Protein S attenuates the invasive potential of THP-1 cells by interfering with plasminogen binding on cell surface via a protein C-independent mechanism.
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.
Hryszko
Tomasz
T
Department of Physiology, Hamamatsu University School of Medicine, 1-20-1 Handa-yama, Hamamatsu 431-3192, Japan.
Suzuki
Yuko
Y
Mogami
Hideo
H
Urano
Tetsumei
T
D002465:Cell Movement / Q000187:drug effects; D002478:Cells, Cultured; D004789:Enzyme Activation; D006801:Humans; D009000:Monocytes / Q000187:drug effects / Q000502:physiology*; D010958:Plasminogen / Q000037:antagonists & inhibitors* / Q000378:metabolism; D011486:Protein C / Q000378:metabolism; D017293:Protein S / Q000378:metabolism / Q000494:pharmacology / Q000502:physiology*
D011486:Protein C; D017293:Protein S; D010958:Plasminogen