Influence of homocysteine on fibrin network lysis

Lauricella, Ana María; Quintana, Irene; Castañon, Mercedes; Sassetti, Beatriz; Kordich, L

doi:10.1097/01.mbc.0000220238.99843.45

Cited by 32 publications

(21 citation statements)

References 30 publications

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“…Homocysteine has also been indicated to have direct effects on fibrin network structure. When fibrin networks were formed from plasma that was incubated with homocysteine, the fibrin network became more compact and more resistant to lysis [48,49]. Black South Africans have been shown to be protected by genetically low levels of homocysteine due its effective metabolism [4].…”

Section: Fibrin Network Structurementioning

confidence: 99%

Nutrition and hemostasis: A focus on urbanization in South Africa

Pieters

Vorster

2008

Molecular Nutrition Food Res

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South Africa is experiencing a rapid urbanization of its African population characterized by a demographic, nutrition, lifestyle, and health transition. The resultant high prevalence of high cardiovascular disease, in particular of stroke, is of concern. In this narrative review it is suggested that, together with hypertension, changes in the hemostatic system may be one of the major contributors to stroke in this population. It is further suggested that these changes are related to increased fat and animal protein intakes, decreased intakes of total carbohydrate and dietary fiber, as well as persistent suboptimal micronutrient intakes of Africans in transition. The effects of this nutrition transition on plasma fibrinogen, fibrin network structures, plasminogen activator inhibitor 1 activity levels and some other clotting and fibrinolytic factors are discussed. It is concluded that despite indications of present protective mechanisms against the development of coronary heart disease (CHD) in this population the observed changes in diet and hemostatic profiles may eventually lead to a high prevalence of both stroke and CHD in urban black South Africans. It is further suggested that timely nutritional interventions and research of effects thereof on the hemostatic system are urgently needed.

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Section: Fibrin Network Structurementioning

confidence: 99%

Nutrition and hemostasis: A focus on urbanization in South Africa

Pieters

Vorster

2008

Molecular Nutrition Food Res

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“…Coagulation factor Va is also S-homocysteinylated (Undas et al 2001) and this modification could play a role in the modulation of hemostasis process. Clots formed from human plasma incubated in vitro with Hcys (at the high concentration -3 mmol/l) have been more compact structure, with shorter and more frequently branched fibers, than those formed in the absence of Hcys (Lauricella et al 2002(Lauricella et al , 2006. Harpel et al (1992) observed that Hcys (< 8 µmol/l) enhances the binding of lipoprotein(a) to fibrin, and this results may suggest a biochemical relationship between thiol compound metabolism, thrombosis and atherogenesis.…”

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confidence: 93%

May modifications of human plasma proteins stimulated by homocysteine and its thiolactone induce changes of hemostatic function of plasma in vitro?

Olas¹,

Kołodziejczyk²,

Malinowska³

2010

gpb

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Abstract. Homocysteine (Hcys) may be implicated in different diseases, especially in cardiovascular illnesses. The most reactive form of Hcys is its cyclic thioester -homocysteine thiolactone (HTL), which is formed in plasma and represents up to 0.29% of plasma total Hcys. Recently, it has been observed that Hcys and HTL may modify plasma proteins, including albumin, hemoglobin or fibrinogen, but the role of this process is not yet well known. The aim of our study in vitro was to investigate the modifications of human plasma total proteins after incubation with the reduced form of Hcys in concentrations 10-100 µmol/l, and HTL in concentrations 1-0.1 µmol/l, which correspond to levels found in human plasma during hyperhomocysteinemia in vivo. The aim of our study was also to explain the effects of Hcys and HTL on coagulation activity of human plasma. We showed that in model system in vitro Hcys and HTL change the level of thiol, amino and carbonyl groups in plasma total proteins. Moreover, our studies reported that not only Hcys (10-100 µmol/l), but also HTL (at lower concentrations than Hcys) modulates the coagulation properties of human plasma.

