國家衛生研究院 NHRI:Item 3990099045/6253
English  |  正體中文  |  简体中文  |  全文笔数/总笔数 : 12145/12927 (94%)
造访人次 : 858785      在线人数 : 783
RC Version 6.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
搜寻范围 查询小技巧：
  • 您可在西文检索词汇前后加上"双引号"，以获取较精准的检索结果
  • 若欲以作者姓名搜寻，建议至进阶搜寻限定作者字段，可获得较完整数据
    •  进阶搜寻
    主页 ‧ 登入 ‧ 上传 ‧ 说明 ‧ 关于NHRI ‧ 管理 到手机版


    jsp.display-item.identifier=請使用永久網址來引用或連結此文件: http://ir.nhri.org.tw/handle/3990099045/6253


    题名: TM hidden treasure: lectin-like domain
    作者: Wu, KK
    贡献者: Institute of Cellular and Systems Medicine
    摘要: Thrombomodulin (TM) anchors to vascular endothelial cell membrane with a single transmembranous domain.2,3 It has a large extracellular region that comprises a C-type lectin-like domain at the N-terminus, an epidermal growth factor (EGF)–homology domain that contains 6 EGF-like structures, and a Ser/Thr-rich domain linked to the membrane (see figure). Thrombin and protein C bind to the EGF-homology domain where thrombin cleaves protein C to generate activated protein C (aPC).2 aPC is released into the blood where together with protein S it degrades coagulation factors VIIIa and Va and thereby prevents excessive blood clotting. aPC also possesses anti-inflammatory actions and is effective in controlling inflammatory tissue damage caused by sepsis. Biochemical mechanisms and physiologic roles of TM in coagulation and inflammation have been well characterized.2 However, biochemical characterization has been focused on the thrombin and protein C binding sites at the EGF-homology domain. Little is known about the biologic activity and physiologic role of the C-type lectin-like domain. Kuo and colleagues have generated recombinant TMD1 and used it to probe the biologic activity of the lectin-like domain. They previously reported in Blood that TMD1 binds specifically to LeY and through its binding to Lewis Y epitope on lipopolysaccharide (LPS), it suppresses LPS-induced inflammatory responses.4 Here, Kuo et al provide evidence that recombinant TMD1 controls endothelial cell migration and tube formation through binding to LeY clustered at the endothelial cell membrane ruffles and protrusions.1 Their results show that LeY mediates angiogenesis and TMD1 or LeY antibodies abrogate the angiogenic effect. Epidermal growth factor receptor (EGFR) is expressed on endothelial cell surface. It contains LeY that may be involved in angiogenesis. Investigations in vivo show that TMD1 blocks in vivo angiogenesis induced by EGF and suppresses tumor growth by inhibiting tumor angiogenesis. Taken together, the results indicate that the lectin-like domain of TM is a receptor for LeY that blocks angiogenesis and attenuates inflammatory tissue damage by binding and neutralizing LeY.
    日期: 2012-02-02
    關聯: Blood. 2012 Feb 2;119(5):1103-1104.
    Link to: http://dx.doi.org/10.1182/blood-2011-12-394544
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=0006-4971&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000300400300007
    Cited Times(Scopus): http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84856592461
    显示于类别:[伍焜玉] 期刊論文

    文件中的档案:

    档案 描述 大小格式浏览次数
    NCS2012022002.pdf262KbAdobe PDF575检视/开启


    在NHRI中所有的数据项都受到原著作权保护.

    TAIR相关文章

    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - 回馈