Artículo

La versión final de este artículo es de uso interno de la institución.
Consulte el artículo en la página del editor
Consulte la política de Acceso Abierto del editor

Abstract:

Introduction: Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II to enhance antithrombin action. It has also been suggested that DS has a profibrinolytic effect, although the exact molecular mechanism is as yet unknown. Materials and methods: An in vitro amidolytic method was used to study the effect of high and low molecular weight-DS on the activation of Glu and Lys-plasminogen by tissue and urinary plasminogen activators (t-PA and u-PA). Results: Both high and low molecular weight-DS exhibited a stimulating effect on the activation of plasminogen by PAs. Interestingly, high molecular weight-DS stimulated Glu and Lys-plasminogen activation by t-PA and u-PA in a way and to an extent similar to that in which fibrin(ogen) degradation products (PDF) increased the t-PA assay. Meanwhile low molecular weight-DS had a lower effect. No DS had any effect on plasmin or u-PA amidolytic activity. The facilitation of the conversion of Glu-plasminogen to plasmin in the presence of DS was confirmed by SDS-PAGE; high molecular weight-DS effect was greater than low molecular weight-DS in accordance with the chromogenic assays. Moreover, the combination of PDF and high and low molecular weight-DS, respectively, did not further stimulate t-PA activation of either Glu or Lys-plasminogen suggesting that both substances may compete for the same binding sites. Conclusions: Through in vitro assays we demonstrated that high and low molecular weight-DS enhance plasminogen activation by u-PA and t-PA, suggesting that the profibrinolytic activity of DS might be via potentiation of plasminogen conversion to plasmin. © 2007 Elsevier Ltd. All rights reserved.

Registro:

Documento: Artículo
Título:Insight into the profibrinolytic activity of dermatan sulfate: Effects on the activation of plasminogen mediated by tissue and urinary plasminogen activators
Autor:Castañon, M.M.; Gamba, C.; Kordich, L.C.
Filiación:Laboratorio de Hemostasia y Trombosis, Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Buenos Aires, Argentina
Palabras clave:Dermatan sulfate; Fibrin-fibrinogen degradation products; Plasminogen activation; Tissue plasminogen activator; Urinary plasminogen activator; dermatan sulfate; fibrin degradation product; glutamic acid; heparin cofactor II; plasmin; plasminogen; plasminogen[glutamic acid]; plasminogen[lysine]; tissue plasminogen activator; unclassified drug; urokinase; article; binding site; controlled study; enzyme activity; fibrinolysis; human; molecular weight; plasminogen activation; polyacrylamide gel electrophoresis; priority journal; protein function; reaction analysis; Anticoagulants; Antithrombins; Dermatan Sulfate; Fibrinolysis; Glutamic Acid; Humans; Hydrolysis; Models, Chemical; Molecular Weight; Peptide Fragments; Plasmin; Plasminogen; Plasminogen Activators; Time Factors; Tissue Plasminogen Activator; Urinary Plasminogen Activator
Año:2007
Volumen:120
Número:5
Página de inicio:745
Página de fin:752
DOI: http://dx.doi.org/10.1016/j.thromres.2006.12.014
Título revista:Thrombosis Research
Título revista abreviado:Thromb. Res.
ISSN:00493848
CODEN:THBRA
CAS:dermatan sulfate, 24967-94-0; glutamic acid, 11070-68-1, 138-15-8, 56-86-0, 6899-05-4; heparin cofactor II, 81604-65-1; plasmin, 9001-90-5, 9004-09-5; plasminogen, 9001-91-6; tissue plasminogen activator, 105913-11-9; urokinase, 139639-24-0; Anticoagulants; Antithrombins; Dermatan Sulfate, 24967-94-0; Glutamic Acid, 56-86-0; Peptide Fragments; Plasmin, 3.4.21.7; Plasminogen, 9001-91-6; Plasminogen Activators, 3.4.21.-; Tissue Plasminogen Activator, 3.4.21.68; Urinary Plasminogen Activator, 3.4.21.73; lysyl-plasminogen
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00493848_v120_n5_p745_Castanon

Referencias:

