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Journal articles on the topic 'Blood – Coagulation'

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Published: 4 June 2021
Last updated: 29 July 2024

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1

Maslov, Artem, and Marta Mashevska. "BLOOD COAGULATION MONITORING SYSTEM." Measuring Equipment and Metrology 81, no. 3 (2020): 24–27. http://dx.doi.org/10.23939/istcmtm2020.03.024.

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2

Mann, Kenneth G. "Blood Coagulation." Alcoholism: Clinical and Experimental Research 23, no. 6 (June 1999): 1111–13. http://dx.doi.org/10.1111/j.1530-0277.1999.tb04233.x.

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3

Norris, Lucy A. "Blood coagulation." Best Practice & Research Clinical Obstetrics & Gynaecology 17, no. 3 (June 2003): 369–83. http://dx.doi.org/10.1016/s1521-6934(03)00014-2.

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4

Chris Ludlam. "Blood Coagulation." Clinica Chimica Acta 186, no. 3 (January 1990): 402–3. http://dx.doi.org/10.1016/0009-8981(90)90329-q.

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5

Dahlbäck, Björn. "Blood coagulation." Lancet 355, no. 9215 (May 2000): 1627–32. http://dx.doi.org/10.1016/s0140-6736(00)02225-x.

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6

Littlewood, J., and S. Bevan. "Canine blood coagulation." Veterinary Record 125, no. 4 (July 22, 1989): 97. http://dx.doi.org/10.1136/vr.125.4.97-a.

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7

Jamnicki, Marina, Andreas Zollinger, Burkhardt Seifert, Dragoljub Popovic, Thomas Pasch, and Donat R. Spahn. "Compromised Blood Coagulation." Anesthesia & Analgesia 87, no. 5 (November 1998): 989–93. http://dx.doi.org/10.1097/00000539-199811000-00002.

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8

Jamnicki, Marina, Andreas Zollinger, Burkhardt Seifert, Dragoljub Popovic, Thomas Pasch, and Donat R. Spahn. "Compromised Blood Coagulation." Anesthesia & Analgesia 87, no. 5 (November 1998): 989–93. http://dx.doi.org/10.1213/00000539-199811000-00002.

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9

Pryzdial, Edward L. G., Frank M. H. Lee, Bryan H. Lin, Rolinda L. R. Carter, Tseday Z. Tegegn, and Mark J. Belletrutti. "Blood coagulation dissected." Transfusion and Apheresis Science 57, no. 4 (August 2018): 449–57. http://dx.doi.org/10.1016/j.transci.2018.07.003.

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10

Krishnaswamy, Sriram. "Supercharged blood coagulation." Blood 113, no. 9 (February 26, 2009): 1873–74. http://dx.doi.org/10.1182/blood-2008-11-188532.

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11

Kasireddy, Nithya, Elizabeth M. Cummins, Huy Q. Pham, Amina Rafique, and Damir B. Khismatullin. "Small-Volume Noncontact Assessment of Blood Coagulation Via Acoustic Tweezing Coagulometry." Blood 138, Supplement 1 (November 5, 2021): 3178. http://dx.doi.org/10.1182/blood-2021-153819.

