Inflammatory Agents, Non-Steroidal; Biphenyl Compounds; Capsaicin; Female; Hydrogen Sulfide; Inflammation Mediators; Lung; Male; Mice; Mice, Inbred BALB C; Mice, Mutant Strains; Neurokinin-1 Receptor Antagonists; Peroxidase; Pneumonia; Protein Precursors; Substance P; Tachykinins; TRPV Cation Channels | 2006 |