Search engine for discovering works of Art, research articles, and books related to Art and Culture
ShareThis
Javascript must be enabled to continue!

Migfilin supports hemostasis and thrombosis through regulating platelet αIIbβ3 outside-in signaling.

View through CrossRef
Elucidating the regulation mechanism of integrin αIIbβ3 is key to understand platelet biology and thrombotic diseases. Previous in vitro studies have implicated a role of migfilin in the support of platelet αIIbβ3 activation, however, contribution of migfilin to thrombosis and hemostasis in vivo and a detailed mechanism of migfilin in platelets are not known. In this study, with migfilin deletion (migfilin-/-) mice, we report that migfilin is a pivotal positive regulator of hemostasis and thrombosis. Migfilin-/- mice showed a nearly doubled tail-bleeding time and a prolonged occlusion time in Fecl3-induced mesenteric arteriolar thrombosis. Migfilin deficiency impedes platelet thrombi formation on collagen surface and impairs platelet aggregation and dense-granule secretion. Supported by characteristic functional readings and phosphorylation status of distinctive signaling molecules in the bidirectional signaling processes of αIIbβ3, the functional defects of migfilin-/- platelets appear to be mechanistically associated with a compromised outside-in signaling, rather than inside-out signaling. A synthesized cell-permeable migfilin peptide harboring filamin A binding sequence rescued the defective function and phosphorylation of signaling molecules of migfilin-/- platelets. Finally, migfilin does not influence the binding of filamin A and β3 subunit of αIIbβ3 in resting platelets, but hampers the re-association of filamin A and β3 during the conduct of outside-in signaling, suggesting that migfilin functions through regulating the interaction dynamics of αIIbβ3 and filamin A in platelets. Our study enhances the current understanding of platelet integrin αIIbβ3-mediated outside-in signaling and proves that migfilin is an important regulator for platelet activation, hemostasis and thrombosis.
Title: Migfilin supports hemostasis and thrombosis through regulating platelet αIIbβ3 outside-in signaling.
Description:
Elucidating the regulation mechanism of integrin αIIbβ3 is key to understand platelet biology and thrombotic diseases.
Previous in vitro studies have implicated a role of migfilin in the support of platelet αIIbβ3 activation, however, contribution of migfilin to thrombosis and hemostasis in vivo and a detailed mechanism of migfilin in platelets are not known.
In this study, with migfilin deletion (migfilin-/-) mice, we report that migfilin is a pivotal positive regulator of hemostasis and thrombosis.
Migfilin-/- mice showed a nearly doubled tail-bleeding time and a prolonged occlusion time in Fecl3-induced mesenteric arteriolar thrombosis.
Migfilin deficiency impedes platelet thrombi formation on collagen surface and impairs platelet aggregation and dense-granule secretion.
Supported by characteristic functional readings and phosphorylation status of distinctive signaling molecules in the bidirectional signaling processes of αIIbβ3, the functional defects of migfilin-/- platelets appear to be mechanistically associated with a compromised outside-in signaling, rather than inside-out signaling.
A synthesized cell-permeable migfilin peptide harboring filamin A binding sequence rescued the defective function and phosphorylation of signaling molecules of migfilin-/- platelets.
Finally, migfilin does not influence the binding of filamin A and β3 subunit of αIIbβ3 in resting platelets, but hampers the re-association of filamin A and β3 during the conduct of outside-in signaling, suggesting that migfilin functions through regulating the interaction dynamics of αIIbβ3 and filamin A in platelets.
Our study enhances the current understanding of platelet integrin αIIbβ3-mediated outside-in signaling and proves that migfilin is an important regulator for platelet activation, hemostasis and thrombosis.

Related Results

Pro-inflammatory chemokines CCL5, CXCL12, and CX3CL1 bind to and activate platelet integrin αIIbβ3 in an allosteric manner
Pro-inflammatory chemokines CCL5, CXCL12, and CX3CL1 bind to and activate platelet integrin αIIbβ3 in an allosteric manner
AbstractPrevious studies showed that pro-inflammatory chemokines CX3CL1 and CXCL12 bound to the allosteric binding site (site 2) of integrins and allosterically activated integrins...
Autoimmune thrombocytopenic purpura
Autoimmune thrombocytopenic purpura
Adult autoimmune throbocytopenic purpura (ATP) is a platelet disorder that develops in certain individuals with a genetic as well as sex (female) predisposition following an enviro...
Autoimmune thrombocytopenic purpura
Autoimmune thrombocytopenic purpura
Abstract Adult autoimmune throbocytopenic purpura (ATP) is a platelet disorder that develops in certain individuals with a genetic as well as sex (female) predisposi...
Association of Genetic Variability in Selected Genes with Platelet Hyperaggregability and Arterial Thrombosis
Association of Genetic Variability in Selected Genes with Platelet Hyperaggregability and Arterial Thrombosis
Abstract Introduction: Inherited platelet hyperaggregability, so called “Sticky platelet syndrome” (SPS), is a prothrombotic platelet disorder. Th...
Platelet Antagonists
Platelet Antagonists
Platelet antagonists play an important role in both primary and secondary prevention of atherothrombotic events. Despite their proven benefit, individual response (and protection) ...
Risk Factors for Umbilical Venous Catheter-Associated Thrombosis in Very Low Birth Weight Infants.
Risk Factors for Umbilical Venous Catheter-Associated Thrombosis in Very Low Birth Weight Infants.
Abstract Background: Thrombosis in neonates is a rare but serious occurrence that is usually associated with central catheterization. Among acquired risk factors, th...
Platelet and Red Blood Cell Indices in Harris Platelet Syndrome.
Platelet and Red Blood Cell Indices in Harris Platelet Syndrome.
Abstract Inherited giant platelet disorders are a group of rare disorders characterized by thrombocytopenia, giant platelets and variable bleeding symptoms. Naina et...
A plant surface protein sharing structural properties with animal integrins
A plant surface protein sharing structural properties with animal integrins
Using a polyclonal antibody (P23) generated against the human platelet integrin αIIbβ3 and a FITC‐conjugate secondary antibody, fluorescence is observed at the surface of protoplas...

Back to Top