Crosslinking of von Willebrand factor to fibrin by factor XIII (2)

Hada, Masao; McDonagh, Jan

doi:10.2491/jjsth1970.15.586

Cited by 12 publications

(18 citation statements)

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“…The main substrate capable of binding VWF is collagen, 36 particularly types I and III in deeper layers of the vessel wall and microfibrillar collagen type VI in the subendothelial matrix, 30,[37][38][39] with heparin, sulfatides, and fibrin providing additional interaction sites (see the online data supplement). Two of the 3 type A domains in VWF, A1 and A3, can mediate binding to collagens, and their respective roles may vary depending on the type of collagen involved and the fluid dynamic conditions.…”

Section: Initial Platelet Adhesion To Thrombogenic Surfaces Substratementioning

confidence: 99%

“…Different types of collagen (particularly I, III, and VI) are thought to be among the most active vessel wall components in the initiation of platelet adhesion and aggregation, 36 but the relevance of their contribution to hemostasis and thrombosis relative to other extracellular matrix molecules remains to be defined. The conformation of different collagens may influence the mechanisms of interaction with platelets under flow and subsequent activation, which is a relevant factor in the interpretation of experimental results.…”

Section: Platelet Adhesion To Collagenmentioning

confidence: 99%

“…The conformation of different collagens may influence the mechanisms of interaction with platelets under flow and subsequent activation, which is a relevant factor in the interpretation of experimental results. 74 Acid-insoluble fibers display a characteristic banded pattern attributable to the regular staggering of collagen monomers, 36,75 whereas pepsin-solubilized microfibrils lack this pattern and form spiral structures ( Figure 4). 74 Spiraled collagen formed by fibrils in helical assembly has been found in both normal and pathological vascular tissues, and may result from the degradation of fibers by matrix metalloproteinases, particularly matrix metalloproteinase 1.…”

Section: Platelet Adhesion To Collagenmentioning

confidence: 99%

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Adhesion Mechanisms in Platelet Function

Ruggeri¹,

Mendolicchio²

2007

Circulation Research

642

514

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Abstract-Platelet adhesion is an essential function in response to vascular injury and is generally viewed as the first step during which single platelets bind through specific membrane receptors to cellular and extracellular matrix constituents of the vessel wall and tissues. This response initiates thrombus formation that arrests hemorrhage and permits wound healing. Pathological conditions that cause vascular alterations and blood flow disturbances may turn this beneficial process into a disease mechanism that results in arterial occlusion, most frequently in atherosclerotic vessels of the heart and brain. Besides their relevant role in hemostasis and thrombosis, platelet adhesive properties are central to a variety of pathophysiological processes that extend from inflammation to immune-mediated host defense and pathogenic mechanisms as well as cancer metastasis. All of these activities depend on the ability of platelets to circulate in blood as sentinels of vascular integrity, adhere where alterations are detected, and signal the abnormality to other platelets and blood cells. In this respect, therefore, platelet adhesion to vascular wall structures, to one another (aggregation), or to other blood cells, represent different aspects of the same fundamental biological process. Detailed studies by many investigators over the past several years have been aimed to dissect the complexity of these functions, and the results obtained now permit an attempt to integrate all the available information into a picture that highlights the balanced diversity and synergy of distinct platelet adhesive interactions. (Circ Res. 2007;100:1673-1685.)Key Words: adhesion molecules Ⅲ platelets Ⅲ vascular biology Ⅲ extracellular matrix Ⅲ collagen P latelets in mammals are anucleated cells that originate from the cytoplasm of bone marrow megakaryocytes 1 and circulate in blood as sentinels of vascular integrity. They show no interaction with the inner surface of normal vessels but adhere promptly where endothelial cells are altered or extracellular matrix substrates are exposed. 2 This is a critical initial step in hemostasis and thrombosis, as well as in inflammatory 3,4 and immunopathogenic responses. 5 The functions of mammalian platelets are conserved throughout evolution and closely reflect those of nucleated thrombocytes in all other vertebrates. 6 -9 After adhering to vascular lesions, platelets can rapidly recruit to the site of injury additional platelets, which are necessary to achieve hemostasis, or different types of leukocytes, which set off host defense responses. Such selective recruitment is orchestrated by activation pathways stimulated by the initial adhesive interactions and by soluble agonists released or generated locally, which lead to the appearance on the platelet membrane of different adhesive molecules capable of attracting distinct circulating cells. Platelet adhesion in a broad sense is the Original received January 2, 2007; revision received March 13, 2007; accepted April 11, 2007 study of the adhesive p...