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Abstract Introduction: Blood coagulation analysis is routinely performed to assess bleeding and thrombotic risks in surgical and critical care patients as well as in patients with diseases that cause coagulation abnormalities (e.g., hemophilia, thrombophilia and sickle cell disease). Majority of coagulation assays are based on photo-optical measurement of coagulation onset in blood plasma such as prothrombin time (PT), international normalized ratio (INR), and activated partial thromboplastin time (aPTT) and viscoelastic measurement of coagulating whole blood, often referred to as "global coagulation analysis", mostly done by thromboelastography (TEG, ROTEM) but they require large sample volume (> 0.5ml) requiring venipuncture, have poor standardization, and are unreliable tools to predict bleeding/thrombotic risk. Acoustic tweezing coagulometry (ATC) is an innovative noncontact drop-of-blood coagulation analysis technique that can perform both photo-optical and viscoelastic coagulation analysis with a sample volume as low as 4 μl to provide a comprehensive set of clinically relevant coagulation parameters such as blood viscosity, elasticity, reaction time, clotting rate, maximum clot stiffness, fibrin formation rate and cross-linking kinetics helpful for diagnosis and prediction of bleeding and thrombotic risks. ATC is particularly valuable for the pediatric patients as it enables safe and reliable point of care coagulation assessment with minimal sample volume. Materials and Methods: In this project, we demonstrate the feasibility of ATC for coagulation analysis by validation and standardization of the technique using whole blood collected from healthy adult volunteers and commercially purchased blood plasma. Further, we present the ability of ATC to assess bleeding risk in commercial blood plasma with coagulation FVIII deficiency with and without inhibitors, as well as whole blood collected from pediatric Hemophilia A patients without inhibitors. The time dependent changes in elasticity (elastic tweezograph, Figure 1A) and viscosity (viscous tweezograph, Figure 1B) of coagulating blood plasma or whole blood sample are used to extract the following coagulation parameters: clot initiation time (CIT), clotting rate (CR), clotting time (CT), time to firm clot formation (TFCF), and maximum clot stiffness (MCS) from elastic tweezograph; reaction time (RT), fibrin formation rate (FFR), and maximum fibrin level (MFL) from viscous tweezograph. Results and Discussion: Figure 1C shows the elastic tweezograph and figure 1D shows the viscous tweezograph of the healthy plasma, plasma with coagulation FVIII deficieny and plasma with inhibitors for coagulation FVIII activated via the intrinsic pathway of coagulation. The tweezographs suggest that the clot initiation is faster in healthy plasma compared to the FVIII deficient plasma and FVIII inhibitor plasma. The clotting rate is highest for healthy plasma followed by the FVIII deficient plasma and is the lowest for the plasma with FVIII inhibitors suggesting a delayed clot formation in the deficient and inhibitor groups. They all reach a similar final clot stiffness, but the time to firm clot formation is least in healthy plasma as expected and increases in the FVIII deficient group and further increases in the FVIII inhibitor group. Conclusions: Acoustic tweezing coagulometry can successfully measure the viscosity, elasticity and coagulation of whole blood and blood plasma with only a drop of the sample. This technique can successfully assess the bleeding risks in pediatric and adult patients with Hemophilia. Acknowledgements: This study has been supported by American Heart Association pre doctoral fellowship 20PRE35210991, U.S. National Science Foundation grant 1438537, American Heart Association Grant-in-Aid 13GRNT17200013, and Tulane University intramural grants. The acoustic tweezing technology is protected by pending patents PCT/US14/55559, PCT/US2018/014879 and PCT/US21/15336. Figure 1 Figure 1. Disclosures Kasireddy: Levisonics Inc.: Current Employment. Rafique: Pfizer Inc.: Consultancy; CSL Behring: Consultancy; HEMA Biologics: Consultancy. Khismatullin: Levisonics Inc.: Current equity holder in publicly-traded company; Levisonics Inc.: Patents & Royalties: PCT/US14/55559 (pending); Levisonics Inc.: Patents & Royalties: PCT/US2018/014879 (issued) ; Levisonics Inc.: Patents & Royalties: PCT/US21/15336 (pending)..
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12

Siroka, Z., B. Krocilova, J. Pikula, H. Bandouchova, L. Peckova, and F. Vitula. "Blood coagulation parameters in fallow deer (Dama dama)." Veterinární Medicína 56, No. 3 (March 24, 2011): 119–22. http://dx.doi.org/10.17221/3160-vetmed.

