User login
Image by Andre E.X. Brown
Preclinical research helps explain how the protein lysyl oxidase (LOX) enhances platelet activation and thrombosis.
Previous studies showed that LOX is overexpressed in pathologies associated with thrombosis, including myeloproliferative neoplasms.
However, it wasn’t clear exactly how LOX leads to thrombosis.
So Shinobu Matsuuras, PhD, of Boston University School of Medicine in Massachusetts, and her colleagues attempted to find out.
The team reported their findings in Blood.
The researchers wanted to determine the role of LOX in thrombosis and platelet function without the compounding influences of other pathologies.
So they generated mice that expressed LOX in wild-type megakaryocytes and platelets—Pf4-Loxtg/tg mice.
These mice had the same number of platelets as control mice, but the platelets in Pf4-Loxtg/tg mice were more likely than normal platelets to form a thrombus.
The time to vessel occlusion after endothelial injury was significantly shorter in Pf4-Loxtg/tg mice than control mice. The average time to occlusion was about 35% shorter in Pf4-Loxtg/tg mice.
The reason for this, according to the researchers’ experiments, is that platelets from Pf4-Loxtg/tg mice adhere better to collagen and have a greater aggregation response to lower doses of collagen.
The researchers were also able to pinpoint the receptor on the platelets that was affected by the oxidation activity of LOX—integrin α2β1.
The team said this is the first study to show that LOX expression enhances platelet adhesion to collagen through integrin α2β1.
And the results suggest LOX could be a target for antithrombotic therapy in myeloproliferative neoplasms and other pathologies associated with LOX overexpression. 
Image by Andre E.X. Brown
Preclinical research helps explain how the protein lysyl oxidase (LOX) enhances platelet activation and thrombosis.
Previous studies showed that LOX is overexpressed in pathologies associated with thrombosis, including myeloproliferative neoplasms.
However, it wasn’t clear exactly how LOX leads to thrombosis.
So Shinobu Matsuuras, PhD, of Boston University School of Medicine in Massachusetts, and her colleagues attempted to find out.
The team reported their findings in Blood.
The researchers wanted to determine the role of LOX in thrombosis and platelet function without the compounding influences of other pathologies.
So they generated mice that expressed LOX in wild-type megakaryocytes and platelets—Pf4-Loxtg/tg mice.
These mice had the same number of platelets as control mice, but the platelets in Pf4-Loxtg/tg mice were more likely than normal platelets to form a thrombus.
The time to vessel occlusion after endothelial injury was significantly shorter in Pf4-Loxtg/tg mice than control mice. The average time to occlusion was about 35% shorter in Pf4-Loxtg/tg mice.
The reason for this, according to the researchers’ experiments, is that platelets from Pf4-Loxtg/tg mice adhere better to collagen and have a greater aggregation response to lower doses of collagen.
The researchers were also able to pinpoint the receptor on the platelets that was affected by the oxidation activity of LOX—integrin α2β1.
The team said this is the first study to show that LOX expression enhances platelet adhesion to collagen through integrin α2β1.
And the results suggest LOX could be a target for antithrombotic therapy in myeloproliferative neoplasms and other pathologies associated with LOX overexpression.
Image by Andre E.X. Brown
Preclinical research helps explain how the protein lysyl oxidase (LOX) enhances platelet activation and thrombosis.
Previous studies showed that LOX is overexpressed in pathologies associated with thrombosis, including myeloproliferative neoplasms.
However, it wasn’t clear exactly how LOX leads to thrombosis.
So Shinobu Matsuuras, PhD, of Boston University School of Medicine in Massachusetts, and her colleagues attempted to find out.
The team reported their findings in Blood.
The researchers wanted to determine the role of LOX in thrombosis and platelet function without the compounding influences of other pathologies.
So they generated mice that expressed LOX in wild-type megakaryocytes and platelets—Pf4-Loxtg/tg mice.
These mice had the same number of platelets as control mice, but the platelets in Pf4-Loxtg/tg mice were more likely than normal platelets to form a thrombus.
The time to vessel occlusion after endothelial injury was significantly shorter in Pf4-Loxtg/tg mice than control mice. The average time to occlusion was about 35% shorter in Pf4-Loxtg/tg mice.
The reason for this, according to the researchers’ experiments, is that platelets from Pf4-Loxtg/tg mice adhere better to collagen and have a greater aggregation response to lower doses of collagen.
The researchers were also able to pinpoint the receptor on the platelets that was affected by the oxidation activity of LOX—integrin α2β1.
The team said this is the first study to show that LOX expression enhances platelet adhesion to collagen through integrin α2β1.
And the results suggest LOX could be a target for antithrombotic therapy in myeloproliferative neoplasms and other pathologies associated with LOX overexpression.