n-n-n-trimethylsphingosine has been researched along with Inflammation* in 2 studies
1 review(s) available for n-n-n-trimethylsphingosine and Inflammation
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[Bioregulatory functions of methylsphingosines: in relation to sphingolipid signaling pathway and on approach of introducing sphingolipid-based drugs].
Topics: Apoptosis; Cell Division; Cell Membrane; Hydrogen Bonding; Inflammation; Neoplasm Metastasis; Neoplasms; Platelet Activation; Protein Kinase C; Reperfusion Injury; Signal Transduction; Sphingolipids; Sphingosine | 1998 |
1 other study(ies) available for n-n-n-trimethylsphingosine and Inflammation
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Inhibition of chemotactic motility and trans-endothelial migration of human neutrophils by sphingosine 1-phosphate.
In previous studies, we reported that sphingosine 1-phosphate (Sph-1-P) inhibits the chemotactic motility of some cancer cell lines such as mouse melanoma cells, as well as human smooth muscle cells, at a very low concentration, as demonstrated by a transwell migration assay method (Proc. Natl. Acad. Sci. USA 89, 9698, 1992; J. Cell Biol. 130, 193, 1995). In this study, we investigated the effect of Sph-1-P on the chemotactic motility and invasiveness of human neutrophils, utilizing three different assay systems: (a) a transwell migration assay where IL-8 or fLMP was added as a chemotactic factor, (b) a phagokinetic assay with gold colloids, and (c) a trans-endothelial migration assay with human umbilical vein endothelial cells (HUVECs) plated on collagen layers. We found that among various sphingosine derivatives, Sph-1-P specifically inhibited the IL-8- or fLMP-induced chemotactic migration of neutrophils at concentrations below 1 microM. Phagokinetic activity of neutrophils was also suppressed by Sph-1-P, but more moderately than by the PKC inhibitory sphingosine analog, trimethylsphingosine. Finally, Sph-1-P inhibited trans-endothelial migration and invasiveness of neutrophils into HUVEC-covered collagen layers, whereas no effect on their adhesion to HUVECs was observed. These observations strongly suggest that Sph-1-P can act as a specific and effective motility regulator of human neutrophils, raising the possibility of future applications of Sph-1-P, or its analogs, as anti-inflammatory agents regulating invasive migration of neutrophils through endothelial layers at injured vascular sites. Topics: Cell Adhesion; Cell Movement; Cells, Cultured; Ceramides; Chemotaxis; Enzyme Inhibitors; Gold Colloid; Humans; Inflammation; Interleukin-8; Lysophospholipids; N-Formylmethionine Leucyl-Phenylalanine; Neutrophils; Phagocytosis; Protein Kinase C; Sphingosine; Umbilical Cord | 1997 |