Protein S attenuates the invasive potential of THP-1 cells by interfering with plasminogen binding on cell surface via a protein C-independent mechanism |
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Authors: | Hryszko Tomasz Suzuki Yuko Mogami Hideo Urano Tetsumei |
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Institution: | Department of Physiology, Hamamatsu University School of Medicine, 1-20-1 Handa-yama, Hamamatsu 431-3192, Japan. |
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Abstract: | Protein S, a cofactor for activated protein C (aPC) to inactivate coagulation factors, also plays a pivotal role in inflammation. Based on our recent findings that aPC and protein S modifies tissue plasminogen activator (tPA)-catalyzed activation of Glu-plasminogen (Glu-plg), we analyzed possible role of protein S in cell-associated plasminogen activation and invasive potential of inflammatory cells. Monocyte-like THP-1 cells, to which both plasminogen and tPA bind, enhanced tPA-catalyzed plasminogen activation, which was partially abolished by protein S but not by aPC. Protein S attenuated both the plasminogen binding to THP-1 cells and associated their invasive potential through Matrigel. |
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Keywords: | aPC activated protein C C4BP C4b-binding protein Gla γ-carboxyl glutamic acid Glu-plg Glu-plasminogen HBSS Hanks’ balanced salt solution tPA tissue plasminogen activator |
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