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investigate the role of cationic antimicrobial protein of Mr 37?kDa (CAP37) a neutrophil derived inflammatory mediator on endothelial cell function Data sources Endothelial cells used in this study were obtained from human lung microvessels and rat aorta The latter was a kind gift of Dr Paula Grammas The mono mac 6 cell line used in this study was the generous gift of Dr H W Loms Ziegler Heitbrock Study selection and data extraction Endothelial cell proteins kinase C activity was determined by measuring calcium and phospholipid dependent phosphorylation of histone Endothelial cell migration was determined using Costar TM Transwell apparatus Cell surface expression of adhesion molecules, ICAM 1 and PECAM 1 was determined using flow cytometry RT PCR was used to amplify the CAP37 from endothelial cells treated with LPS Results We demonstrated that CAP37 which was originally identified as having potent antimicrobial activity and chemotactic activity for monocytes was capable of modulating endothelial cell functions CAP37 activated endothelial cell protein kinase C in a dose and time dependent fashion Importantly CAP37 increased the adhesive properties of the endothelium for monocytes CAP37 upregulated the well known adhesion molecules, ICAM 1 and PECAM 1 in a dose and time dependent manner In addition, CAP37 promoted endothelial cell migration Further investigations indicated that CAP37 was induced in endothelial cells in response to pro inflammatory cytokines such as tumor necrosis factor α and interleukin 1α as well as inflammatory mediators such as lipopolysaccharide Unstimulated endothelial cells did not constitutively express CAP37 The cDNA sequence of endothelial CAP37 was determined and found to be highly homologous to the sequence obtained for neutrophil derived CAP37 Conclusions Our studies strongly suggest that CAP37 plays a pivotal role in monocyte endothelial interactions and the transmigration of monocytes from the vasculature into extravascular tissues
The investigation of role of cationic antimicrobial protein of Mr 37?kDa (CAP37) a neutrophil derived inflammatory mediator on endothelial cell function Data sources Endothelial cells used in this study were obtained from human lung microvessels and rat aorta The latter was a kind gift of Dr Paula Grammas The mono mac 6 cell line used in this study was the generous gift of Dr HW Loms Ziegler Heitbrock Study selection and data extraction Endothelial cell proteins kinase C activity was determined by measuring calcium and phospholipid dependent phosphorylation of histone Endothelial cell migration was determined using Costar TM Transwell apparatus Cell surface expression of adhesion molecules, ICAM 1 and PECAM 1 was determined using flow cytometry RT PCR was used to amplify the CAP37 from endothelial cells treated with LPS Results We demonstrated that CAP37 which was opened as having potent antimicrobial activity and chemotactic Activity fo r monocytes was capable of modulating endothelial cell functions CAP37 activated endothelial cell protein kinase C in a dose and time dependent fashion Importantly CAP37 increased the adhesive properties of the endothelium for monocytes CAP37 upregulated the well known adhesion molecules, ICAM 1 and PECAM 1 in a dose And time time dependent manner In addition, CAP37 promoted endothelial cell migration further investigations were indicated and that CAP37 was induced in endothelial cells in response to pro inflammatory cytokines such as tumor necrosis factor α and interleukin 1α as well as inflammatory mediators such as lipopolysaccharide Unstimulated endothelial cells did not Constitutively express CAP37 The cDNA sequence of endothelial CAP37 was determined and found to be highly homologous to the sequence obtained ne nemophily derived CAP37 CONCLUSIONs our study strongly suggests that CAP37 plays a pivotal role in monocyte endothelial interactions and the transmi GrAtion of monocytes from the vasculature into extravascular tissues