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There are frequent reports from around the world of wild animals being poisoned with anticoagulants. Granulated baits can result in primary or secondary poisoning of non-target animals. Moreover, there are several diseases including infections that influence haemostasis in wild animals. The present study focused on fallow deer (Dama dama) for which insufficient data on physiological values of coagulation parameters are available. Six parameters of blood coagulation were established in clinically normal fallow deer from a game enclosure in North Moravia (Czech Republic). The fibrinogen content of 1.94 g/l is in agreement with the results obtained by other authors. Factor VIII and IX concentrations amounted to 198.42% and 169.91% of human concentration of these parameters in blood. These have never before been measured for fallow deer, but most animal species have concentrations of these factors higher than humans. Prothrombin time (PT), average activated partial thromboplastin time (APTT), and thrombin time (TT) were assessed as 20.99 s, 33.76 s, and 24.78 s, respectively. Prothrombin time assessed in the present study was longer compared to available data, while APTT is in agreement with the previous data. Thrombin time value is a new piece of information and is comparable with TT values obtained in other ruminants. The possible explanation for the prolonged PT may be the stress associated with yarding and handling the animals which is reported to cause haemorrhages or changes in haemostatic parameters in deer. Interestingly, males had significantly longer clotting times compared to females.
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13

Denis Solomons, Hilary. "Hereditary disorders of blood coagulation factors amongst Jews!" Journal of Clinical Research and Reports 5, no. 3 (September 14, 2020): 01. http://dx.doi.org/10.31579/2690-1919/113.

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This is picked up on routine bloods such as partial thromboplastin times. The prothrombin time is usually normal. There is no excess bleeding after trauma. They may however still bleed excessively after surgery. In terms of treatment or therapy the factor XI level must be kept at greater than 30 % with fresh frozen plasma 5-20 ml./kg./ day. The inheritance is autosomal recessive.In Israel the incidence is 8% amongst Ashkenazi Jews. FactorXI deficiency is also known as; Rosenthal Syndrome or Haemophilia C. Sometimes the child may bleed excessively e.g. at circumcision but they do not bleed as severely as haemophiliacs (factor VIII deficiency) and rarely present with haemarthroses. Haemorrhage is usually from mucousal surfaces.
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14

Mackman, Nigel, and George E. Davis. "Blood Coagulation and Blood Vessel Development." Arteriosclerosis, Thrombosis, and Vascular Biology 31, no. 11 (November 2011): 2364–66. http://dx.doi.org/10.1161/atvbaha.111.236703.

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15

Okazaki, Masako, Hideharu Sakamoto, Makoto Suzuki, and Katsuji Oguchi. "Effects of Single and Multiple Moxibustions on Activity of Platelet Function, Blood Coagulation and Fibrinolysis in Mice." American Journal of Chinese Medicine 18, no. 01n02 (January 1990): 77–85. http://dx.doi.org/10.1142/s0192415x90000113.

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The effects of single and multiple moxibustions on platelet function, blood coagulation and fibrinolytic activity in ddY mice were studied. The increase in platelet aggregation and ATP-release after a single moxibustion was dependent on moxa weight and the kind of platelet stimulus. Blood coagulative activity tended to increase in the early phase after a single moxibustion. However, multiple moxibustions maintained the homeostasis on blood coagulation and fibrinolytic activiity. This investigation suggests that the effects of moxibustion on platelet functions and coagulative and fibrinolytic activities cause an enhancement of the phagocytic activity in the host defense mechanism.
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16

Castellone, Donna D. "Coagulation for Blood Bankers." Immunohematology 22, no. 2 (2020): 85–88. http://dx.doi.org/10.21307/immunohematology-2019-360.

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17

SUZUKI, KOJI. "Blood coagulation control proteins." Nihon Naika Gakkai Zasshi 83, no. 4 (1994): 646–53. http://dx.doi.org/10.2169/naika.83.646.

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18

PÄLOS, L. A. "Respiration and blood-coagulation." Acta Medica Scandinavica 134, no. 3 (April 24, 2009): 221–24. http://dx.doi.org/10.1111/j.0954-6820.1949.tb06629.x.

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19

MOSONYI, L., L. Á. PÁLOS, and J. KOMAROMY. "Penicillin and Blood-Coagulation." Acta Medica Scandinavica 135, no. 6 (April 24, 2009): 458–64. http://dx.doi.org/10.1111/j.0954-6820.1949.tb09607.x.

