Enhanced <i>in vitro</i> fibrinolytic activity of immobilized plasmin on collagen beads

Shankar, Hariharan; Senatore, Fred; Zuniga, P.; Venkataramani, E.S.

doi:10.1002/jbm.820210706

Cited by 9 publications

(12 citation statements)

References 17 publications

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“…CU/cm2 graft) are significant (22) For personal use only. The numbers reported for plasmin loading (i.e.…”

Section: Resultsmentioning

confidence: 99%

“…Senatore (19,20) immobilized urokinase on fibrocollagenous tubes. Shankar et al (22) immobilized plasmin on collagen beads. Shankar et al (22) immobilized plasmin on collagen beads.…”

Section: Introductionmentioning

confidence: 99%

“…In assuming that Michaelis-Menten kinetics apply(22) to plasmin activity, the kinetic parameters Vmax and K , were identified by the Cornish-Bowden-Eisenthal Method for plasmin as a function of heparin interaction both in the soluble and immobilized state. In assuming that Michaelis-Menten kinetics apply(22) to plasmin activity, the kinetic parameters Vmax and K , were identified by the Cornish-Bowden-Eisenthal Method for plasmin as a function of heparin interaction both in the soluble and immobilized state.…”

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confidence: 99%

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Co-Immobilization and Interaction of Heparin and Plasmin on Collageno-Elastic Tubes

Shankar

Senatore

et al. 1990

Biomaterials, Artificial Cells and Artificial Organs

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Heparin and plasmin were co-immobilized on collageno-elastic tubes (CETs) in order to develop a thromboresistant and fibrinolytic vascular prosthesis. The mutual interaction between heparin and plasmin both in the soluble and in the immobilized state was studied. The immobilization condition rendering maximum co-immobilized heparin and plasmin activity was identified to require heparin immobilization followed by plasmin immobilization. Soluble heparin exerts a positive synergistic effect on soluble plasmin. Immobilized heparin enhances plasmin loading on the CET as compared to the heparin-free graft. Heparin, in both the soluble or immobilized state, significantly decreases the Michaelis-Menten (M-M) parameter Km for immobilized plasmin over heparin-free immobilized plasmin. Furthermore, the M-M parameter Vmax for the immobilized plasmin in the presence of heparin decreases over heparin-free immobilized plasmin. These results suggest a decrease in the kinetic constant k3 for heparin-modified immobilized plasmin over the heparin-free form. Co-immobilized heparin-plasmin collagenous grafts represent a unique advance in the development of fibrinolytically active prostheses.

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“…CU/cm2 graft) are significant (22) For personal use only. The numbers reported for plasmin loading (i.e.…”

Section: Resultsmentioning

confidence: 99%

“…Senatore (19,20) immobilized urokinase on fibrocollagenous tubes. Shankar et al (22) immobilized plasmin on collagen beads. Shankar et al (22) immobilized plasmin on collagen beads.…”

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

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Co-Immobilization and Interaction of Heparin and Plasmin on Collageno-Elastic Tubes

Shankar

Senatore

et al. 1990

Biomaterials, Artificial Cells and Artificial Organs

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“…As might be expected, these particular SK1 expressing strains possess variable tissue and cell tropism in experimental settings. This is not particularly puzzling as hPm formed in blood in vivo would be rapidly inactivated by the circulating natural hPm inhibitor, ␣2-antiplasmin, whereas receptor-or surface-bound hPm is more resistant to inactivation from ␣2-antiplasmin (50,51).…”

Section: Discussionmentioning

confidence: 99%

Direct Host Plasminogen Binding to Bacterial Surface M-protein in Pattern D Strains of Streptococcus pyogenes Is Required for Activation by Its Natural Coinherited SK2b Protein

Chandrahas

Glinton

Zhong

et al. 2015

Journal of Biological Chemistry

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Background: Dissemination of Pattern D strains of S. pyogenes depends on a functional human fibrinolytic system. Results: hPg binding domains of PAM, when transferred to unrelated M-proteins, up-regulates hPg binding and activation. Conclusion:The nature of the streptokinase and the M-protein influence GAS virulence. Significance: In vitro studies indicate pathways for GAS to gain hypervirulence by gene transfer of small functional domains.

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“…Various strategies have been used to control surface coagulation including coating the surface with proteinresistant polymers, (7)(8)(9) active molecules such as anticoagulants [10,11] or fibrinolysis promoters, [12][13][14][15] endothelial cells [16,17] or polymers mimicking their membrane, [18,19] and last but not least inorganic thin films conferring various surface properties as reviewed by Mani and colleagues [20]. A strategy not comprised in this list was proposed by P. N. Sawyer more than 40 years ago and consisted in cathodically polarizing the implant's surface.…”

Section: Introductionmentioning

confidence: 99%

Coagulation at the Blood–Electrode Interface: The Role of Electrochemical Desorption and Degradation of Fibrinogen

et al. 2014

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The influence of electrochemistry on the coagulation of blood on metal surfaces was demonstrated several decades ago. In particular, the application of cathodic currents resulted in reduced surface thrombogenicity, but no molecular mechanism has been so far proposed to explain this observation. In this article we used for the first time the quartz crystal microbalance with dissipation monitoring technique coupled with an electrochemical setup (EQCM-D) to study thrombosis at the blood-electrode interface. We confirmed the reduced thrombus deposition at the cathode, and we subsequently studied the effect of cathodic currents on adsorbed fibrinogen (Fg). Using EQCM and mass spectrometry, we found that upon applying currents Fg desorbed from the electrode and was electrochemically degraded. In particular, we show that the flexible N-terminus of the -chain, containing an important polymerization site, was cleaved from the protein, thus affecting its clottability. Our work proposes a molecular mechanism that at least partially explains how cathodic currents reduce thrombosis at the blood-electrode interface and is a relevant contribution to the rational development of medical devices with reduced thrombus formation on their surface. ABSTRACTThe influence of electrochemistry on the coagulation of blood on metal surfaces was demonstrated several decades ago. In particular, the application of cathodic currents resulted in reduced surface thrombogenicity, but no molecular mechanism has been so far proposed to explain this observation. In this article we used for the first time the quartz crystal microbalance with dissipation monitoring technique coupled with an electrochemical setup (EQCM-D) to study thrombosis at the blood-electrode interface. We confirmed the reduced thrombus deposition at the cathode, and we subsequently studied the effect of cathodic currents on adsorbed fibrinogen (Fg). Using EQCM and mass spectrometry, we found that upon applying currents Fg desorbed from the electrode and was electrochemically degraded. In particular, we show that the flexible N-terminus of the α-chain, containing an important polymerization site, was cleaved from the protein, thus affecting its clottability. Our work proposes a molecular mechanism that at least partially explains how cathodic currents reduce thrombosis at the blood-electrode interface and is a relevant contribution to the rational development of medical devices with reduced thrombus formation on their surface.2

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Enhanced in vitro fibrinolytic activity of immobilized plasmin on collagen beads

Cited by 9 publications

References 17 publications

Co-Immobilization and Interaction of Heparin and Plasmin on Collageno-Elastic Tubes

Co-Immobilization and Interaction of Heparin and Plasmin on Collageno-Elastic Tubes

Direct Host Plasminogen Binding to Bacterial Surface M-protein in Pattern D Strains of Streptococcus pyogenes Is Required for Activation by Its Natural Coinherited SK2b Protein

Coagulation at the Blood–Electrode Interface: The Role of Electrochemical Desorption and Degradation of Fibrinogen

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