1,012
Views
31
CrossRef citations to date
0
Altmetric
HEMOSTASIS AND THROMBOSIS

Hydroxyl radical-modified fibrinogen as a marker of thrombosis: the role of iron

&
Pages 241-247 | Published online: 18 Jul 2013

References

  • Kruszewski M. Labile iron pool: the main determinant of cellular response to oxidative stress. Mutat Res. 2003;531:81–92.
  • Lipinski B. Hydroxyl radical and its scavengers in health and disease. Oxid Med Cell Longev. 2011;2011:809696.
  • Lee DW, Andersen JK. Iron elevation in the aging Parkinsonian brain: a consequence of impaired iron homeostasis? J Neurochem. 2010;112:332–9.
  • Thomas C, Mackey MM, Diaz AA, Cox DP. Hydroxyl radical is produced via the Fenton reaction in submitochondrial particles under oxidative stress: implications for diseases associated with iron accumulation. Redox Rep. 2009;14:102–8.
  • Weinberg EB. The hazards of iron loading. Metallomics. 2010;2:732–40.
  • Reeder BJ, Svistunenko DA, Cooper CE, Wilson MT. The radical and redox chemistry of myoglobin and hemoglobin: from in vitro studies to human pathology. Antioxid Redox Signal. 2004;6:954–66.
  • Balla J, Vercellotti GM, Jeney V, Yachie A, Varga Z, Jacob HS, et al.. Heme, heme oxygenase, and ferritin: how the vascular endothelium survives and dies in an iron-rich environment. Antioxid Redox Signal. 2007;9:2119–37.
  • Andersen JK. Iron elevations in the aging Parkinsonian brain: a consequence of impaired iron homeostasis? J Neurochem. 2010;112:332–9.
  • Ahluwalia N, Genoux A, Ferrieres J, Perret B, Carayol M, Drouet L, et al.. Iron status is associated with carotid atherosclerotic plaques in middle-aged adults. J Nutr. 2010;140:812–6.
  • Brissot P, Ropert M, Lan LeC, Loreal O. Nontransferrin bound iron: A key role in iron overload and iron toxicity. Biochim Biophys Acta. 2012;1820:403–10.
  • Kell DB. Towards a unifying, system biology understanding of large-scale cellular death and destruction caused by poorly liganded iron: Parkinson’s, Huntington’s, Alzheimer’s, prions, bactercides, chemical toxicology and others as example. Arch Toxicol. 2010;84:825–89.
  • Yuan XM, Li W. The iron hypothesis of atherosclerosis and its clinical impact. Ann Med. 2003;35:578–91.
  • Aigner E, Aigner E, Hinz C, Steiner K, Rossmann B, Pfleger J, et al.. Iron stores, liver transaminase levels and metabolic risk in healthy teenagers. Eur J Clin Invest. 2010;40:155–63.
  • Franchini M, Targher G, Mntagnana M, Lippi G. Iron and thrombosis. Ann Hematol. 2008;87:167–73.
  • Kruszewski M. The role of labile iron pool in cardiovascular diseases. Acta Biochim Pol. 2004;51:471–80.
  • Marx G, Chevion M. Fibrinogen coagulation without thrombin: reaction with vitamin C and copperII. Thromb Res. 1985;40:11–8.
  • Manevich Y, Held KD, Biaglow JE. Coumarin-3-carboxylic acid as a detector for hydroxyl radicals generated chemically and by gamma radiation. Radiat Res. 1997;148:580–91.
  • Pretorius E, Oberholzer HM, van der Spuy WJ, Meiring JH. Age-related changes in fibrin networks and platelets of individuals over 75: a scanning electron microscopy study showing ‘thrombotic preparedness’. J Thromb Thrombolysis. 2010;29:271–5.
  • Yang X, Chasteen ND. Ferroxidase activity of ferritin: effects of pH, buffer and Fe(II) and Fe(III) concentrations on Fe(II) autoxidation and ferroxidation. Biochem J. 1999;338:615–8.
  • Alayash AI, Patel RP, Cashon RE. Redox reactions of hemoglobin and myoglobin: biological and toxicological implications. Antioxid Redox Sign. 2001;3:313–27.
  • Woollar KJ, Sturgeon S, Chin-Dusting JP, Salem HH, Jackson SP. Erythrocyte hemolysis and hemoglobin oxidation promote ferric chloride-induced vascular injury. J Biol Chem. 2009;284:13110–8.