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20

Tobias, Mitchell David, Michael A. Pilla, Celia Rogers, and David R. Jobes. "Lidocaine Inhibits Blood Coagulation." Anesthesia & Analgesia 82, no. 4 (April 1996): 766–69. http://dx.doi.org/10.1097/00000539-199604000-00016.

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21

Porwes, C. V. "Coagulation and Blood Transfusion." Blood Coagulation & Fibrinolysis 3, no. 3 (June 1992): 344. http://dx.doi.org/10.1097/00001721-199206000-00015.

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22

Butenas, S., C. van ʼt Veer, K. Cawthern, K. E. Brummel, and K. G. Mann. "Models of blood coagulation." Blood Coagulation & Fibrinolysis 11 (April 2000): S9—S13. http://dx.doi.org/10.1097/00001721-200004001-00003.

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23

Tobias, Mitchell David, Michael A. Pilla, Celia Rogers, and David R. Jobes. "Lidocaine Inhibits Blood Coagulation." Anesthesia & Analgesia 82, no. 4 (April 1996): 766–69. http://dx.doi.org/10.1213/00000539-199604000-00016.

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24

Muszbek, László, Vivien C. Yee, and Zsuzsa Hevessy. "Blood Coagulation Factor XIII." Thrombosis Research 94, no. 5 (June 1999): 271–305. http://dx.doi.org/10.1016/s0049-3848(99)00023-7.

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25

Stubbs, James R. "Coagulation for Blood Bankers." Clinics in Laboratory Medicine 16, no. 4 (December 1996): 837–71. http://dx.doi.org/10.1016/s0272-2712(18)30242-7.

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26

Green, David. "Overview of Blood Coagulation." Hemodialysis International 5, no. 1 (January 2001): 70–73. http://dx.doi.org/10.1111/hdi.2001.5.1.70.

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27

Riddel, James P., Bradley E. Aouizerat, Christine Miaskowski, and David P. Lillicrap. "Theories of Blood Coagulation." Journal of Pediatric Oncology Nursing 24, no. 3 (May 2007): 123–31. http://dx.doi.org/10.1177/1043454206298693.

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28

Newland, James R. "Blood coagulation: A review." American Journal of Obstetrics and Gynecology 156, no. 6 (June 1987): 1420–22. http://dx.doi.org/10.1016/0002-9378(87)90010-x.

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29

Boccaccio, C., and E. Medico. "Cancer and blood coagulation." Cellular and Molecular Life Sciences 63, no. 9 (April 14, 2006): 1024–27. http://dx.doi.org/10.1007/s00018-005-5570-9.

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30

Mann, Kenneth G., Kathleen Brummel-Ziedins, Thomas Orfeo, and Saulius Butenas. "Models of blood coagulation." Blood Cells, Molecules, and Diseases 36, no. 2 (March 2006): 108–17. http://dx.doi.org/10.1016/j.bcmd.2005.12.034.

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31

KAIBARA, M. "Rheology of blood coagulation." Biorheology 33, no. 2 (March 1996): 101–17. http://dx.doi.org/10.1016/0006-355x(96)00010-8.

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32

Esmon, Charles T. "Regulation of blood coagulation." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1477, no. 1-2 (March 2000): 349–60. http://dx.doi.org/10.1016/s0167-4838(99)00266-6.

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33

Undas, Anetta, Kathleen E. Brummel-Ziedins, and Kenneth G. Mann. "Statins and Blood Coagulation." Arteriosclerosis, Thrombosis, and Vascular Biology 25, no. 2 (February 2005): 287–94. http://dx.doi.org/10.1161/01.atv.0000151647.14923.ec.

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34

Oliva, Maria Luiza Vilela, Ingrid Dreveny, and Jonas Emsley. "Exosites expedite blood coagulation." Journal of Biological Chemistry 295, no. 45 (November 6, 2020): 15208–9. http://dx.doi.org/10.1074/jbc.h120.016301.

