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

• Published in: BMB reports Vol. 48; no. 11; pp. 624 - 629
• Main Authors: Ku, Sae-Kwang, Yoon, Eun-Kyung, Lee, Hyun Gyu, Han, Min-Su, Lee, Taeho, Bae, Jong-Sup
• Format: Journal Article
• Language: English
• Published: Korea (South) 생화학분자생물학회 01.11.2015
• Subjects: Animals; Blood Coagulation Factors - metabolism; Humans; Interleukin-1beta - metabolism; Male; Mice; Mice, Inbred C57BL; Muramidase - metabolism; Muramidase - pharmacology; p38 Mitogen-Activated Protein Kinases - metabolism; Primary Cell Culture; Receptors, Cell Surface - metabolism; Tetradecanoylphorbol Acetate - pharmacology; Tumor Necrosis Factor-alpha - metabolism; 화학
• ISSN: 1976-6696; 1976-670X
• DOI: 10.5483/BMBRep.2015.48.11.038

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)-1β-, and 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.