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  1. Article ; Online: The effect of factor XIa on thrombin and plasmin generation, clot formation, lysis and density in coagulation factors deficiencies.

    Tarandovskiy, Ivan D / Ovanesov, Mikhail V

    Thrombosis research

    2023  Volume 233, Page(s) 189–199

    Abstract: Introduction: Growing evidence supports the importance of factor (F) XI activation for thrombosis and hemostasis as well as inflammation and complement systems. In this study, we evaluated the effect of activated FXI (FXIa) on the detection of factor ... ...

    Abstract Introduction: Growing evidence supports the importance of factor (F) XI activation for thrombosis and hemostasis as well as inflammation and complement systems. In this study, we evaluated the effect of activated FXI (FXIa) on the detection of factor deficiencies by global hemostasis assays of thrombin generation (TG), plasmin generation (PG), and clot formation and lysis (CFL).
    Materials and methods: An absorbance and fluorescence microplate assay was used to simultaneously observe TG, PG, and CFL in FV-, FVII-, FVIII-, and FIX-deficient plasmas supplemented with purified factors. Coagulation was initiated with tissue factor with or without FXIa in the presence of tissue plasminogen activator. Thrombin and plasmin peak heights (TPH and PPH), maximal clot density (MCD), times to clotting (CT), thrombin and plasmin peaks (TPT and PPT) and clot lysis (LyT) and a new parameter, clot lifetime (LiT), were evaluated.
    Results: TG/CFL were elevated by the FXIa at low FV (below 0.1 IU/mL), and at FVIII and FIX above 0.01 IU/mL. FXIa affected PG only at low FV and FVII. At high factor concentrations, FXIa reduced MCD. Thrombin and plasmin substrates had effect on CT, LyT, LiT and MCD parameters.
    Conclusions: FXIa reveals new relationships between TG, PG and CFL parameters in factor deficiencies suggesting potential benefits for discrimination of bleeding phenotypes.
    MeSH term(s) Humans ; Thrombin ; Factor XIa ; Fibrinolysin ; Tissue Plasminogen Activator ; Blood Coagulation Tests ; Thrombosis
    Chemical Substances Thrombin (EC 3.4.21.5) ; Factor XIa (EC 3.4.21.27) ; Fibrinolysin (EC 3.4.21.7) ; Tissue Plasminogen Activator (EC 3.4.21.68)
    Language English
    Publishing date 2023-11-23
    Publishing country United States
    Document type Journal Article
    ZDB-ID 121852-9
    ISSN 1879-2472 ; 0049-3848
    ISSN (online) 1879-2472
    ISSN 0049-3848
    DOI 10.1016/j.thromres.2023.11.024
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  2. Article ; Online: Comparative Thrombin Generation in Animal Plasma: Sensitivity to Human Factor XIa and Tissue Factor.

    Liang, Yideng / Tarandovskiy, Ivan / Surov, Stepan S / Ovanesov, Mikhail V

    International journal of molecular sciences

    2023  Volume 24, Issue 16

    Abstract: Preclinical evaluation of drugs in animals helps researchers to select potentially informative clinical laboratory markers for human trials. To assess the utility of animal thrombin generation (TG) assay, we studied the sensitivity of animal plasmas to ... ...