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A careful balance between active-site and exosite contributions is critically important for the specificity of many proteases, but this balance is not yet defined for some of the serine proteases that serve as coagulation factors. Basavaraj and Krishnaswamy have closed an important gap in our knowledge of coagulation factor X activation by the intrinsic Xase complex by showing that exosite binding plays a critical role in this process, which they describe as a “dock and lock.” This finding not only significantly enhances our understanding of this step in the coagulation cascade and highlights parallels with the prothrombinase complex, but will also provide a novel rationale for inhibitor development in the future.
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35

Schenone, Monica, Barbara C. Furie, and Bruce Furie. "The blood coagulation cascade." Current Opinion in Hematology 11, no. 4 (July 2004): 272–77. http://dx.doi.org/10.1097/01.moh.0000130308.37353.d4.

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36

Bloom, A. L. "Physiology of Blood Coagulation." Pathophysiology of Haemostasis and Thrombosis 20, no. 1 (1990): 14–29. http://dx.doi.org/10.1159/000216159.

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37

Dobrovol'skii, N. A., P. R. Kostritso, T. A. Labinskaya, V. V. Makarov, A. S. Parfenov, and A. V. Peshkov. "A blood coagulation analyzer." Biomedical Engineering 33, no. 1 (January 1999): 44–47. http://dx.doi.org/10.1007/bf02388386.

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38

Belovezhdov, N., R. Robeva, and V. Genova. "Blood coagulation in glomerulonephritis." International Urology and Nephrology 18, no. 2 (June 1986): 193–203. http://dx.doi.org/10.1007/bf02082608.

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39

Green, David. "Overview of Blood Coagulation." Hemodialysis International 5, no. 1 (January 2001): 70–73. http://dx.doi.org/10.1002/hdi.2001.5.1.70.

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40

Davie, Earl W. "Introduction to the blood coagulation cascade and cloning of blood coagulation factors." Journal of Protein Chemistry 5, no. 4 (August 1986): 247–53. http://dx.doi.org/10.1007/bf01025423.

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41

Johnson, K., L. Aarden, Y. Choi, E. De Groot, and A. Creasey. "The proinflammatory cytokine response to coagulation and endotoxin in whole blood." Blood 87, no. 12 (June 15, 1996): 5051–60. http://dx.doi.org/10.1182/blood.v87.12.5051.bloodjournal87125051.

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Acute inflammatory illnesses, including the sepsis syndrome, often include a component of coagulation. A human whole blood culture system was developed so that the relationship between coagulation activation and cytokine responses in the presence or absence of lipopolysaccharide (LPS) could be evaluated. In the absence of LPS stimulation, coagulation activation resulted in a novel pattern of cytokine production. During a 4-hour culture of coagulating blood, significant production of interleukin-8 (IL-8; >2,000 pg/mL) was observed, whereas other proinflammatory cytokines including IL-1 beta, IL-6, or tumor necrosis factor a were undetectable or less than 35 pg/mL. The cytokine profile was distinct from that of fully anticoagulated, LPS-stimulated blood, which showed levels of all the indicated proinflammatory cytokines > or = 2,000 pg/mL over the same time period. Over 24 to 48 hours, the coagulation-induced cytokine response was characterized by marked and sustained IL-8 production, limited IL-6 generation (with kinetics delayed relative to IL-8), and minimal or undetectable tumor necrosis factor alpha levels. The magnitude of the whole blood IL-8 response correlated with the level of coagulation activation as determined by measurement of thrombin-antithrombin III complex formation. The combined stimuli of coagulation activation and LPS challenge induced a synergistic enhancement of IL-8 production but not of IL-6. Coagulation-induced cytokine production and the synergistic production of IL-8 by coagulation and LPS could be attenuated by hirudin or tissue factor pathway inhibitor (TFPI). Studies to elucidate mechanisms implicated (1) the TFPI third Kunitz and carboxy-terminus as important structural components for TFPI regulation of coagulation activation and (2) thrombin as a candidate mediator of the mononuclear cell cytokine response to coagulation activation. In summary, a unique aspect of the crosstalk between the coagulation and cytokine cascades in whole blood is shown with the identification of IL-8 as a key proinflammatory participant.
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42

Chabin, I. A., N. A. Podoplelova, and M. A. Panteleev. "Red blood cells contribution in blood coagulation." Pediatric Hematology/Oncology and Immunopathology 21, no. 3 (October 15, 2022): 136–41. http://dx.doi.org/10.24287/1726-1708-2022-21-3-136-141.