  • Bachmann, F., Plasminogen-plasmin enzyme system (2001) Basic Principles and clinical practice, pp. 275-320. , Hemostasis and Thrombosis. Colman R.W., Hirsh J., Marder V.J., Clowes A.W., and George J.N. (Eds), Lippincott Williams & Wilkins, Philadelphia, LA, USA
  • Holvoet, P., Lijnen, H.R., Collen, D., A monoclonal antibody specific for Lys-plasminogen (1985) J Biol Chem, 260 (22), pp. 12106-12111
  • Casu, B., Structural features and binding properties of chondroitin sulfate, dermatan sulfate and heparan sulfate (1991) Semin Thromb Hemost, 17 (1), pp. 9-14
  • Andrew, M.A., Mitchell, L., Berry, L., Paes, B., Delorme, M., Ofosu, F., An anticoagulant dermatan sulfate proteoglycan circulates in pregnant woman and her fetus (1992) J Clin Invest, 89 (1), pp. 321-326
  • Delorme, M.A., Saees, N., Sevick, A., Mitchell, L., Berry, L., Johnston, M., Plasma dermatan sulfate proteoglycan in a patient on chronic hemodialysis (1993) Blood, 82, pp. 3380-3385
  • Rossi, E., Duboscq, C., Peragallo, M., Kordich, L., Heparin cofactor II (HC II) and dermatan sulfate plasmatic levels in acute burnt patients (1997) Thromb Haemost, p. 435. , Suppl
  • Duboscq, C., Rossi, E., Quintana, I., Kordich, L., Actividad del cofactor II de la heparina y concentración de dermatán sulfato en pacientes sépticos (1994) Medicina, 54 (5-2), p. 509
  • Tollefsen, D.M., Pestka, C.A., Monafo, W.J., Activation of heparin cofactor II by dermatan sulfate (1983) J Biol Chem, 258 (11), pp. 6713-6716
  • Han, J.H., Cote, H.C.F., Tollefsen, D.M., Inhibition of meizothrombin and meizothrombin(des F1) by heparin cofactor II (1997) J Biol Chem, 272, pp. 28660-28665
  • Bock, S.C., Antithrombin III and heparin cofactor II (2006) Basis Principles and Clinical Practice, pp. 235-248. , Hemostasis and Thrombosis. Colman R.W., Clowes A.W., Goldhaber S.Z., Marder V.J., and George J.N. (Eds), Lippincott Williams & Wilkins, Philadelphia-United States
  • Barbanti, M., Calani, F., Babbini, M., Bergonzini, G., Parma, B., Marchi, E., Antithrombotic activity of Desmin 370 comparison with a high molecular weight dermatan sulphate (1993) Thromb Res, 71, pp. 417-422
  • Agnelli, G., Cosmi, B., Di Filippo, P., Ranucci, V., Veschi, F., Longetti, M., A randomized, double-blind, placebo-controlled trial of dermatan sulfate for prevention of deep vein thrombosis in hip fracture (1992) Thromb Haemost, 67, pp. 203-208
  • Prandoni, P., Meduri, F., Cuppini, S., Toniato, A., Zangrandi, Z., Polisterna, P., Dermatan sulphate: a safe approach to prevention of post operative deep vein thrombosis (1992) Br J Surg, 79, pp. 505-509
  • Kretz, J., Chakje, N., Wiesel, M.L., Grunebaum, L., Zamboni, V., Palazzini, E., The treatment of deep vein thrombosis with intravenous low-molecular-weight dermatan sulphate (Desmin). A pilot study (1996) Thromb Res, 84 (6), pp. 391-398
  • Von Kemp, K., Jochmans, K., Tussenbroek, F., Debruyne, H., Van den Brade, P., Desmin (a low molecular weight dermatan sulfate) versus heparin in treatment of patients with deep venous thrombosis (1998) Eur J Clin Pharmacol, 54 (2), pp. 133-139
  • Attanasio, E., Russo, P., Carunchio, G., Caprino, L., Dermatan sulfate versus unfractionated heparin for the prevention of venous thromboembolism in patients undergoing surgery for cancer. A cost-effectiveness analysis (2001) Pharmacoeconomics, 19 (1), pp. 57-68
  • Taliani, M.R., Agnelli, G., Nenci, G.G., Gianese, F., Dermatan sulfate in patients with heparin-induced thrombocytopenia (1999) Br J Haematol, 104, pp. 87-89
  • Imberti, D., Verso, M., Silvestrini, E., Taliani, M.R., Agnelli, G., Successful treatment with dermatan sulfate in six patients with heparin-induced thrombocytopenia and acute venous thromboembolism (2003) J Thromb Haemost, 1, pp. 2696-2697
  • Boccardo, P., Melacini, D., Rota, S., Mecca, G., Boletta, A., Casiraghi, F., Individualized anticoagulation with dermatan sulphate for haemodialysis in chronic renal failure (1997) Nephrol Dial Transplant, 12 (11), pp. 2349-2354
  • Ryan, K.E., Lane, D.A., Flynn, A., Ireland, H., Boisclair, M., Shepperd, J., Antithrombotic properties of dermatan sulphate (MF 701) in haemodialysis for chronic renal failure (1992) Thromb Haemost, 68 (5), pp. 563-569
  • Van Ryn-McKenna, J., Weber, E.G.E., Ofosu, F.A., Buchnan, M.R., Effects of sulfated polysaccharides on inhibition of thrombus formation initiated by different stimuli (1989) Thromb Haemost, 61 (1), pp. 7-9
  • Van Ryn-McKenna, J., Ofosu, F.A., Gray, E., Hirsh, J., Buchanan, M.R., Effects of dermatan sulphate and heparin on inhibition of thrombus growth in vivo (1989) Ann NY Acad Sci, 556, pp. 304-312
  • Carrie, D., Caranobe, C., Gabaig, A.M., Larroche, M., Boneu, B., Effects of heparin, dermatan sulphate and of their association on the inhibition of venous thrombosis growth in the rabbit (1992) Thromb Haemost, 68 (6), pp. 637-641
  • Santoro, F.M., Alvarez, R., Fussi, F., Pharmacological profile of a native dermatan sulphate (1992) Thromb Res, 67 (2), pp. 201-211