    Abstract Preclinical evaluation of drugs in animals helps researchers to select potentially informative clinical laboratory markers for human trials. To assess the utility of animal thrombin generation (TG) assay, we studied the sensitivity of animal plasmas to triggers of TG, human Tissue Factor (TF), and Activated Factor XI (FXIa). Pooled human, mouse, rat, guinea pig, rabbit, bovine, sheep, and goat plasmas were used in this study. TF- or FXIa-triggered TG and clotting were measured via fluorescence and optical density, respectively. Thrombin peak height (TPH) and time (TPT), clot time (CT), and fibrin clot density (FCD) were all analyzed. The trigger low and high sensitivity borders (LSB and HSB) for each assay parameter were defined as TF and FXIa concentrations, providing 20 and 80% of the maximal parameter value, unless the baseline (no trigger) value exceeded 20% of the maximal, in which case, LSB was derived from 120% of baseline value. Normal human samples demonstrated lower TPH HSB than most of the animal samples for both TF and FXIa. Animal samples, except mice, demonstrated lower TPT LSB for FXIa versus humans. Most rodent and rabbit samples produced baseline TG in the absence of TG triggers that were consistent with the pre-activation of blood coagulation. FCD was not sensitive to both TF and FXIa in either of the plasmas. Animal plasmas have widely variable sensitivities to human TF and FXIa, which suggests that optimization of trigger concentration is required prior to test use, and this complicates the extrapolation of animal model results to humans.
    MeSH term(s) Humans ; Animals ; Cattle ; Mice ; Rats ; Guinea Pigs ; Rabbits ; Sheep ; Factor XIa ; Thromboplastin ; Thrombin ; Plasma ; Fibrin ; Goats
    Chemical Substances Factor XIa (EC 3.4.21.27) ; Thromboplastin (9035-58-9) ; Thrombin (EC 3.4.21.5) ; Fibrin (9001-31-4)
    Language English
    Publishing date 2023-08-18
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms241612920
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  3. Article ; Online: Investigation of thrombin concentration at the time of clot formation in simultaneous thrombin and fibrin generation assays.

    Tarandovskiy, Ivan D / Surov, Stepan S / Parunov, Leonid A / Liang, Yideng / Jankowski, Wojciech / Sauna, Zuben E / Ovanesov, Mikhail V

    Scientific reports

    2024  Volume 14, Issue 1, Page(s) 9225

    Abstract: Thrombin generation (TG) and fibrin clot formation represent the central process of blood coagulation. Up to 95% of thrombin is considered to be generated after the clot is formed. However, this was not investigated in depth. In this study, we conducted ... ...

    Abstract Thrombin generation (TG) and fibrin clot formation represent the central process of blood coagulation. Up to 95% of thrombin is considered to be generated after the clot is formed. However, this was not investigated in depth. In this study, we conducted a quantitative analysis of the Thrombin at Clot Time (TCT) parameter in 5758 simultaneously recorded TG and clot formation assays using frozen plasma samples from commercial sources under various conditions of activation. These samples were supplemented with clotting factor concentrates, procoagulant lipid vesicles and a fluorogenic substrate and triggered with tissue factor (TF). We found that TCT is often close to a 10% of thrombin peak height (TPH) yet it can be larger or smaller depending on whether the sample has low or high TPH value. In general, the samples with high TPH are associated with elevated TCT. TCT appeared more sensitive to some procoagulant phenotypes than other commonly used parameters such as clotting time, TPH or Thrombin Production Rate (TPR). In a minority of cases, TCT were not predicted from TG parameters. For example, elevated TCT (above 15% of TPH) was associated with either very low or very high TPR values. We conclude that clotting and TG assays may provide complementary information about the plasma sample, and that the TCT parameter may serve as an additional marker for the procoagulant potential in plasma sample.
    MeSH term(s) Thrombin/metabolism ; Humans ; Fibrin/metabolism ; Blood Coagulation ; Blood Coagulation Tests/methods ; Thromboplastin/metabolism ; Thromboplastin/analysis
    Chemical Substances Thrombin (EC 3.4.21.5) ; Fibrin (9001-31-4) ; Thromboplastin (9035-58-9)
    Language English
    Publishing date 2024-04-22
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-023-47694-5
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  4. Article: Sources of bias and limitations of thrombinography: inner filter effect and substrate depletion at the edge of failure algorithm.

    Jackson, Joseph W / Longstaff, Colin / Woodle, Samuel A / Chang, William C / Ovanesov, Mikhail V

    Thrombosis journal

    2023  Volume 21, Issue 1, Page(s) 104

    Abstract: Background: Fluorogenic thrombin generation (TG) is a global hemostasis assay that provides an overall representation of hemostasis potential. However, the accurate detection of thrombin activity in plasma may be affected by artifacts inherent to the ... ...

