메뉴 건너뛰기




Volumn 178, Issue 1, 2017, Pages 119-129

Platelets stored at 4°C contribute to superior clot properties compared to current standard-of-care through fibrin-crosslinking

Author keywords

clot strength; factor XIII; refrigeration; rheology; ultrastructure

Indexed keywords

BLOOD CLOTTING FACTOR 13; CYTOCHALASIN; EPTIFIBATIDE; THROMBIN; FIBRIN;

EID: 85020220016     PISSN: 00071048     EISSN: 13652141     Source Type: Journal    
DOI: 10.1111/bjh.14751     Document Type: Article
Times cited : (80)

References (52)
  • 3
    • 85021210444 scopus 로고    scopus 로고
    • Last accessed August 2015
    • Bob. (2014) Kittler-Illingworth Thresholding. Available at: http://www.mathworks.com/matlabcentral/fileexchange/45685-kittler-illingworth-thresholding Last accessed August 2015.
    • (2014) Kittler-Illingworth Thresholding
  • 4
    • 85013673980 scopus 로고    scopus 로고
    • The interaction between fibrinogen and zymogen FXIII-A2B2 is mediated by fibrinogen residues gamma390-396 and the FXIII-B subunits
    • Byrnes, J.R., Wilson, C., Boutelle, A.M., Brandner, C.B., Flick, M.J., Philippou, H. & Wolberg, A.S. (2016) The interaction between fibrinogen and zymogen FXIII-A2B2 is mediated by fibrinogen residues gamma390-396 and the FXIII-B subunits. Blood, 128, 1969–1978.
    • (2016) Blood , vol.128 , pp. 1969-1978
    • Byrnes, J.R.1    Wilson, C.2    Boutelle, A.M.3    Brandner, C.B.4    Flick, M.J.5    Philippou, H.6    Wolberg, A.S.7
  • 6
    • 0017910967 scopus 로고
    • Size and density of fibrin fibers from turbidity
    • Carr, M.E. Jr & Hermans, J. (1978) Size and density of fibrin fibers from turbidity. Macromolecules, 11, 46–50.
    • (1978) Macromolecules , vol.11 , pp. 46-50
    • Carr, M.E.1    Hermans, J.2
  • 7
    • 68949198026 scopus 로고    scopus 로고
    • The in vitro effect of eptifibatide, a glycoprotein IIb/IIIa antagonist, on various responses of porcine blood platelets
    • Ciborowski, M. & Tomasiak, M. (2009) The in vitro effect of eptifibatide, a glycoprotein IIb/IIIa antagonist, on various responses of porcine blood platelets. Acta Poloniae Pharmaceutica, 66, 235–242.
    • (2009) Acta Poloniae Pharmaceutica , vol.66 , pp. 235-242
    • Ciborowski, M.1    Tomasiak, M.2
  • 8
    • 0036086957 scopus 로고    scopus 로고
    • Hypotensive resuscitation during active hemorrhage: impact on in-hospital mortality
    • Dutton, R.P., Mackenzie, C.F. & Scalea, T.M. (2002) Hypotensive resuscitation during active hemorrhage: impact on in-hospital mortality. Journal of Trauma, 52, 1141–1146.
    • (2002) Journal of Trauma , vol.52 , pp. 1141-1146
    • Dutton, R.P.1    Mackenzie, C.F.2    Scalea, T.M.3
  • 10
    • 0345052707 scopus 로고
    • The conversion of fibrinogen to fibrin. VII. Rigidity and stress relaxation of fibrin clots, eff. of calcium
    • Ferry, J.D., Miller, M. & Shulman, S. (1951) The conversion of fibrinogen to fibrin. VII. Rigidity and stress relaxation of fibrin clots, eff. of calcium. Archives of Biochemistry and Biophysics, 34, 424–436.
    • (1951) Archives of Biochemistry and Biophysics , vol.34 , pp. 424-436
    • Ferry, J.D.1    Miller, M.2    Shulman, S.3
  • 11
    • 0017853687 scopus 로고
    • Relative hemostatic effectiveness of human platelets stored at 4°C and 22°C
    • Filip, D.J. & Aster, R.H. (1978) Relative hemostatic effectiveness of human platelets stored at 4°C and 22°C. Journal of Laboratory and Clinical Medicine, 91, 618–624.
