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請使用永久網址來引用或連結此文件:
http://ir.cmu.edu.tw/ir/handle/310903500/18566
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| 題名: | In search of the proteins associated with thrombomodulin |
| 作者: | 黃蕙君(Huang,Huey-Chun) |
| 貢獻者: | 健康照護學院醫學檢驗生物技術學系 |
| 日期: | 2005-03-26 |
| 上傳時間: | 2009-09-04 15:50:02 (UTC+8) |
| 摘要: | In search of the proteins associated with thrombomodulin Feng-Yi Lin,* Huey-Chun Huang, * Jia-Wei Huang, * Guey-Yueh Shi,* Hua-Lin Wu,* *Department of Biochemistry and Molecular Biology, National Cheng Kung University, Tainan, Taiwan Thrombomodulin(TM) is a membrane-intercalated glycoprotein, which functions in anticoagulation by virtue of complexation with thrombin. Ablation of the TM gene causes early postimplantation embryonic lethality that precedes the establishment of a functional cardiovascular system. TM may also possess functions distinct from its anticoagulant activity. Previous immunocytochemical studies have demonstrated that TM antigen was principally localized to the intercellular bridges between human keratinocytes (HaCaT) and TM-expressed human malignant melanoma (A2058) cell line. The TM antigen was found principally to the cellular protrusions such as microvilli, filopodia, and lamellipodia in human umbilical vein endothelial cells. Ezrin/radixin/moesin(ERM) proteins have been thought to play a central role in the organization of cortical actin-based cytoskeletons , including microvillar formation, through cross-linking actin filaments and integral membrane proteins such as CD43, CD44, and ICAM-2. ERM proteins bind to integral membrane proteins bearing a positively charged amino acid cluster in their juxta-membrane cytoplasmic domain. TM has a cluster of positively charged amino acids in the juxtamembrane region of the cytoplasmic tail similar to the sequence responsible for ERM binding in CD43, CD44 and ICAM-2. In this study, we explored whether ezrin could mediate TM association with the actin cytoskeleton. We found that the colocalization of ezrin and TM in actin-rich microspikes in HaCaT cells by confocal microscopy. Moreover we will investigate the interaction of TM and ezrin by in vitro binding assay. |
| 關聯: | 第20屆生物醫學聯合學術年會 |
| 顯示於類別: | [營養學系暨碩士班 ] 會議論文
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