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“…1 Variables known to influence fibrin clot structure include fibrinogen and thrombin concentrations, 1 pH, 2,3 ionic strength, 3 chloride ion concentration, 2 and presence of calcium ions. 4 A variety of molecules are reported to affect fibrin clot structure, including homocysteine, 5 decorin core protein, 6 heparins, 7,8 dextran, 9 and hydroxyethylstarch. 10 In this study, we demonstrate that inorganic polyphosphate (polyP) strongly modulates fibrin clot structure.…”

Section: Introductionmentioning

confidence: 99%

Polyphosphate enhances fibrin clot structure

Smith

Morrissey

2008

Blood

189

185

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Polyphosphate, a linear polymer of inorganic phosphate, is present in platelet dense granules and is secreted on platelet activation. We recently reported that polyphosphate is a potent hemostatic regulator, serving to activate the contact pathway of blood clotting and accelerate factor V activation. Because polyphosphate did not alter thrombin clotting times, it appeared to exert all its procoagulant actions upstream of thrombin. We now report that polyphosphate enhances fibrin clot structure in a calciumdependent manner. Fibrin clots formed in the presence of polyphosphate had up to 3-fold higher turbidity, had higher masslength ratios, and exhibited thicker fibers in scanning electron micrographs. The ability of polyphosphate to enhance fibrin clot turbidity was independent of factor XIIIa activity. When plasmin or a combination of plasminogen and tissue plasminogen activators were included in clotting reactions, fibrin clots formed in the presence of polyphosphate exhibited prolonged clot lysis times. Release of polyphosphate from activated platelets or infectious microorganisms may play an important role in modulating fibrin clot structure and increasing its resistance to fibrinolysis. Polyphosphate may also be useful in enhancing the structure of surgical fibrin sealants. (Blood. 2008;112: 2810-2816) IntroductionA fibrin clot is the final product of the blood clotting cascade. Thrombin catalyzes release of fibrinopeptide A from fibrinogen to create fibrin monomers, which then aggregate to protofibrils. Proteolytic release of fibrinopeptide B by thrombin permits lateral protofibril aggregation, resulting in a three-dimensional fibrin gel. Factor XIIIa, a transglutaminase activated by thrombin, covalently crosslinks these fibers to increase the strength and elasticity of the resulting clot. 1 Variables known to influence fibrin clot structure include fibrinogen and thrombin concentrations, 1 pH, 2,3 ionic strength, 3 chloride ion concentration, 2 and presence of calcium ions. 4 A variety of molecules are reported to affect fibrin clot structure, including homocysteine, 5 decorin core protein, 6 heparins, 7,8 dextran, 9 and hydroxyethylstarch. 10 In this study, we demonstrate that inorganic polyphosphate (polyP) strongly modulates fibrin clot structure.polyP is a negatively charged, linear polymer of phosphate units linked by high-energy phosphoanhydride bonds. polyP has a wide biologic distribution, 11 but its functions have been studied most extensively in prokaryotes and unicellular eukaryotes, in which high levels of polyP accumulate in organelles known as acidocalcisomes. In such organisms, polyP plays essential roles in stress responses and virulence. 12 Although polyP has been studied less extensively in mammalian cells, 13 it has been reported to induce apoptosis in plasma cells, 14 promote calcification in osteoblasts, 15 and block metastasis of melanoma cells in a mouse model. 16 It has also been proposed to serve as a regulatory factor in proliferative signaling pathways. 17 Dense granules of human...

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Influence of homocysteine on fibrin network lysis

Cited by 32 publications

References 30 publications

Nutrition and hemostasis: A focus on urbanization in South Africa

Nutrition and hemostasis: A focus on urbanization in South Africa

May modifications of human plasma proteins stimulated by homocysteine and its thiolactone induce changes of hemostatic function of plasma in vitro?

Polyphosphate enhances fibrin clot structure

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