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For a long time, red blood cells have been known to have a procoagulant effect on hemostatic system. This effect was usually ascribed to either general increase of blood viscosity due to increased hematocrit value, RBCs' transport-enhancing effect on platelets adhesion under flow conditions. It is known that red blood cells can have a procoagulant effect on the hemostasis system. This effect is usually explained either by a general increase in blood viscosity due to an increase in hematocrit, or by the effect of red blood cells on the transport of platelets to the vessel wall and their further adhesion. However, recent studies indicate that the role of red blood cells in blood coagulation is much wider. In this review, we will consider the main mechanisms currently known, through which red blood cells can influence the processes of hemostasis and thrombosis in normal and pathological conditions.
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43

ROATH, STUART, and JOHN L. FRANCIS. "Normal Blood Coagulation, Fibrinolysis, and Natural Inhibitors of Coagulation." International Anesthesiology Clinics 23, no. 2 (1985): 23–36. http://dx.doi.org/10.1097/00004311-198523020-00004.

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44

Bevers, Edouard, Theo Lindhout, and Johan Heemskerk. "Platelet Activation and Blood Coagulation." Thrombosis and Haemostasis 88, no. 08 (2002): 186–93. http://dx.doi.org/10.1055/s-0037-1613209.

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SummaryPlatelet activation and blood coagulation are complementary, mutually dependent processes in haemostasis and thrombosis. Platelets interact with several coagulation factors, while the coagulation product thrombin is a potent platelet-activating agonist. Activated platelets come in a procoagulant state after a prolonged elevation in cytosolic [Ca2+]i. Such platelets, e. g. when adhering to collagen via glycoprotein VI, expose phosphatidylserine (PS) at their outer surface and produce (PS-exposing) membrane blebs and microvesicles. Inhibition of aminophospholipid translocase and activation of phospholipid scramblase mediate the exposure of PS, whereas calpain-mediated protein cleavage leads to membrane blebbing and vesiculation. Surface-exposed PS strongly propagates the coagulation process by facilitating the assembly and activation of tenase and prothrombinase complexes. Factor IXa and platelet-bound factor Va support these activities. In addition, platelets can support the initiation phase of coagulation by providing binding sites for prothrombin and factor XI. They thereby take over the initiating role of tissue factor and factor VIIa in coagulation activation.
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45

Romanenko, S. Yu, K. V. Vilchevska, I. O. Bakhchivandzhi, and Yu V. Martinenko. "A rare disorder of blood coagulation." Modern pediatrics. Ukraine, no. 6(126) (October 29, 2022): 97–100. http://dx.doi.org/10.15574/sp.2022.126.97.