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Section: Initial Platelet Adhesion To Thrombogenic Surfaces Substratementioning

confidence: 99%

Section: Platelet Adhesion To Collagenmentioning

confidence: 99%

Section: Platelet Adhesion To Collagenmentioning

confidence: 99%

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Adhesion Mechanisms in Platelet Function

Ruggeri¹,

Mendolicchio²

2007

Circulation Research

642

514

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“…It is well accepted that under conditions of high shear stress VWF plays a critical role in the recruitment of circulating platelets to the fibrin network. 3,15 The initial evidence indicating that VWF binds to fibrin from a plasma milieu was provided by Hada et al 16 Those investigators demonstrated that factor XIIIa mediated the cross-linking between fibrin and VWF. In contrast, Loscalzo et al 17 demonstrated that VWF interacts noncovalently with immobilized fibrin monomers.…”

Section: Introductionmentioning

confidence: 99%

Von Willebrand factor C1C2 domain is involved in platelet adhesion to polymerized fibrin at high shear rate

Keuren

Baruch

Legendre

et al. 2004

Blood

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Fibrin is actively involved in platelet reactions essential for thrombus growth, in which von Willebrand factor (VWF) might be an important mediator. The aim of this study was to localize VWF domains that bind to fibrin and to determine their relevance in platelet adhesion. VWF binds specifically to fibrin with an apparent K d of 2.2 g/mL. Competition in the presence of 2 complementary fragments, SpIII (residues 1-1365) and SpII (residues 1366-2050), indicated that the high affinity binding site for fibrin is located in the Cterminal part, thus distinct from the A domains. Comparison of 2 deleted rVWF (⌬D4B-rVWF, ⌬C1C2-rVWF) suggested that the C1C2 domains contained a fibrin binding site. This site is distinct from RGD, as shown by binding of D1746G-rVWF to fibrin. Perfusion studies at high shear rate demonstrated that C1C2 domains were required for optimal platelet adhesion to fibrin. With the use of a VWF-deficient mouse model, it was found that plasma VWF is critical for platelet tethering and adhesion to fibrin. These results suggest a dual role of fibrinbound VWF in thrombus formation: first, fibrin-bound VWF is critical in the recruitment of platelets by way of glycoprotein (GP) Ib, and, second, it contributes to stationary platelet adhesion by way of binding to activated ␣ IntroductionThe process of hemostasis and pathologic thrombus formation at an injured vessel wall is initiated when platelets are captured from flowing blood by way of a rapid bond formation between their glycoprotein (GP) Ib receptor and von Willebrand factor (VWF) immobilized on collagen. Platelets subsequently roll over the damaged area prior to irreversible binding through integrin ␣ IIb ␤ 3 . 1-3 GP Ib and ␣ IIb ␤ 3 binding sites on VWF are localized on the A1 and C1 domain, respectively. [4][5][6][7][8] Immobilized VWF present on the platelet membranes then serves for further platelet recruitment and thrombus growth. 9 In parallel with the platelet adhesion process, coagulation is initiated through release of tissue factor from the damaged vessel wall. 10 Propagation of blood coagulation occurs by localized enzymatic complexes assembled on the plasma membrane of adherent platelets that expose negatively charged phospholipids (reviewed in Heemskerk et al 11 ). The thrombin thus formed further activates platelets and stabilizes the growing thrombus by the formation of fibrin. Previous work from our laboratory 12,13 and others 14 suggests that in addition to its nonspecific trapping of platelets, fibrin could be actively involved in regulating thrombus growth. It is well accepted that under conditions of high shear stress VWF plays a critical role in the recruitment of circulating platelets to the fibrin network. 3,15 The initial evidence indicating that VWF binds to fibrin from a plasma milieu was provided by Hada et al. 16 Those investigators demonstrated that factor XIIIa mediated the cross-linking between fibrin and VWF. In contrast, Loscalzo et al 17 demonstrated that VWF interacts noncovalently with immobilized fibrin monomers...

