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10.1002/rth2.12088 http://scihub22266oqcxt.onion/10.1002/rth2.12088 C5974921!5974921!30046741     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Res+Pract+Thromb+Haemost 2018 ; 2 (2): 370-9 Nephropedia Template TP {{tp|p=30046741|t=2018. MMP?13 binds to platelet receptors ?IIb?3 and GPVI and impairs aggregation and thrombus formation |pdf=|usr=}}{{30046741}} gab.com Text MMP 13 binds to platelet receptors IIb 3 and GPVI and impairs aggregation and thrombus formation JO: Res Pract Thromb Haemost http://www.kidney.de/pget.php?&tw=1&pmid=30046741 #FOAvip Essentials: MMP?13 has the potential to influence platelet function and thrombus formation directly.We sought to elucidate whether MMP?13 is able to bind to specific platelet receptors.MMP?13 is able to bind to platelet alphaIIbbeta3 (?IIb?3) and glycoprotein (GP)VI.These interactions are sufficient to inhibit platelet aggregation and thrombus formation. Background: Acute thrombotic syndromes lead to atherosclerotic plaque rupture with subsequent thrombus formation, myocardial infarction and stroke. Following rupture, flowing blood is exposed to plaque components, including collagen, which triggers platelet activation and aggregation. However, plaque rupture releases other components into the surrounding vessel which have the potential to influence platelet function and thrombus formation. Objectives: Here we sought to elucidate whether matrix metalloproteinase?13 (MMP?13), a collagenolytic metalloproteinase up?regulated in atherothrombotic and inflammatory conditions, affects platelet aggregation and thrombus formation. Results: We demonstrate that MMP?13 is able to bind to platelet receptors alphaIIbbeta3 (?IIb?3) and platelet glycoprotein (GP)VI. The interactions between MMP?13, GPVI and ?IIb?3 are sufficient to significantly inhibit washed platelet aggregation and decrease thrombus formation on fibrillar collagen. Conclusions: Our data demonstrate a role for MMP?13 in the inhibition of both platelet aggregation and thrombus formation in whole flowing blood, and may provide new avenues of research into the mechanisms underlying the subtle role of MMP?13 in atherothrombotic pathologies. Twit Text FOAVip MMP 13 binds to platelet receptors IIb 3 and GPVI and impairs aggregation and thrombus formation ????Res Pract Thromb Haemost http://www.kidney.de/pget.php?&tw=1&pmid=30046741 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=30046741 #FOAvip English Wikipedia <ref>{{Cite pmid|30046741}}</ref> MMP?13 binds to platelet receptors ?IIb?3 and GPVI and impairs aggregation and thrombus formation #MMPMID30046741 Howes J; Pugh N; Hamaia SW; Jung SM; Knäuper V; Malcor J; Farndale RW Res Pract Thromb Haemost 2018[Apr]; 2 (2): 370-9 PMID30046741show ga Essentials: MMP?13 has the potential to influence platelet function and thrombus formation directly.We sought to elucidate whether MMP?13 is able to bind to specific platelet receptors.MMP?13 is able to bind to platelet alphaIIbbeta3 (?IIb?3) and glycoprotein (GP)VI.These interactions are sufficient to inhibit platelet aggregation and thrombus formation. Background: Acute thrombotic syndromes lead to atherosclerotic plaque rupture with subsequent thrombus formation, myocardial infarction and stroke. Following rupture, flowing blood is exposed to plaque components, including collagen, which triggers platelet activation and aggregation. However, plaque rupture releases other components into the surrounding vessel which have the potential to influence platelet function and thrombus formation. Objectives: Here we sought to elucidate whether matrix metalloproteinase?13 (MMP?13), a collagenolytic metalloproteinase up?regulated in atherothrombotic and inflammatory conditions, affects platelet aggregation and thrombus formation. Results: We demonstrate that MMP?13 is able to bind to platelet receptors alphaIIbbeta3 (?IIb?3) and platelet glycoprotein (GP)VI. The interactions between MMP?13, GPVI and ?IIb?3 are sufficient to significantly inhibit washed platelet aggregation and decrease thrombus formation on fibrillar collagen. Conclusions: Our data demonstrate a role for MMP?13 in the inhibition of both platelet aggregation and thrombus formation in whole flowing blood, and may provide new avenues of research into the mechanisms underlying the subtle role of MMP?13 in atherothrombotic pathologies. äMMP?13 binds to platelet receptors ?IIb?3 and GPVI and impairs aggrega(epmc).pdf DeepDyve Pubget Overpricing