    Abstract Background: Fluorogenic thrombin generation (TG) is a global hemostasis assay that provides an overall representation of hemostasis potential. However, the accurate detection of thrombin activity in plasma may be affected by artifacts inherent to the assay-associated fluorogenic substrate. The significance of the fluorogenic artifacts or their corrections has not been studied in hemophilia treatment applications.
    Methods: We sought to investigate TG in hemophilia plasma samples under typical and worst-case fluorogenic artifact conditions and assess the performance of artifact correction algorithms. Severe hemophilic plasma with or without added Factor VIII (FVIII) was evaluated using commercially available and in-house TG reagents, instruments, and software packages. The inner filter effect (IFE) was induced by spiking elevated amounts of fluorophore 7-amino-4-methylcoumarin (AMC) into plasma prior to the TG experiment. Substrate consumption was modeled by adding decreasing amounts of Z-Gly-Gly-Arg-AMC (ZGGR-AMC) to plasma or performing TG in antithrombin deficient plasma.
    Results: All algorithms corrected the AMC-induced IFE and antithrombin-deficiency induced substrate consumption up to a certain level of either artifact (edge of failure) upon which TG results were not returned or overestimated. TG values in FVIII deficient (FVIII-DP) or supplemented plasma were affected similarly. Normalization of FVIII-DP resulted in a more accurate correction of substrate artifacts than algorithmic methods.
    Conclusions: Correction algorithms may be effective in situations of moderate fluorogenic substrate artifacts inherent to highly procoagulant samples, but correction may not be required under typical conditions for hemophilia treatment studies if TG parameters can be normalized to a reference plasma sample.
    Language English
    Publishing date 2023-10-04
    Publishing country England
    Document type Journal Article
    ZDB-ID 2118392-2
    ISSN 1477-9560
    ISSN 1477-9560
    DOI 10.1186/s12959-023-00549-5
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  5. Article ; Online: Considerations on activity assay discrepancies in factor VIII and factor IX products.

    Ovanesov, Mikhail V / Jackson, Joseph W / Golding, Basil / Lee, Timothy K

    Journal of thrombosis and haemostasis : JTH

    2021  Volume 19, Issue 9, Page(s) 2102–2111

    Abstract: New modified coagulation factor VIII (FVIII) and factor IX (FIX) products have been designed to improve the treatment of individuals with hemophilia A and B by increasing the interval between dosing. Although these FVIII and FIX molecules have been ... ...

    Abstract New modified coagulation factor VIII (FVIII) and factor IX (FIX) products have been designed to improve the treatment of individuals with hemophilia A and B by increasing the interval between dosing. Although these FVIII and FIX molecules have been structurally modified to improve the circulation time, the changes have also influenced their behavior in functional assays in comparison with traditional plasma-derived or recombinant coagulation factors. The assignment of potencies for these products can be problematic because discordance in factor activity values between the commonly used one-stage clotting and chromogenic substrate assays is often observed. Discrepancies in potency assay values also exist when different assay kits and reagents are used in the same assay type. Ideally, all FVIII and FIX products should be calibrated against the World Health Organization (WHO) International Standards (IS) because the assignment of potencies in international units (IU) helps maintain treatment tradition and meaningful references for manufacturers, patients, and clinicians. The discrepant measurements, attributed to the modified structural and functional properties of these products, are manifested in their lack of commutability with the WHO IS for FVIII or FIX. Herein, we discuss the considerations upon which an assay is chosen for potency assignment and postadministration monitoring of a new factor product, which include the validity of the assay calibrated with the IS, the meaning of the potency values in IU, standards of care for patients, clinical relevance between the assigned potency value and recovery value from clinical laboratories, and patient safety.
    MeSH term(s) Blood Coagulation Tests ; Chromogenic Compounds ; Factor IX ; Factor VIII ; Hemophilia A/diagnosis ; Hemophilia A/drug therapy ; Humans
    Chemical Substances Chromogenic Compounds ; Factor VIII (9001-27-8) ; Factor IX (9001-28-9)
    Language English
    Publishing date 2021-07-20
    Publishing country England
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 2112661-6
    ISSN 1538-7836 ; 1538-7933
    ISSN (online) 1538-7836
    ISSN 1538-7933
    DOI 10.1111/jth.15425
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    Zs.MO 295: Show issues

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  6. Article ; Online: Isolated Variable Domains of an Antibody Can Assemble on Blood Coagulation Factor VIII into a Functional Fv-like Complex.