    • (1978) Journal of Laboratory and Clinical Medicine , vol.91 , pp. 618-624
    • Filip, D.J.1    Aster, R.H.2
  • 13
    • 84882570807 scopus 로고    scopus 로고
    • Rubber elasticity: basic concepts and behavior
    • In, (ed., J.E. Mark, B. Erman, &, C.M. Roland, 4th edn, Chapter 1, Academic Press, Waltham, MA, USA
    • Gent, A.N. (2013) Rubber elasticity: basic concepts and behavior. In: The Science and Technology of Rubber, (ed. J.E. Mark, B. Erman & C.M. Roland) 4th edn, Chapter 1, pp. 1–26. Academic Press, Waltham, MA, USA.
    • (2013) The Science and Technology of Rubber , pp. 1-26
    • Gent, A.N.1
  • 14
    • 0016274342 scopus 로고
    • Rheology of fibrin clots. II. Linear viscoelastic behavior in shear creep
    • Gerth, C., Roberts, W.W. & Ferry, J.D. (1974) Rheology of fibrin clots. II. Linear viscoelastic behavior in shear creep. Biophysical Chemistry, 2, 208–217.
    • (1974) Biophysical Chemistry , vol.2 , pp. 208-217
    • Gerth, C.1    Roberts, W.W.2    Ferry, J.D.3
  • 15
    • 78649337010 scopus 로고    scopus 로고
    • Differential phosphorylation of myosin light chain (Thr)18 and (Ser)19 and functional implications in platelets
    • Getz, T.M., Dangelmaier, C.A., Jin, J., Daniel, J.L. & Kunapuli, S.P. (2010) Differential phosphorylation of myosin light chain (Thr)18 and (Ser)19 and functional implications in platelets. Journal of Thrombosis and Haemostasis, 8, 2283–2293.
    • (2010) Journal of Thrombosis and Haemostasis , vol.8 , pp. 2283-2293
    • Getz, T.M.1    Dangelmaier, C.A.2    Jin, J.3    Daniel, J.L.4    Kunapuli, S.P.5
  • 16
    • 84958817419 scopus 로고    scopus 로고
    • Storage of platelets at 4°C in platelet additive solutions prevents aggregate formation and preserves platelet functional responses
    • Getz, T.M., Montgomery, R.K., Bynum, J.A., Aden, J.K., Pidcoke, H.F. & Cap, A.P. (2016) Storage of platelets at 4°C in platelet additive solutions prevents aggregate formation and preserves platelet functional responses. Transfusion, 56, 1320–1328.
    • (2016) Transfusion , vol.56 , pp. 1320-1328
    • Getz, T.M.1    Montgomery, R.K.2    Bynum, J.A.3    Aden, J.K.4    Pidcoke, H.F.5    Cap, A.P.6
  • 17
    • 0016796805 scopus 로고
    • Dynamic coagulation studies: influence of normal and abnormal platelets on clot structure formation
    • Glover, C.J., McIntire, L.V., Brown, C.H. 3rd & Natelson, E.A. (1975) Dynamic coagulation studies: influence of normal and abnormal platelets on clot structure formation. Thrombosis Research, 7, 185–198.
    • (1975) Thrombosis Research , vol.7 , pp. 185-198
    • Glover, C.J.1    McIntire, L.V.2    Brown, C.H.3    Natelson, E.A.4
  • 22
    • 77949521779 scopus 로고    scopus 로고
    • Impaired clot retraction in factor XIII A subunit-deficient mice
    • Kasahara, K., Souri, M., Kaneda, M., Miki, T., Yamamoto, N. & Ichinose, A. (2010) Impaired clot retraction in factor XIII A subunit-deficient mice. Blood, 115, 1277–1279.
    • (2010) Blood , vol.115 , pp. 1277-1279
    • Kasahara, K.1    Souri, M.2    Kaneda, M.3    Miki, T.4    Yamamoto, N.5    Ichinose, A.6
  • 27
    • 84925635114 scopus 로고    scopus 로고
    • (Perona & Malik) Available from, last accessed August 2015
    • Lopes, D. (2007) Anisotropic Diffusion (Perona & Malik) Available from: http://www.mathworks.com/matlabcentral/fileexchange/14995-anisotropicdiffusion-perona-, last accessed August 2015.
    • (2007) Anisotropic Diffusion
    • Lopes, D.1
  • 28
    • 79952178145 scopus 로고    scopus 로고