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The problem of impaired hemostasis remains relevant even today. Rare bleeding disorders that cause life-threatening bleeding in patient are often overlooked by clinicians. Rare blood coagulation disorders are a genetically determined group of coagulopathies caused by a deficiency of blood plasma proteins involved in hemostasis, as well as a deficiency of fibrinogen, prothrombin, blood coagulation factor V (FV), blood coagulation factors V and VIII (FV+FVIII), blood coagulation factor VII (FVII), blood coagulation factor X (FX), blood coagulation factor XI (FXI), blood coagulation factor XII (FXII), blood coagulation factor XIII (FXIII), which are clinically are manifested by bleeding. The amount of the factor determines not only the nature of bleeding, but also their severity and prognosis for the disease. In such patients, the general hemostatic balance is important, since the level of each blood coagulation factor and the general control of hemostasis, which can determine the risk of bleeding, remain important. Purpose - to draw the attention of doctors of various specialties to the problem of clinical manifestations of rare hereditary disorders of blood coagulation, which can be accompanied by bleeding that poses a threat to the health and life of patient. Clinical case. A clinical case is presented that illustrates the course of a rare blood coagulation disorder in children from one family, where a comprehensive diagnostic search was conducted by doctors of various specialties to establish a final diagnosis. Conclusions. Rare blood coagulation disorders are a pathology that is not often found in the population, but clinical symptoms can have negative consequences for a person's health and life. Children with various manifestations of hemorrhagic syndrome need a thorough diagnostic examination in specialized laboratories. Physicians of related specialties should look for a possible rare deficiency of the coagulation factor in early and late complications in the postoperative period or after medical manipulations. It is necessary to remember the hereditary genesis of this pathology and examine all family members. The research was carried out in accordance with the principles of the Helsinki Declaration. The informed consent of the patient was obtained for conducting the studies. No conflict of interests was declared by the authors.
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46

Korolova, D. S., O. V. Hornytska, A. S. Lavrik, N. M. Druzhyna, N. Prysyazhna, and T. M. Platonova. "Characterization of the blood coagulation system in morbidly obese patients." Ukrainian Biochemical Journal 95, no. 4 (September 11, 2023): 3–9. http://dx.doi.org/10.15407/ubj95.04.003.

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Obesity is a complex metabolic disorder that can be followed by blood coagulation disorders, athero­sclerosis and atherothrombosis. In the present work, the levels of fibrinogen, soluble fibrin, D-dimer as well as protein C were measured in the blood plasma of 24 morbidly obese patients (the body mass index exceeds 40 kg/m2) to evaluate the risk of prothrombotic state. The study showed that near by 80% of patients had substantially increased fibrinogen concentration, 33% had increased concentration of soluble fibrin, 42% had increased level of D-dimer in blood plasma as compared to control. According to the results of individual analysis, the high level of fibrinogen and soluble fibrin while reduced protein C indicated the threat of thrombosis, which requires complex diagnostics to be identified. Therefore, simultaneous quantification of hemostatic system biomarkers in the blood plasma is the confident way to predict the risk of thrombotic complications in morbidly obese patients. Keywords: D-dimer, hemostasis, obesity, protein C, soluble fibrin, thrombosis
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47

Shibeko, A. M., A. N. Balandina, N. A. Podoplelova, and M. A. Panteleev. "Current trends in blood coagulation studies." Pediatric Hematology/Oncology and Immunopathology 19, no. 3 (October 9, 2020): 144–50. http://dx.doi.org/10.24287/1726-1708-2020-19-3-144-150.

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Blood coagulation occurs in flow or stasis conditions, it involves components of cell hemostasis and enzymatic cascades of reactions; it serves to stop bleeding yet it can lead to life-threatening blood thrombi. Despite the fact that a complete list of coagulation proteins was well known for decades, in recent years numerous facts has accumulated about its structure and regulation. All that has led to the creation of new methods for diagnosing of blood coagulation disorders and methods for their correction. Congenital and acquired coagulation disorders are still an acute clinical problem. This review shows modern ideas about the structure and functioning of the blood coagulation system in various conditions.
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48

Kojima, Tetsuhito. "Blood coagulation regulation and thrombosis." Japanese Journal of Thrombosis and Hemostasis 31, no. 4 (2020): 420–31. http://dx.doi.org/10.2491/jjsth.31.420.

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49

Ernst, E., A. Matrai, and J. Dormandy. "Shear dependence of blood coagulation." Clinical Hemorheology and Microcirculation 4, no. 4 (December 9, 2016): 395–99. http://dx.doi.org/10.3233/ch-1984-4403.

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50

Beraia, Merab, and Guram Beraia. "Electromagnetism, Blood Flow and Coagulation." Journal of Biomedical Science and Engineering 15, no. 07 (2022): 187–97. http://dx.doi.org/10.4236/jbise.2022.157017.

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