    Shestopal, Svetlana A / Parunov, Leonid A / Olivares, Philip / Chun, Haarin / Ovanesov, Mikhail V / Pettersson, John R / Sarafanov, Andrey G

    International journal of molecular sciences

    2022  Volume 23, Issue 15

    Abstract: ... where both subunits (V ...

    Abstract Single-chain variable fragments (scFv) are antigen-recognizing variable fragments of antibodies (FV) where both subunits (V
    MeSH term(s) Antigens ; Baculoviridae/metabolism ; Factor VIII/genetics ; Factor VIII/metabolism ; Low Density Lipoprotein Receptor-Related Protein-1 ; Single-Chain Antibodies/genetics ; Single-Chain Antibodies/metabolism ; Thrombin
    Chemical Substances Antigens ; Low Density Lipoprotein Receptor-Related Protein-1 ; Single-Chain Antibodies ; Factor VIII (9001-27-8) ; Thrombin (EC 3.4.21.5)
    Language English
    Publishing date 2022-07-23
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms23158134
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  7. Article ; Online: Fluorescence artifact correction in the thrombin generation assay: Necessity for correction algorithms in procoagulant samples.

    Chang, William C / Jackson, Joseph W / Machlus, Kellie R / Wolberg, Alisa S / Ovanesov, Mikhail V

    Research and practice in thrombosis and haemostasis

    2021  Volume 5, Issue 3, Page(s) 447–455

    Abstract: ... increases in blood coagulation factors I, V, VIII, IX, X, and XI, or prothrombin in the presence or absence ...

    Abstract Introduction: The thrombin generation (TG) test is a global hemostasis assay sensitive to procoagulant conditions. However, some TG assays may underestimate elevated TG when the thrombin fluorogenic substrate is depleted or fluorescence is attenuated by the inner filter effect (IFE).
    Objectives: We sought to elucidate the extent to which procoagulant conditions require correcting for fluorogenic substrate depletion and/or IFE.
    Methods: We analyzed corrections for substrate depletion and IFE and their effect on TG parameters in plasma samples with elevated blood coagulation factors in the presence or absence of thrombomodulin via commercial calibrated automated thrombogram (CAT) platform and in-house software capable of internal thrombin calibration with or without CAT-like artifact correction.
    Results: Elevated thrombin peak height (TPH) and endogenous thrombin potential (ETP) were detected with 2× and 4× increases in blood coagulation factors I, V, VIII, IX, X, and XI, or prothrombin in the presence or absence of artifact correction. The effect of the CAT algorithm was evident in TG curves from both low procoagulant (thrombomodulin-supplemented) and procoagulant (factor-supplemented) plasma samples. However, in all samples, with the exception of elevated prothrombin, CAT's correction was small (<10%) and did not affect detection of procoagulant samples versus normal plasma. For elevated prothrombin samples, uncorrected TPH or ETP values were underestimated, and CAT correction produced drastically elevated TG curves.
    Conclusions: Our data suggest that correction for substrate consumption and IFE, as offered by the CAT algorithm, is critical for detecting a subset of extremely procoagulant samples, such as elevated prothrombin, but is not necessary for all other conditions, including elevated factors XI and VIII.
    Language English
    Publishing date 2021-03-26
    Publishing country United States
    Document type Journal Article
    ISSN 2475-0379
    ISSN (online) 2475-0379
    DOI 10.1002/rth2.12499
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  8. Article ; Online: Effect of pH on thrombin activity measured by calibrated automated thrombinography.

    Jackson, Joseph W / Surov, Stepan S / Liang, Yideng / Parunov, Leonid A / Ovanesov, Mikhail V

    Research and practice in thrombosis and haemostasis

    2020  Volume 4, Issue 5, Page(s) 944–945

    Language English
    Publishing date 2020-06-12
    Publishing country United States
    Document type Journal Article
    ISSN 2475-0379
    ISSN (online) 2475-0379
    DOI 10.1002/rth2.12370
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  9. Article ; Online: Thrombin generation assay modifications needed for its application to monitoring of replacement therapy for haemophilia.