    • Molecular mechanisms affecting fibrin structure and stability
    • Lord, S.T. (2011) Molecular mechanisms affecting fibrin structure and stability. Arteriosclerosis, Thrombosis, and Vascular Biology, 31, 494–499.
    • (2011) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.31 , pp. 494-499
    • Lord, S.T.1
  • 29
    • 79953301142 scopus 로고    scopus 로고
    • Factor XIII supports platelet activation and enhances thrombus formation by matrix proteins under flow conditions
    • Magwenzi, S.G., Ajjan, R.A., Standeven, K.F., Parapia, L.A. & Naseem, K.M. (2011) Factor XIII supports platelet activation and enhances thrombus formation by matrix proteins under flow conditions. Journal of Thrombosis and Haemostasis, 9, 820–833.
    • (2011) Journal of Thrombosis and Haemostasis , vol.9 , pp. 820-833
    • Magwenzi, S.G.1    Ajjan, R.A.2    Standeven, K.F.3    Parapia, L.A.4    Naseem, K.M.5
  • 32
    • 0014677132 scopus 로고
    • Effect of storage temperature on maintenance of platelet viability–deleterious effect of refrigerated storage
    • Murphy, S. & Gardner, F.H. (1969) Effect of storage temperature on maintenance of platelet viability–deleterious effect of refrigerated storage. New England Journal of Medicine, 280, 1094–1098.
    • (1969) New England Journal of Medicine , vol.280 , pp. 1094-1098
    • Murphy, S.1    Gardner, F.H.2
  • 34
    • 0025957849 scopus 로고
    • Effect of plasminogen and tissue-type plasminogen activator on fibrin gel structure
    • Petersen, L.C. & Suenson, E. (1991) Effect of plasminogen and tissue-type plasminogen activator on fibrin gel structure. Fibrinolysis, 5, 51–59.
    • (1991) Fibrinolysis , vol.5 , pp. 51-59
    • Petersen, L.C.1    Suenson, E.2
  • 37
    • 84957821838 scopus 로고    scopus 로고
    • Endothelium-derived inhibitors efficiently attenuate the aggregation and adhesion responses of refrigerated platelets
    • Reddoch, K.M., Montgomery, R.K., Rodriguez, A.C., Meledeo, M.A., Pidcoke, H.F., Ramasubramanian, A.K. & Cap, A.P. (2016) Endothelium-derived inhibitors efficiently attenuate the aggregation and adhesion responses of refrigerated platelets. Shock, 45, 220–227.
    • (2016) Shock , vol.45 , pp. 220-227
    • Reddoch, K.M.1    Montgomery, R.K.2    Rodriguez, A.C.3    Meledeo, M.A.4    Pidcoke, H.F.5    Ramasubramanian, A.K.6    Cap, A.P.7
  • 38
    • 0015594187 scopus 로고
    • Viscoelastic properties of fibrin clots
    • Roberts, W.W., Lorand, L. & Mockros, L.F. (1973) Viscoelastic properties of fibrin clots. Biorheology, 10, 29–42.
    • (1973) Biorheology , vol.10 , pp. 29-42
    • Roberts, W.W.1    Lorand, L.2    Mockros, L.F.3
  • 39
    • 0028789679 scopus 로고
    • Effects of storage time on quantitative and qualitative platelet function after transfusion
    • Rosenfeld, B.A., Herfel, B., Faraday, N., Fuller, A. & Braine, H. (1995) Effects of storage time on quantitative and qualitative platelet function after transfusion. Anesthesiology, 83, 1167–1172.
    • (1995) Anesthesiology , vol.83 , pp. 1167-1172
    • Rosenfeld, B.A.1    Herfel, B.2    Faraday, N.3    Fuller, A.4    Braine, H.5
  • 40
    • 0032750788 scopus 로고    scopus 로고
    • Influence of a natural and a synthetic inhibitor of factor XIIIa on fibrin clot rheology
    • Ryan, E.A., Mockros, L.F., Stern, A.M. & Lorand, L. (1999a) Influence of a natural and a synthetic inhibitor of factor XIIIa on fibrin clot rheology. Biophysical Journal, 77, 2827–2836.
    • (1999) Biophysical Journal , vol.77 , pp. 2827-2836