  • Barbanti, M., Calanni, F., Milani, M.R., Marchi, E., Semerano, N., Colucci, M., Therapeutic effect of a low molecular weight dermatan sulphate (Desmin 370) in rat venous thrombosis. Evidence for an anticoagulant-independent mechanism (1993) Thromb Haemost, 69 (2), pp. 147-151
  • Colucci, M., Sardella, L., Barbanti, M., Calanni, F., Semerano, N., Thrombolysis enhancing activity of a low molecular weight dermatan sulfate (Desmin 370) in experimental pulmonary embolism in rats (1997) Thromb Res, 87 (5), pp. 441-446
  • Colucci, M., Rossiello, M.R., Barbanti, M., Calanni, F., Semerano, N., Prevention and therapy of experimental venous trombosis in rabbits by Desmin 370 (1998) Thromb Haemost, 80, pp. 338-341
  • Barbanti, M., Calanni, F., Marchi, E., Semerano, N., Colucci, M., Desmin 370, a low molecular weight dermatan sulphate, reduces the weight of performed thrombi in rats made afibrinogenemic by ancrod (1995) Thromb Haemost, 73 (2), pp. 287-290
  • Tripodi, A., Moia, M., Bottasso, B., Tenconi, P.M., Gianese, F., Mannucci, P.M., Effects of subcutaneously administered dermatan sulfate (MF 701) on the coagulation and fibrinolytic parameters of healthy volunteers (1991) Thromb Res, 62 (6), pp. 663-672
  • Dettori, A.G., Galli, G., Manotti, C., Palazzini, E., Pharmacological activity of a low molecular weight dermatan sulfate (Desmin) in healthy volunteers (1994) Semin Thromb Hemost, 20 (3), pp. 259-265
  • Harenberg, J., Jeschek, M., Acker, M., Malsch, R., Huhle, G., Heene, D.L., Effect of low-molecular-weight dermatan sulphate on coagulation, fibrinolysis and tissue factor pathway inhibitor in healthy volunteers (1996) Blood Coagul Fibrinolysis, 7 (1), pp. 49-56
  • Abbadini, M., Zhu, G.J., Maggi, A., Pangrazzi, J., Donati, M.B., Mussoni, L., Dermatan sulphate induces plasminogen activator release in perfused rat hindquarters (1987) Blood, 70 (6), pp. 1858-1860
  • Krupinski, K., Bielawiec, M., Yoshida, K., Kyogashima, M., Takada, Y., Takada, A., Dermatan sulphate enhances lysis of laser induced thrombus in vivo (1998) Thromb Res, 91, pp. 199-202
  • Marsh, N.A., Minter, A.J., Chesterman, C.N., The effect of heparin and other glycosaminoglycans on levels of tissue plasminogen activator and plasminogen activator inhibitor in cultured human umbilical vein endothelial cells (1990) Blood Coagul Fibrinolysis, 1 (2), pp. 133-138
  • Kyogashima, M., Onaya, J., Miyauchi, S., Arai, M., Shibata, Y., Suda, A., Antithrombotic activity of avian crown dermatan sulphate (1999) Thromb Res, 96, pp. 459-465
  • Paques, E.P., Stohr, H.A., Heimburger, N., Study on the mechanism of action of heparin and related substances on the fibrinolytic system: relationship between plasminogen activators and heparin (1986) Thromb Res, 42, pp. 797-807
  • Takada, Y., Urano, T., Takada, A., Effects of heparan sulfated analogue or other sulphate polysaccharides on the activation of plasminogen by t-PA and u-PA (1994) Thromb Res, 73 (5), pp. 301-311
  • Andrade-Gordon, P., Strickland, S., Interaction of heparin with plasminogen activators and plasminogen: Effects on the activation of plasminogen (1986) Biochemistry, 25, pp. 4033-4040
  • Stein, P.L., Van Zonneveld, A.J., Pannekoek, H., Strickland, S., Structural domains of human-type plasminogen activator that confer stimulation by heparin (1989) J Biol Chem, 264 (26), pp. 15441-15444
  • Stephens, R.W., Bokman, A.M., Myohanen, H.T., Reisberg, T., Tapiovaara, H., Pedersen, N., Heparin binding to the urokinase kringle domain (1992) Biochemistry, 31, pp. 7572-7579
  • Liang, J.F., Li, Y., Yang, V., The potential mechanism for the effect of heparin on tissue plasminogen activator-mediated plasminogen activation (2000) Thromb Res, 97, pp. 349-358
  • Takada, A., Takada, Y., Sugawara, Y., Effects of fibrinogen and fibrin on the activation of Glu- and Lys-Plasminogen by urokinase (1984) Thromb Res, 33, pp. 561-569
  • Laemmli, K.V., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685
  • Rydzewski, A., Takada, Y., Takada, A., Stimulation of plasmin catalyzed conversion of single-chain to two chain urokinase-type plasminogen activator by sulphated polysaccharides (1989) Thromb Haemost, 62 (2), pp. 752-755
  • Dosne, A.M., Bendetowitz, A.V., Kher, A., Samama, M., Marked potentiation of the plasminogenolytic activity of pro-urokinase by unfractionated heparin and low molecular weight heparin (1988) Thromb Res, 51, pp. 627-630
  • Mangel, W.F., Lin, B.H., Ramakrishanan, V., Characterization of an extremely large, ligand-induced conformational change in plasminogen (1990) Science, 248 (4951), pp. 69-73
  • Markus, G., Evers, J.L., Hobika, G.H., Comparison of some properties of native (Glu) and modified (Lys) human plasminogen (1978) J Biol Chem, 253 (3), pp. 733-739
  • Andrade-Gordon, P., Strickland, S., Anticoagulant low molecular weight heparin does not enhance the activation of plasminogen by t-PA (1989) J Biol Chem, 264 (26), pp. 15177-15181
  • Edelberg, J.M., Weissler, M., Pizzo, S.V., Heparin oligosaccharides enhance t-PA: a correlation between oligosaccharide length and stimulation of plasminogen activation (1991) Biochemistry, 30, pp. 10999-11003

