메뉴 건너뛰기




Volumn 25, Issue 8, 2014, Pages 845-850

Iron-enhanced coagulation is attenuated by chelation: A thrombelastographic and ultrastructural analysis

Author keywords

Coagulation; Electron microscopy; Iron; Thrombelastography

Indexed keywords

DEFEROXAMINE; FERRIC CHLORIDE; IRON; CHLORIDE; FERRIC ION; FIBRINOGEN; IRON CHELATING AGENT; TISSUE PLASMINOGEN ACTIVATOR;

EID: 84919735043     PISSN: 09575235     EISSN: 14735733     Source Type: Journal    
DOI: 10.1097/MBC.0000000000000160     Document Type: Article
Times cited : (31)

References (19)
  • 1
    • 84897442035 scopus 로고    scopus 로고
    • Serum ferritin is an important inflammatory disease marker, as it is mainly a leakage product from damaged cells
    • Kell DB, Pretorius E. Serum ferritin is an important inflammatory disease marker, as it is mainly a leakage product from damaged cells. Metallomics 2014;6:748-773. doi: 10.1039/c3mt00347g.
    • (2014) Metallomics , vol.6 , pp. 748-773
    • Kell, D.B.1    Pretorius, E.2
  • 2
    • 84859489238 scopus 로고    scopus 로고
    • Novel pathway of iron-induced blood coagulation: Implications for diabetes mellitus and its complications
    • Lipinski B, Pretorius E. Novel pathway of iron-induced blood coagulation: implications for diabetes mellitus and its complications. Pol Arch Med Wewn 2012;122:115-122.
    • (2012) Pol Arch Med Wewn , vol.122 , pp. 115-122
    • Lipinski, B.1    Pretorius, E.2
  • 3
    • 84865431617 scopus 로고    scopus 로고
    • Iron enhances generation of fibrin fibers in human blood: Implications for pathogenesis of stroke
    • Lipinski B, Pretorius E, Oberholzer HM, van der Spuy WJ. Iron enhances generation of fibrin fibers in human blood: implications for pathogenesis of stroke. Microsc Res Tech 2012;75:1185-1190.
    • (2012) Microsc Res Tech , vol.75 , pp. 1185-1190
    • Lipinski, B.1    Pretorius, E.2    Oberholzer, H.M.3    Van Der Spuy, W.J.4
  • 4
    • 84874390563 scopus 로고    scopus 로고
    • Novel use of scanning electron microscopy for detection of iron-induced morphological changes in human blood
    • Pretorius E, Vermeulen N, Bester J, Lipinski B. Novel use of scanning electron microscopy for detection of iron-induced morphological changes in human blood. Microsc Res Tech 2013;76:268-271.
    • (2013) Microsc Res Tech , vol.76 , pp. 268-271
    • Pretorius, E.1    Vermeulen, N.2    Bester, J.3    Lipinski, B.4
  • 5
    • 84880311179 scopus 로고    scopus 로고
    • Iron-induced fibrin in cardiovascular disease
    • Lipinski B, Pretorius E. Iron-induced fibrin in cardiovascular disease. Curr Neurovasc Res 2013;10:269-274.
    • (2013) Curr Neurovasc Res , vol.10 , pp. 269-274
    • Lipinski, B.1    Pretorius, E.2
  • 6
    • 84878514911 scopus 로고    scopus 로고
    • Differences in morphology of fibrin clots induced with thrombin and ferric ions and its pathophysiological consequences
    • Pretorius E, Lipinski B. Differences in morphology of fibrin clots induced with thrombin and ferric ions and its pathophysiological consequences. Heart Lung Circ 2013;22:447-449.
    • (2013) Heart Lung Circ , vol.22 , pp. 447-449
    • Pretorius, E.1    Lipinski, B.2
  • 8
    • 84863988965 scopus 로고    scopus 로고
    • Scanning electron microscopy of fibrin networks in rheumatoid arthritis: A qualitative analysis
    • Pretorius E, Oberholzer HM, van der Spuy WJ, Swanepoel AC, Soma P. Scanning electron microscopy of fibrin networks in rheumatoid arthritis: a qualitative analysis. Rheumatol Int 2012;32:1611-1615.
    • (2012) Rheumatol Int , vol.32 , pp. 1611-1615
    • Pretorius, E.1    Oberholzer, H.M.2    Van Der Spuy, W.J.3    Swanepoel, A.C.4    Soma, P.5
  • 9
    • 77957965529 scopus 로고    scopus 로고
    • Modification of fibrin structure as a possible cause of thrombolytic resistance
    • Lipinski B. Modification of fibrin structure as a possible cause of thrombolytic resistance. J Thromb Thrombolysis 2010;29:296-298.
