Effects of calcium ion and covalent crosslinking on formation and elasticity of fibrin gels

Shen, Linus L.; Hermans, Jan; McDonagh, Jan; McDonagh, R. P.; Carr, Marcus E.

doi:10.1016/0049-3848(75)90073-0

Cited by 113 publications

(55 citation statements)

References 20 publications

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“…Suenson et al and more recently Harpel et al [8, 91 have shown that fibrin, which had been prepared by clotting with thrombin or reptilase, respectively, of partially plasmin-digested fibrinogen, bound increased amounts of Glu-plasminogen. The structure of fibrin formed from fibrinogen degraded by plasmin and of Des-A-fibrin is, however, markedly different from that formed from native fibrinogen [25]. Furthermore, in these studies plasmindegraded fibrinogen has been homogeneously subjected to the proteolytic action of plasmin.…”

Section: (----)mentioning

confidence: 95%

High‐affinity binding sites for human Glu‐plasminogen unveiled by limited plasmic degradation of human fibrin

Tran‐Thang¹,

Kruithof²,

Atkinson³

et al. 1986

European Journal of Biochemistry

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The binding of human 1251-Glu-plasminogen to human plasmin-degraded fibrin was studied. Treatment of preformed and polymerized fibrin with 0.01 IU plasmin/ml resulted in an increased binding of '251-G1~-plasminogen depending upon the length of time of preincubation of fibrin with plasmin. Binding reached a plateau of 30% of total added radioactivity after 60min. At this time, less than 10% of fibrin had been digested. Polyacrylamide/urea/acetic acid gel electrophoresis revealed that the radioiodinated plasminogen bound to plasmin-degraded fibrin was of the Glu form. Computerized non-linear regression analysis of the binding experiments revealed that limited plasmic degradation of fibrin progressively generates high-affinity binding sites (Kd ~0 . 3 pM) for Glu-plasminogen. At the time of maximal Glu-plasminogen binding approximately 5 highaffinity binding sites per 100 molecules of fibrin had been generated. The low-affinity type of binding sites were also identified. These observations describe a new mechanism which exquisitely modulates the plasmic breakdown of fibrin by a continuous renewal of high-affinity binding sites for Glu-plasminogen on the surface of the fibrin gel during the fibrinolytic process.

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Section: (----)mentioning

confidence: 95%

High‐affinity binding sites for human Glu‐plasminogen unveiled by limited plasmic degradation of human fibrin

Tran‐Thang¹,

Kruithof²,

Atkinson³

et al. 1986

European Journal of Biochemistry

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“…The extent of a-chain polymer formation influences the physical properties of fibrin clots by increasing the degree of cross-linking resulting in greater rigidity and elasticity (45,46), and greater resistance to plasmic degradation (23-25). However, these studies assessed cross-linking with gel systems of lower resolution did not define the a-polymers ofthe size demonstrated in this report, and the effect of Factor XIII concentrations > 100% was not considered.…”

Section: Discussionmentioning

confidence: 99%

Rapid formation of large molecular weight alpha-polymers in cross-linked fibrin induced by high factor XIII concentrations. Role of platelet factor XIII.

Francis¹,

Marder²

1987

J. Clin. Invest.

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After fibrin polymerization, activated Factor XIII catalyzes the formation of intermolecular cross-links between '-ychain pairs and also among two or more a-chains to form polymers. In this report we characterize the size and heterogeneity of a-chain polymers, establish the role of high concentrations of Factor XIII in determining the extent and rate of a-polymer formation, and also provide evidence that the Factor XIII required can be provided by platelets. Fibrin prepared from purified fibrinogen or platelet-deficient plasma contained a series of cross-linked a-chain polymers with M, from 140,000 to 770,000 with a mean Mr difference of 32,000 consistent with a staggered, overlapping addition of monomers to the growing a-polymer chain. In plasma containing no platelets, a-polymer formation was incomplete with residual a-monomer remaining, but higher platelet counts facilitated more rapid cross-linking into larger polymers. Purified Factor XIII was equally effective as platelets in facilitating cross-linking. We conclude that cross-linked a-polymer chains are heterogeneous in size reaching a molecular weight of several million and that high concentrations of Factor XIII as provided by platelets are required for maximum cross-linking.

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“…This protein will form clots in response to thrombin action, as does fibrinogen (19). However, clots formed from fragment X have lower tensile strength and are more susceptible to plasminmediated lysis (20)(21)(22).…”

Section: Introductionmentioning

confidence: 99%

Quantitation of fragment X formation during thrombolytic therapy with streptokinase and tissue plasminogen activator.

Owen¹,

Friedman²,

Grossman³

et al. 1987

J. Clin. Invest.

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We have determined the extent of fragment X formation during thrombolytic therapy by integration over time of the plasma fibrinopeptide B#1-42 concentration. This peptide is quantitatively released when fragment X is formed by plasmin action on fibrinogen or fibrin I. In response to streptokinase (SK) and rt-PA, 264±54 and 95±12 mg/dl respectively of fibrinogen was converted to fragment X. By immunoblotting, fragment X was demonstrated as early as 5 min after SK and 30 min after rt-PA, and was still evident 24 h after treatment. Patients treated with SK showed extensive further plasmin degradation of fragment X to fragments Y and D. Thus fragment X concentrations tend to be more similar in the two groups than would be expected from the extent of fibrinogen breakdown. Fragment X forms clots, but these have lower tensile strength and are more susceptible to further plasmin lysis than clots of fibrin. Thus the similar bleeding observed in the two treatment groups might be a reflection of their similar plasma fragment X concentrations.

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Effects of calcium ion and covalent crosslinking on formation and elasticity of fibrin gels

Cited by 113 publications

References 20 publications

High‐affinity binding sites for human Glu‐plasminogen unveiled by limited plasmic degradation of human fibrin

High‐affinity binding sites for human Glu‐plasminogen unveiled by limited plasmic degradation of human fibrin

Rapid formation of large molecular weight alpha-polymers in cross-linked fibrin induced by high factor XIII concentrations. Role of platelet factor XIII.

Quantitation of fragment X formation during thrombolytic therapy with streptokinase and tissue plasminogen activator.

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