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http://dx.doi.org/10.5483/BMBRep.2015.48.11.038

Inhibitory effects of lysozyme on endothelial protein C 1receptor shedding in vitro and in vivo  

Ku, Sae-Kwang (Department of Anatomy and Histology, College of Korean Medicine, Daegu Haany University)
Yoon, Eun-Kyung (College of Pharmacy, CMRI, Research Institute of Pharmaceutical Sciences, Kyungpook National University)
Lee, Hyun Gyu (Department of Microbiology and Immunology, Yonsei University College of Medicine)
Han, Min-Su (Laboratory for Arthritis and Bone Biology, Fatima Research Institute, Daegu Fatima Hospital)
Lee, Taeho (College of Pharmacy, CMRI, Research Institute of Pharmaceutical Sciences, Kyungpook National University)
Bae, Jong-Sup (College of Pharmacy, CMRI, Research Institute of Pharmaceutical Sciences, Kyungpook National University)
Publication Information
BMB Reports / v.48, no.11, 2015 , pp. 624-629 More about this Journal
Abstract
Lysozyme protects us from the ever-present danger of bacterial infection and binds to bacterial lipopolysaccharide (LPS) with high affinity. Beyond its role in the activation of protein C, the endothelial cell protein C receptor (EPCR) plays an important role in the cytoprotective pathway. EPCR can be shed from the cell surface, which is mediated by tumor necrosis factor-α converting enzyme (TACE). However, little is known about the effects of lysozyme on EPCR shedding. We investigated this issue by monitoring the effects of lysozyme on phorbol-12-myristate 13-acetate (PMA)-, tumor necrosis factor (TNF)-α-, interleukin (IL)-1βand cecal ligation and puncture (CLP)-mediated EPCR shedding and underlying mechanism. Data demonstrate that lysozyme induced potent inhibition of PMA-, TNF-α-, IL-1β-, and CLP-induced EPCR shedding. Lysozyme also inhibited the expression and activity of PMA-induced TACE in endothelial cells. These results demonstrate the potential of lysozyme as an anti-EPCR shedding reagent against PMA-mediated and CLP-mediated EPCR shedding.
Keywords
CLP; EPCR shedding; Lysozyme; Vascular inflammation;
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