  • Wang X, Xu L. An optimized murine model of ferric chloride-induced arterial thrombosis for thrombosis research. Thromb Res. 2005;115:95–100.
  • Alayash AI, Patel RP, Cashon RE. Redox reaction of hemoglobin and myoglobin: biological and toxicological implications. Antioxid Redox Sign. 2001;3:313–27.
  • Puppo A, Halliwell B. Formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Is hemoglobin a biological Fenton reagent? Biochem J. 1988;249:185–90.
  • Dyke VanBR, Saltman P. Hemoglobin: a mechanism of the generation of hydroxyl radicals. Free Radic Biol Med. 1996;20:985–9.
  • Belcher JD, Beckman JD, Balla G, Balla J, Vercellotti G. Heme degradation and vascular injury. Antioxid Redox Signal. 2010;12:233–48.
  • Kato GJ, Taylor JG. Pleiotropic effects of intravascular haemolysis on vascular homeostasis. Br J Haematol. 2010;148:690–701.
  • Rother RP, Bell L, Hillmen P, Gladwin MT. The clinical sequelae of intravascular hemolysis and extracellular plasma hemoglobin: a novel mechanism of human disease. JAMA. 2006;293:1653–62.
  • Shah SV, Rajapurkar MM. The role of labile iron in kidney diseases and treatment with chelation. Hemoglobin. 2009;33:378–85.
  • Jomova K, Vondrakova D, Lawson M, Valko M. Metals, oxidative stress and neurodegenerative disorders. Mol Cell Biochem. 2010;345:91–104.
  • Salonen JT, Nyyssonen K, Korpela H, Tuomilehto J, Seppanen R, Salonen R. High stored iron levels are associated with excess risk of myocardial infarction in eastern Finnish men. Circulation. 1992;86:803–11.
  • Nagy E, Eaton JW, Jeney V, Soares MP, Varga Z, Galajda Z, et al.. Red cells, hemoglobin, heme, iron, and atherogenesis. Arterioscler Thromb Vasc Biol. 2010;30:1347–53.
  • Brewer GJ. Risk of copper and iron toxicity during aging in humans. Chem Res Toxicol. 2010;23:319–26.
  • Muckenthaler MU. Iron toxicity in diseases of aging: Alzheimer’s disease, Parkinson’s disease and atherosclerosis. J Alzheimers Dis. 2009;16:879–95.
  • Morkedal B, Laugsand LE, Romundstad PR, Vatten LJ. Mortality from ischaemic heart disease: sex-specific effects of transferrin saturation, serum iron, and total iron binding capacity. The HUNT study. Eur J Cardiovasc Prev Rehabil. 2011;18:687–94.
  • Prior RL, Wu X. Anthocyanins: structural characteristics that result in unique metabolic patterns and biological activities. Free Radic Res. 2006;40:1014–28.
  • Ferrara DE, Taylor WR. Iron chelation and vascular function. In search of the mechanisms. Arterioscler Thromb Vasc Biol. 2005;25:2235–40.
  • Matthews AJ, Vercellotti GM, Menchaca HJ, Bloch PH, Michalek VN, Marker PH, et al.. Iron and atherosclerosis: inhibition by the iron chelator deferiprone L(1). J Surg Res. 1997;73:35–40.
  • Capellini MD, Taher A. Deferasirox (Exjade) for the treatment of iron overload. Acata Hematol. 2009;122:165–72.
  • Leys D, Deplanque D. Thrombolysis beyond the three-hour time window. Clin Exp Hypertens. 2006;28:313–6.
  • Lipinski B. Modification of fibrin structure as a possible cause of thrombolytic resistance. J Thromb Thrombolysis. 2010;29:296–8.
  • Robinson SR, Dang TN, Dringen R, Bishop GM. Hemin toxicity: a preventable source of brain damage following hemorrhagic stroke. Redox Rep. 2009;14:228–35.
  • Eckly A, Hechler B, Freund M, Zerr M, Cazevane JP, Lanza F, et al.. Mechanism underlying Fe(Cl3)-induced arterial thrombosis. J Thromb Haemost. 2011;9:779–89.
  • Lipinski B, Nowak A, Gurewich V. The organ distribution of I-125-fibrin in the generalized Shwartzman reaction and its relation to leukocytes. Br J Haematol. 1974;28:221–31.
  • Li L, Frei B. Prolonged exposure to lipopolysaccharide increases iron, heme, and p22 levels and NADPH oxidase activity in human aortic endothelial cells: inhibition by desferrioxamine. Arterioscl Thromb Vasc Biol. 2009;29:732–8.