    • (2010) J Thromb Thrombolysis , vol.29 , pp. 296-298
    • Lipinski, B.1
  • 10
    • 84866080059 scopus 로고    scopus 로고
    • Hydroxyl radical-modified fibrinogen as a marker of thrombosis: The role of iron
    • Lipinski B, Pretorius E. Hydroxyl radical-modified fibrinogen as a marker of thrombosis: the role of iron. Hematology 2012;17:241-247.
    • (2012) Hematology , vol.17 , pp. 241-247
    • Lipinski, B.1    Pretorius, E.2
  • 11
    • 84877038303 scopus 로고    scopus 로고
    • A novel method for assessing the role of iron and its functional chelation in fibrin fibril formation: The use of scanning electron microscopy
    • Pretorius E, Vermeulen N, Bester J, Lipinski B, Kell DB. A novel method for assessing the role of iron and its functional chelation in fibrin fibril formation: the use of scanning electron microscopy. Toxicol Mech Methods 2013;23:352-359.
    • (2013) Toxicol Mech Methods , vol.23 , pp. 352-359
    • Pretorius, E.1    Vermeulen, N.2    Bester, J.3    Lipinski, B.4    Kell, D.B.5
  • 12
    • 84897404263 scopus 로고    scopus 로고
    • Profound morphological changes in the erythrocytes and fibrin networks of patients with hemochromatosis or with hyperferritinemia, and their normalization by iron chelators and other agents
    • Pretorius E, Bester J, Vermeulen N, Lipinski B, Gericke GS, Kell DB. Profound morphological changes in the erythrocytes and fibrin networks of patients with hemochromatosis or with hyperferritinemia, and their normalization by iron chelators and other agents. PLoS One 2014;9:e85271.
    • (2014) PLoS One , vol.9 , pp. e85271
    • Pretorius, E.1    Bester, J.2    Vermeulen, N.3    Lipinski, B.4    Gericke, G.S.5    Kell, D.B.6
  • 13
    • 0028918335 scopus 로고
    • Oxidative modification of fibrinogen inhibits thrombin-catalyzed clot formation
    • Shacter E, Williams JA, Levine RL. Oxidative modification of fibrinogen inhibits thrombin-catalyzed clot formation. Free Radic Biol Med 1995;18:815-821.
    • (1995) Free Radic Biol Med , vol.18 , pp. 815-821
    • Shacter, E.1    Williams, J.A.2    Levine, R.L.3
  • 14
    • 84881507608 scopus 로고    scopus 로고
    • Functional impact of oxidative posttranslational modifications on fibrinogen and fibrin clots
    • Martinez M, Weisel JW, Ischiropoulos H. Functional impact of oxidative posttranslational modifications on fibrinogen and fibrin clots. Free Radic Biol Med 2013;65:411-418.
    • (2013) Free Radic Biol Med , vol.65 , pp. 411-418
    • Martinez, M.1    Weisel, J.W.2    Ischiropoulos, H.3
  • 15
    • 4344648152 scopus 로고    scopus 로고
    • Biomarkers of antioxidant capacity in the hydrophilic and lipophilic compartments of human plasma
    • Yeum KJ, Russell RM, Krinsky NI, Aldini G. Biomarkers of antioxidant capacity in the hydrophilic and lipophilic compartments of human plasma. Arch Biochem Biophys 2004;430:97-103.
    • (2004) Arch Biochem Biophys , vol.430 , pp. 97-103
    • Yeum, K.J.1    Russell, R.M.2    Krinsky, N.I.3    Aldini, G.4
  • 16
    • 84885468679 scopus 로고    scopus 로고
    • Functional binding analysis of human fibrinogen as an iron- and heme-binding protein
    • Orino K. Functional binding analysis of human fibrinogen as an iron- and heme-binding protein. Biometals 2013;26:789-794.
    • (2013) Biometals , vol.26 , pp. 789-794
    • Orino, K.1
  • 18
    • 84927691106 scopus 로고    scopus 로고
    • Iron and carbon monoxide enhance coagulation and attenuate fibrinolysis by different mechanisms
    • 24732176 in press
    • Nielsen VG, Pretorius E. Iron and carbon monoxide enhance coagulation and attenuate fibrinolysis by different mechanisms. Blood Coagul Fibrinolysis 2014; in press, PMID: 24732176.
    • (2014) Blood Coagul Fibrinolysis
    • Nielsen, V.G.1    Pretorius, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.