| RRC ID |
42464
|
| Author |
Hryszko T, Suzuki Y, Mogami H, Urano T.
|
| Title |
Protein S attenuates the invasive potential of THP-1 cells by interfering with plasminogen binding on cell surface via a protein C-independent mechanism.
|
| Journal |
FEBS Lett
|
| 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.
|
| Volume |
579(27)
|
| Pages |
6023-6
|
| Published |
2005-11-7
|
| DOI |
10.1016/j.febslet.2005.09.080
|
| PII |
S0014-5793(05)01171-3
|
| PMID |
16229836
|
| MeSH |
Cell Movement* / drug effects
Cells, Cultured
Enzyme Activation
Humans
Monocytes / drug effects
Monocytes / physiology*
Plasminogen / antagonists & inhibitors*
Plasminogen / metabolism
Protein C / metabolism
Protein S / metabolism
Protein S / pharmacology
Protein S / physiology*
|
| IF |
3.057
|
| Times Cited |
1
|
|
WOS Category
|
BIOPHYSICS
BIOCHEMISTRY & MOLECULAR BIOLOGY
CELL BIOLOGY
|
| Resource |
| Human and Animal Cells |
THP-1(RCB1189) |