  • Lins L, Brausseur R. The hydrophobic effect in protein folding. FASEB J. 1995;9:535–40.
  • van Oss CJ. Long-range and short-range mechanisms of hydrophobic attraction and hydrophilic repulsion in specific and aspecific interactions. J Mol Recognit. 2003;16:177–90.
  • Lipinski B, Sajdel-Sulkowska EM. New insight into Alzheimer’s disease: demonstration of (fibrinogen)-serum albumin insoluble deposits in brain tissue. Alzheimer Dis Assoc Disord. 2006;20:324–6.
  • Kim YM, Chung SI, Lee SY. Roles of plasma proteins in the formation of silicotic nodules in rats. Toxicol Lett. 2005;158:1–9.
  • Wasiutynski A, Wiczynski GM, Morton M. Fibrinogen/fibrin and albumin colocalize on the surface of placental villi a novel element of feto-maternal barrier. Ann Diagn Paediatr Pathol. 2002;6:125–9.
  • Lipinski B, Wegrzynowicz Z, Budzynski AZ, Kopec M, Latallo ZS, Kowalski E. Soluble unclottable complexes formed in the presence of fibrinogen degradation products (FDP) during the fibrinogen-fibrin conversion and their potential significance in pathology. Thromb Diath Haemorrh. 1967;17:65–9.
  • Lipinski B, Worowski K. Detection of soluble fibrin monomer complexes in blood by means of protamine sulphate test. Thromb Diathes Haemorrh. 1968;20:44–9
  • Lipinski NowakB, Drzewiecki J. Levels of soluble fibrin monomer complexes level in the course of myocardial infarction. Br Heart J. 1972;34:593–6.
  • Lipinski B, Gurewich V. Non-clottable, protamine sulfate precipitable protein of blood. Studies on its in vitro generation and incorporation into the fibrin clot. Thromb Res. 1972;1:569–72.
  • Andrews BA, Schmidt AS, Asenjo JA. Correlation for the partition behavior of proteins in aqueous two-phase systems: Effects of surface hydrophobicity and charge. Biotechnol Bioeng. 2005;90:380–90.
  • Lipinski B, Federman SM, Krolewski AS. Plasma macromolecular protein complex: Interaction with fibrin and fibrinolysis. Thromb Res. 1995;78:461–5.
  • Witko-Sarsat V, Friedlander M. Capeillere-Blandidn C, Nguyen AT, Canteloup S, Dayer JM, et al. Advanced oxidation protein products as a novel marker of oxidative stress in uremia. Kidney Int. 1996;49:1304–13.
  • Lipinski B, Pretorius E, Oberholzer HM, van der Spuy WJ. Interaction of fibrin with red blood cells: the role of iron. Ultrastruct Pathol. In press.
  • Undas A, Szuldrzynski K, Stepien E, Zalewski J, Godlewski J, Tracz W, et al.. Reduced clot permeability and susceptibility to lysis in patients with acute coronary syndrome: effects of inflammation and oxidative stress. Athertosclerosis. 2008;196:551–7.
  • Stoclet JC, Chataigneau T, Ndiaye TM, Oak MH, Bedoui EI, Chataigneau M, et al.. Vascular protection by dietary polyphenols. Eur J Pharmacol. 2004;500:299–313.
  • Mladenka P, Zatloukalova L, Filipsky T, Hrdina R. Cardiovascular effects of flavonoids are not caused only by direct antioxidant activity. Free Radic Biol Med. 2010;49:963–75.
  • Jomova K, Valko M. Importance of iron chelation in free radical-induced oxidative stress and human disease. Curr Pharm Des. 2011;17:3460–73.
  • Philpott M, Lim CC, Ferguson LR. Dietary protection against free radicals: a case for multiple testing to establish structure-activity relationships for antioxidant potential of anthocyanic plant species. Int J Mol Sci. 2009;10:1081–110.
  • Visavadiya NP, Soni B, Dalwadi N. Free radical scavenging and antiatherogenic activities of Sesamum indicum seed extracts in chemical and biological model systems. Food Chem Toxicol. 2009;47:2507–15.
  • Yadav AS, Bhatnagar D. Free radical scavenging activity, metal chelation and antioxidant power of some of the Indian spices. Biofactors. 2007;31:219–27.
  • Bengmark S, Mesa MD, Gil A. Plant-derived health: the effects of turmeric and curcuminoids. Nutr Hosp. 2009;24:273–81.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.