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“…1,2 The mature proenzyme circulates as a tetramer consisting of 2 A-subunits containing the active site and 2 B-subunits serving as carriers of the A-subunits in plasma. In addition to introducing peptide bonds between aligned fibrin ␣-and ␥-chains, FXIII incorporates ␣ 2 -antiplasmin, 3,4 von Willebrand factor, 5 thrombospondin, 6 and fibronectin 7,8 into the fibrin network. Through these crosslinking reactions, the mechanical, chemical, and proteolytic vulnerability of the fibrin clot is decreased by FXIII.…”

mentioning

confidence: 99%

Subunit Antigen and Activity Levels of Blood Coagulation Factor XIII in Healthy Individuals

Ariëns

Köhler

Mansfield

et al. 1999

ATVB

120

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Abstract-Factor (F) XIII covalently cross-links and stabilizes the fibrin-clot. Recent evidence suggests a role for FXIII in atherothrombotic diseases, but no information is available regarding the association of FXIII with common risk factors. The aim of this study was to investigate the relationship of FXIII with age, sex, smoking, and hypertension. Plasma levels of FXIII A-subunit antigen, FXIII B-subunit antigen, and FXIII cross-linking activity were measured in 612 healthy individuals (250 men and 362 women). FXIII A-and B-subunit levels were correlated significantly with age in both men (rϭ0.21, Pϭ0.001, and rϭ0.17, Pϭ0.008, respectively) and women (rϭ0.20, PϽ0.0005, and rϭ0.13, Pϭ0.011, respectively Key Words: factor XIII Ⅲ sex Ⅲ age Ⅲ smoking Ⅲ hypertension T he transglutaminase blood coagulation factor XIII (FXIII) covalently cross-links and therefore stabilizes the fibrin clot, which initially is held together solely by electrostatic interactions. 1,2 The mature proenzyme circulates as a tetramer consisting of 2 A-subunits containing the active site and 2 B-subunits serving as carriers of the A-subunits in plasma. In addition to introducing peptide bonds between aligned fibrin ␣-and ␥-chains, FXIII incorporates ␣ 2 -antiplasmin, 3,4 von Willebrand factor, 5 thrombospondin, 6 and fibronectin 7,8 into the fibrin network. Through these crosslinking reactions, the mechanical, chemical, and proteolytic vulnerability of the fibrin clot is decreased by FXIII. Because a deficiency of FXIII leads to severe bleeding, the critical role of FXIII in blood clotting has long been acknowledged. The involvement of FXIII in thrombotic disease is instead starting to emerge only now. It has been shown that FXIII levels were increased in non-insulin-dependent diabetic patients with microangiopathy and macroangiopathy 9 and in patients with obliterative atherosclerosis of the lower limbs. 10 Increased cross-linking of fibrin ␥-chains has been found in patients with acute myocardial infarction. 11 In addition, plasma samples from men with myocardial infarction at a young age formed fibrin gel structures that were more tight and rigid than did plasma samples from normal subjects. 12 Recently, we have shown that a common genetic polymorphism in the FXIII A-subunit, coding for a substitution of valine with leucine at residue 34, is protective against myocardial infarction. 13 These studies suggest that FXIII may be a risk factor for the development of atherothrombotic disorders. To date, there is no information available regarding the relation of FXIII with other known risk factors of cardiovascular disease, such as age and smoking. The aim of the present study was to investigate the influence of sex, age, smoking, and hypertension on FXIII activity and subunit antigen levels in a population of healthy individuals. Methods SubjectsPlasma samples were obtained from 612 healthy, white northern Europeans, 250 men and 362 women, aged between 22 and 93 years.

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Crosslinking of von Willebrand factor to fibrin by factor XIII (2)

Cited by 12 publications

References 3 publications

Adhesion Mechanisms in Platelet Function

Adhesion Mechanisms in Platelet Function

Von Willebrand factor C1C2 domain is involved in platelet adhesion to polymerized fibrin at high shear rate

Subunit Antigen and Activity Levels of Blood Coagulation Factor XIII in Healthy Individuals

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