| First Author | Popp M | Year | 2015 |
| Journal | PLoS One | Volume | 10 |
| Issue | 7 | Pages | e0133429 |
| PubMed ID | 26172113 | Mgi Jnum | J:233538 |
| Mgi Id | MGI:5784945 | Doi | 10.1371/journal.pone.0133429 |
| Citation | Popp M, et al. (2015) Normal Platelet Integrin Function in Mice Lacking Hydrogen Peroxide-Induced Clone-5 (Hic-5). PLoS One 10(7):e0133429 |
| abstractText | Integrin alphaIIbbeta3 plays a central role in the adhesion and aggregation of platelets and thus is essential for hemostasis and thrombosis. Integrin activation requires the transmission of a signal from the small cytoplasmic tails of the alpha or beta subunit to the large extracellular domains resulting in conformational changes of the extracellular domains to enable ligand binding. Hydrogen peroxide-inducible clone-5 (Hic-5), a member of the paxillin family, serves as a focal adhesion adaptor protein associated with alphaIIbbeta3 at its cytoplasmic tails. Previous studies suggested Hic-5 as a novel regulator of integrin alphaIIbbeta3 activation and platelet aggregation in mice. To assess this in more detail, we generated Hic-5-null mice and analyzed activation and aggregation of their platelets in vitro and in vivo. Surprisingly, lack of Hic-5 had no detectable effect on platelet integrin activation and function in vitro and in vivo under all tested conditions. These results indicate that Hic-5 is dispensable for integrin alphaIIbbeta3 activation and consequently for arterial thrombosis and hemostasis in mice. |