Citas:

---------- APA ----------
Castañon, M.M., Gamba, C. & Kordich, L.C. (2007) . Insight into the profibrinolytic activity of dermatan sulfate: Effects on the activation of plasminogen mediated by tissue and urinary plasminogen activators. Thrombosis Research, 120(5), 745-752.
http://dx.doi.org/10.1016/j.thromres.2006.12.014
---------- CHICAGO ----------
Castañon, M.M., Gamba, C., Kordich, L.C. "Insight into the profibrinolytic activity of dermatan sulfate: Effects on the activation of plasminogen mediated by tissue and urinary plasminogen activators" . Thrombosis Research 120, no. 5 (2007) : 745-752.
http://dx.doi.org/10.1016/j.thromres.2006.12.014
---------- MLA ----------
Castañon, M.M., Gamba, C., Kordich, L.C. "Insight into the profibrinolytic activity of dermatan sulfate: Effects on the activation of plasminogen mediated by tissue and urinary plasminogen activators" . Thrombosis Research, vol. 120, no. 5, 2007, pp. 745-752.
http://dx.doi.org/10.1016/j.thromres.2006.12.014
---------- VANCOUVER ----------
Castañon, M.M., Gamba, C., Kordich, L.C. Insight into the profibrinolytic activity of dermatan sulfate: Effects on the activation of plasminogen mediated by tissue and urinary plasminogen activators. Thromb. Res. 2007;120(5):745-752.
http://dx.doi.org/10.1016/j.thromres.2006.12.014