    Parunov, Leonid A / Surov, Stepan S / Chattopadhyay, Maitreyi / Liang, Yideng / Lee, Timothy K / Ovanesov, Mikhail V

    Haemophilia : the official journal of the World Federation of Hemophilia

    2020  Volume 27, Issue 1, Page(s) e129–e132

    MeSH term(s) Blood Coagulation ; Hemophilia A/drug therapy ; Hemophilia B/diagnosis ; Hemophilia B/drug therapy ; Humans ; Thrombin
    Chemical Substances Thrombin (EC 3.4.21.5)
    Language English
    Publishing date 2020-09-08
    Publishing country England
    Document type Letter
    ZDB-ID 1229713-6
    ISSN 1365-2516 ; 1351-8216 ; 1355-0691
    ISSN (online) 1365-2516
    ISSN 1351-8216 ; 1355-0691
    DOI 10.1111/hae.14024
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    Zs.A 4249: Show issues Location:
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    Zs.MO 450: Show issues

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  10. Article ; Online: Thrombogenic potential of picomolar coagulation factor XIa is mediated by thrombin wave propagation.

    Parunov, Leonid A / Liang, Yideng / Lu, Qijin / Shibeko, Alexey M / Tucker, Erik I / Lee, Timothy K / Ataullakhanov, Fazoil I / Scott, Dorothy E / Ovanesov, Mikhail V

    Blood advances

    2023  Volume 7, Issue 11, Page(s) 2622–2631

    Abstract: Inhibitors of coagulation factor XIa (FXIa) are currently being investigated as potential anticoagulant therapies. We hypothesize that circulating FXIa could be a potential target for these therapies. Using previous analyses of FXIa impurities in immune ... ...

    Abstract Inhibitors of coagulation factor XIa (FXIa) are currently being investigated as potential anticoagulant therapies. We hypothesize that circulating FXIa could be a potential target for these therapies. Using previous analyses of FXIa impurities in immune globulin products involved in thrombotic adverse events, we estimated that picomolar levels of FXIa can be thrombogenic. In an in vitro clot-growth assay, 0.1-3 pM of FXIa did not, by itself, activate clotting but increased the size of growing clots. Spatio-temporal reconstruction of thrombin activity inside the clot revealed that FXIa's effect was limited to the clot-plasma interface, in which FXIa produced a taller than standard wave of thrombin. Factor-depleted plasma and a panel of selective anti-FXIa antibodies showed that exogenous FXIa effects are (1) blocked by anti-FXIa antibodies, (2) independent of FXI activation inside the clot, and (3) larger than the contribution of in situ FXIa. In a thrombin generation (TG) assay, picomolar FXIa did not initiate TG but rather promoted TG triggered by tissue factor or thrombin, suggesting that the effect of FXIa on the thrombin wave is mediated by the elevation of thrombin-triggered TG. In circulating bovine blood, low doses of human FXIa did not initiate clotting but increased the size of stenosis-triggered thrombi. FXIa injection in mice enhanced TG in plasma for at least 6 hours ex vivo, confirming the persistence of circulating FXIa. Our findings suggest that picomolar levels of circulating FXIa may not be able to initiate thrombosis but can facilitate thrombus growth through the facilitation of TG inside the clot.
    MeSH term(s) Animals ; Cattle ; Humans ; Mice ; Factor XIa ; Thrombin ; Blood Coagulation ; Thrombosis/etiology ; Anticoagulants
    Chemical Substances Factor XIa (EC 3.4.21.27) ; Thrombin (EC 3.4.21.5) ; Anticoagulants
    Language English
    Publishing date 2023-02-01
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Research Support, Non-U.S. Gov't
    ZDB-ID 2915908-8
    ISSN 2473-9537 ; 2473-9529
    ISSN (online) 2473-9537
    ISSN 2473-9529
    DOI 10.1182/bloodadvances.2022008743
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