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10.1007/s00018-017-2694-7 http://scihub22266oqcxt.onion/10.1007/s00018-017-2694-7 C5843676!5843676!29080903     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Mol+Life+Sci 2018 ; 75 (7): 1269-84 Nephropedia Template TP {{tp|p=29080903|t=2018. Human endoglin as a potential new partner involved in platelet?endothelium interactions |pdf=|usr=}}{{29080903}} gab.com Text Human endoglin as a potential new partner involved in platelet endothelium interactions JO: Cell Mol Life Sci http://www.kidney.de/pget.php?&tw=1&pmid=29080903 #FOAvip Complex interactions between platelets and activated endothelium occur during the thrombo-inflammatory reaction at sites of vascular injuries and during vascular hemostasis. The endothelial receptor endoglin is involved in inflammation through integrin-mediated leukocyte adhesion and transmigration; and heterozygous mutations in the endoglin gene cause hereditary hemorrhagic telangiectasia type 1. This vascular disease is characterized by a bleeding tendency that is postulated to be a consequence of telangiectasia fragility rather than a platelet defect, since platelets display normal functions in vitro in this condition. Here, we hypothesize that endoglin may act as an adhesion molecule involved in the interaction between endothelial cells and platelets through integrin recognition. We find that the extracellular domain of human endoglin promotes specific platelet adhesion under static conditions and confers resistance of adherent platelets to detachment upon exposure to flow. Also, platelets adhere to confluent endothelial cells in an endoglin-mediated process. Remarkably, Chinese hamster ovary cells ectopically expressing the human ?IIb?3 integrin acquire the capacity to adhere to myoblast transfectants expressing human endoglin, whereas platelets from Glanzmann?s thrombasthenia patients lacking the ?IIb?3 integrin are defective for endoglin-dependent adhesion to endothelial cells. Furthermore, the bleeding time, but not the prothrombin time, is significantly prolonged in endoglin-haplodeficient (Eng+/?) mice compared to Eng+/+ animals. These results suggest a new role for endoglin in ?IIb?3 integrin-mediated adhesion of platelets to the endothelium, and may provide a better understanding on the basic cellular mechanisms involved in hemostasis and thrombo-inflammatory events.Electronic supplementary material: The online version of this article (doi:10.1007/s00018-017-2694-7) contains supplementary material, which is available to authorized users. Twit Text FOAVip Human endoglin as a potential new partner involved in platelet endothelium interactions ????Cell Mol Life Sci http://www.kidney.de/pget.php?&tw=1&pmid=29080903 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29080903 #FOAvip English Wikipedia <ref>{{Cite pmid|29080903}}</ref> Human endoglin as a potential new partner involved in platelet?endothelium interactions #MMPMID29080903 Rossi E; Pericacho M; Bachelot-Loza C; Pidard D; Gaussem P; Poirault-Chassac S; Blanco FJ; Langa C; González-Manchón C; Novoa JML; Smadja DM; Bernabeu C Cell Mol Life Sci 2018[]; 75 (7): 1269-84 PMID29080903show ga Complex interactions between platelets and activated endothelium occur during the thrombo-inflammatory reaction at sites of vascular injuries and during vascular hemostasis. The endothelial receptor endoglin is involved in inflammation through integrin-mediated leukocyte adhesion and transmigration; and heterozygous mutations in the endoglin gene cause hereditary hemorrhagic telangiectasia type 1. This vascular disease is characterized by a bleeding tendency that is postulated to be a consequence of telangiectasia fragility rather than a platelet defect, since platelets display normal functions in vitro in this condition. Here, we hypothesize that endoglin may act as an adhesion molecule involved in the interaction between endothelial cells and platelets through integrin recognition. We find that the extracellular domain of human endoglin promotes specific platelet adhesion under static conditions and confers resistance of adherent platelets to detachment upon exposure to flow. Also, platelets adhere to confluent endothelial cells in an endoglin-mediated process. Remarkably, Chinese hamster ovary cells ectopically expressing the human ?IIb?3 integrin acquire the capacity to adhere to myoblast transfectants expressing human endoglin, whereas platelets from Glanzmann?s thrombasthenia patients lacking the ?IIb?3 integrin are defective for endoglin-dependent adhesion to endothelial cells. Furthermore, the bleeding time, but not the prothrombin time, is significantly prolonged in endoglin-haplodeficient (Eng+/?) mice compared to Eng+/+ animals. These results suggest a new role for endoglin in ?IIb?3 integrin-mediated adhesion of platelets to the endothelium, and may provide a better understanding on the basic cellular mechanisms involved in hemostasis and thrombo-inflammatory events.Electronic supplementary material: The online version of this article (doi:10.1007/s00018-017-2694-7) contains supplementary material, which is available to authorized users. äHuman endoglin as a potential new partner involved in platelet?endothe(epmc).pdf DeepDyve Pubget Overpricing