    • Ryan, E.A.1    Mockros, L.F.2    Stern, A.M.3    Lorand, L.4
  • 43
    • 0017225319 scopus 로고
    • Preparation and storage of platelet concentrates
    • Slichter, S.J. & Harker, L.A. (1976) Preparation and storage of platelet concentrates. Transfusion, 16, 8–12.
    • (1976) Transfusion , vol.16 , pp. 8-12
    • Slichter, S.J.1    Harker, L.A.2
  • 44
    • 34547942696 scopus 로고    scopus 로고
    • Functional analysis of fibrin {gamma}-chain cross-linking by activated factor XIII: determination of a cross-linking pattern that maximizes clot stiffness
    • Standeven, K.F., Carter, A.M., Grant, P.J., Weisel, J.W., Chernysh, I., Masova, L., Lord, S.T. & Ariens, R.A. (2007) Functional analysis of fibrin {gamma}-chain cross-linking by activated factor XIII: determination of a cross-linking pattern that maximizes clot stiffness. Blood, 110, 902–907.
    • (2007) Blood , vol.110 , pp. 902-907
    • Standeven, K.F.1    Carter, A.M.2    Grant, P.J.3    Weisel, J.W.4    Chernysh, I.5    Masova, L.6    Lord, S.T.7    Ariens, R.A.8
  • 45
    • 34547595111 scopus 로고    scopus 로고
    • Platelet transfusions
    • Stroncek, D.F. & Rebulla, P. (2007) Platelet transfusions. Lancet, 370, 427–438.
    • (2007) Lancet , vol.370 , pp. 427-438
    • Stroncek, D.F.1    Rebulla, P.2
  • 47
    • 0032535294 scopus 로고    scopus 로고
    • Structural studies of fibrinolysis by electron microscopy
    • Veklich, Y., Francis, C.W., White, J. & Weisel, J.W. (1998) Structural studies of fibrinolysis by electron microscopy. Blood, 92, 4721–4729.
    • (1998) Blood , vol.92 , pp. 4721-4729
    • Veklich, Y.1    Francis, C.W.2    White, J.3    Weisel, J.W.4
  • 48
    • 84870485110 scopus 로고    scopus 로고
    • Fibrin clot structure and mechanics associated with specific oxidation of methionine residues in fibrinogen
    • Weigandt, K.M., White, N., Chung, D., Ellingson, E., Wang, Y., Fu, X. & Pozzo, D.C. (2012) Fibrin clot structure and mechanics associated with specific oxidation of methionine residues in fibrinogen. Biophysical Journal, 103, 2399–2407.
    • (2012) Biophysical Journal , vol.103 , pp. 2399-2407
    • Weigandt, K.M.1    White, N.2    Chung, D.3    Ellingson, E.4    Wang, Y.5    Fu, X.6    Pozzo, D.C.7
  • 49
    • 9644260704 scopus 로고    scopus 로고
    • The mechanical properties of fibrin for basic scientists and clinicians
    • Weisel, J.W. (2004) The mechanical properties of fibrin for basic scientists and clinicians. Biophysical Chemistry, 112, 267–276.
    • (2004) Biophysical Chemistry , vol.112 , pp. 267-276
    • Weisel, J.W.1
  • 50
    • 84876403873 scopus 로고    scopus 로고
    • The hydraulic permeability of blood clots as a function of fibrin and platelet density
    • Wufsus, A.R., Macera, N.E. & Neeves, K.B. (2013) The hydraulic permeability of blood clots as a function of fibrin and platelet density. Biophysical Journal, 104, 1812–1823.
    • (2013) Biophysical Journal , vol.104 , pp. 1812-1823
    • Wufsus, A.R.1    Macera, N.E.2    Neeves, K.B.3
  • 52
    • 0023716787 scopus 로고
    • B protein of factor XIII: differentiation between free B and complexed B
    • Yorifuji, H., Anderson, K., Lynch, G.W., Van de Water, L. & McDonagh, J. (1988) B protein of factor XIII: differentiation between free B and complexed B. Blood, 72, 1645–1650.
    • (1988) Blood , vol.72 , pp. 1645-1650
    • Yorifuji, H.1    Anderson, K.2    Lynch, G.W.3    Van de Water, L.4    McDonagh, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.