Journal
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
Volume 1840, Issue 8, Pages 2498-2505Publisher
ELSEVIER
DOI: 10.1016/j.bbagen.2014.02.002
Keywords
Serglycin; Chemokine; Primary human endothelial cell; Inflammation; Lipopolysaccharide; Interleukin-1 beta
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Funding
- South Eastern Norway Regional Health Authority
- Throne Hoist Foundation
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Background: Endothelial cells have important functions in e.g. regulating blood pressure, coagulation and host defense reactions. Serglycin is highly expressed by endothelial cells, but there is limited data on the roles of this proteoglycan in immune reactions. Methods: Cultured primary human endothelial cells were exposed to proinflammatory agents lipopolysaccharide (LPS) and interleukin 1 beta (IL-1 beta). The response in serglycin synthesis, secretion and intracellular localization and effect on the proteoglycan binding chemokines CXCL-1 and CXCL-8 were determined by qRT-PCR, Western blotting, immunocytochemistry, ELISA and serglycin knockdown experiments. Results: Both LPS and IL-1 beta increased the synthesis and secretion of serglycin, while only IL-1 beta increased serglycin mRNA expression. Stimulation increased the number of serglycin containing vesicles, with a greater portion of large vesicles after LPS treatment. Also, increased intracellular and secreted levels of CXCL-1 and CXCL-8 were observed. The increase in CXCL-8 secretion was unchanged in serglycin knockdown cells. However, the increase in CXCL-1 secretion from IL-1 beta stimulation was reduced 27% in serglycin knockdown cells; while the LPS-induced secretion was not affected. In serglycin expressing cells CXCL-1 positive vesicles were evenly distributed throughout the cytoplasm, while confided to the Golgi region in serglycin knockdown cells. This was the case only for IL-1 beta stimulated cells. LPS-induced CXCL-1 distribution was unaffected by serglycin expression. Conclusions: These results suggest that different signaling pathways are involved in regulating secretion of serglycin and partner molecules in activated endothelial cells. General significance: This knowledge increases our understanding of the roles of serglycin in immune reactions. This article is part of a Special Issue entitled: Matrix-mediated cell behaviour and properties. (C) 2014 Elsevier B.V. All rights reserved.
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