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    Please use this identifier to cite or link to this item: http://asiair.asia.edu.tw/ir/handle/310904400/16107

    Title: Lysophosphatidic acid stimulates thrombomodulin lectin-like domain shedding in human endothelial cells
    Authors: 黃元勵;Huang, Yuan-Li
    Contributors: 生物科技學系
    Keywords: Thrombomodulin;Lysophosphatidic acid;Endothelial cells
    Date: 2008
    Issue Date: 2012-11-23 17:08:38 (UTC+8)
    Abstract: "Thrombomodulin (TM) is an anticoagulant glycoprotein highly expressed on endothelial cell surfaces. Increased levels of soluble TM
    in circulation have been widely accepted as an indicator of endothelial damage or dysfunction. Previous studies indicated that various
    proinflammatory factors stimulate TM shedding in various cell types such as smooth muscle cells and epithelial cells. Lysophosphatidic
    acid (LPA) is a bioactive lipid mediator present in biological fluids during endothelial damage or injury. In the present study, we first
    observed that LPA triggered TM shedding in human umbilical vein endothelial cells (HUVECs). By Cyflow analysis, we showed that
    the LPA-induced accessibility of antibodies to the endothelial growth factor (EGF)-like domain of TM is independent of matrix metalloproteinases (MMPs), while LPA-induced TM lectin-like domain shedding is MMP-dependent. Furthermore, a stable cell line expressing
    TM without its lectin-like domain exhibited a higher cell proliferation rate than a stable cell line expressing full-length TM. These results
    imply that LPA induces TM lectin-like domain shedding, which might contribute to the exposure of its EGF-like domain for EGF receptor (EGFR) binding, thereby stimulating subsequent cell proliferation. Based on our findings, we propose a novel mechanism for the
    exposure of TM EGF-like domain, which possibly mediates LPA-induced EGFR transactivation.
    2007 Elsevier Inc. All rights reserved."
    Appears in Collections:[生物科技學系] 期刊論文

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