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Journal articles on the topic 'Blood plasma'

Author: Grafiati

Published: 4 June 2021

Last updated: 28 July 2024

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1

Vahidi, Mehrnoosh, Hamidreza Fallah Haghmohammadi, Masoumesadat Peyghambarzadeh, and Erfan Niazi. "Experimental Estimation of Human Blood Plasma Viscosity." International Journal of Pharma Medicine and Biological Sciences 8, no. 1 (January 2019): 1–6. http://dx.doi.org/10.18178/ijpmbs.8.1.1-6.

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2

UDOVENKO, A. V. "DETERMINATION OF THROMBIN AND PLASMIN ACTIVITY IN HUMAN BLOOD PLASMA USING THE TURBIDIMETRIC CURVE OF CLOT FORMATION AND DISSOLUTION." Biotechnologia Acta 16, no. 2 (April 28, 2023): 50–52. http://dx.doi.org/10.15407/biotech16.02.050.

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The aim of the study was to develop a method for determination the activity of thrombin, which is based on the turbidimetry curve of the formation and dissolution of a blood plasma clot. Methods. Donor blood samples were collected in 3.8% sodium citrate (1 part of sodium citrate and 9 parts of blood, pH 7.4). Plasma was separated from blood cells within 1 hour after blood collection by centrifugation the latter at 1200 g for 20 minutes. Aliquots of plasma were stored at -20 °C. Results. To determine the concentrations of thrombin and plasmin, TDCs of the formation and dissolution of blood plasma clots, initiated by the APTT reagent, were used. Based on the values of τ obtained, a calibration curve was constructed in the coordinates 1/τ – [Thr] (the rate of protofibrils formation in s-1 vs thrombin concentration in NIH units in 1 ml). Conclusion. The proposed methods to determine the activity of thrombin and plasmin made it possible to quantitatively calculate the rate of prothrombin activation in the lag period, the concentration and activity of thrombin based on the rate of fibrin and protofibrils formation as well as the activity and concentration of plasmin at the point of the complete clot dissolution,

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3

Golovanova, Olga. "Kinetic characteristics of crystallization in prototypes of human blood plasma." Bulletin of the Karaganda University. "Chemistry" series 85, no. 1 (March 29, 2017): 48–58. http://dx.doi.org/10.31489/2017ch1/48-58.

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4

Forrest, A. R., S. Morton, and C. Lambardarios. "Blood or plasma lactate?" British Journal of Sports Medicine 24, no. 2 (June 1, 1990): 132. http://dx.doi.org/10.1136/bjsm.24.2.132.

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5

Adams, G. "Microwave Blood Plasma Defroster." Journal of Microwave Power and Electromagnetic Energy 26, no. 3 (January 1991): 156–59. http://dx.doi.org/10.1080/08327823.1991.11688152.

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6

Jacobs, Anne C., and Jeanne M. Fair. "Bacteria-killing ability of fresh blood plasma compared to frozen blood plasma." Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology 191 (January 2016): 115–18. http://dx.doi.org/10.1016/j.cbpa.2015.10.004.

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7

Kriger-, Olga. "Advantages of Porcine Blood Plasma as a Component of Functional Drinks." Foods and Raw Materials 2, no. 2 (September 1, 2014): 26–32. http://dx.doi.org/10.12737/5456.

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8

Tomin, Tamara, Natalie Bordag, Elmar Zügner, Abdullah Al-Baghdadi, Maximilian Schinagl, Ruth Birner-Gruenberger, and Matthias Schittmayer. "Blood Plasma Quality Control by Plasma Glutathione Status." Antioxidants 10, no. 6 (May 27, 2021): 864. http://dx.doi.org/10.3390/antiox10060864.

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Timely centrifugation of blood for plasma preparation is a key step to ensure high plasma quality for analytics. Delays during preparation can significantly influence readouts of key clinical parameters. However, in a routine clinical environment, a strictly controlled timeline is often not feasible. The next best approach is to control for sample preparation delays by a marker that provides a readout of the time-dependent degradation of the sample. In this study, we explored the usefulness of glutathione status as potential marker of plasma preparation delay. As the concentration of glutathione in erythrocytes is at least two orders of magnitude higher than in plasma, even the slightest leakage of glutathione from the cells can be readily observed. Over the 3 h observation period employed in this study, we observed a linear increase of plasma concentrations of both reduced (GSH) and oxidized glutathione (GSSG). Artificial oxidation of GSH is prevented by rapid alkylation with N-ethylmaleimide directly in the blood sampling vessel as recently published. The observed relative leakage of GSH was significantly higher than that of GSSG. A direct comparison with plasma lactate dehydrogenase activity, a widely employed hemolysis marker, clearly demonstrated the superiority of our approach for quality control. Moreover, we show that the addition of the thiol alkylating reagent NEM directly to the blood tubes does not influence downstream analysis of other clinical parameters. In conclusion, we report that GSH gives an excellent readout of the duration of plasma preparation and the associated pre-analytical errors.

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9

Emsley, Jonas. "Plasma kallikrein's low gear." Blood 135, no. 8 (February 20, 2020): 518–19. http://dx.doi.org/10.1182/blood.2019004339.

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10

Shuai, Wen, and Shaoying Li. "CD138− plasma cell myeloma." Blood 134, no. 11 (September 12, 2019): 906. http://dx.doi.org/10.1182/blood.2019001845.

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11

Didkivskyi, V. A. "HPLC DETECTION OF ANTITHROMBITIC CALIX[4]ARENE IN BLOOD PLASMA OF ANIMALS." Biotechnologia Acta 15, no. 2 (April 2022): 51–52. http://dx.doi.org/10.15407/biotech15.02.051.

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Previously sodium salt of 5,11,17,23-bis (dihydroxyphosphoryl) methylcalix[4]arene (C-145) was shown to be promising antithrombotic agent. Aim. This work was focused on the development of the method for the direct detection of this substance in blood plasma and estimation of pharmacokinetics of this compound. Methods. C-145 was injected into the Wistar rat’s lateral tail vein and into rabbit’s marginal vein of the ear (12 mg/kg) or was administrated per-oral. The anticoagulant effects of C-145 in blood plasma were confirmed by activated partial thromboplastin time (APTT) test. HPLC was performed using Agilent 1100 series (Agilent, USA) on the phase cyano ZorbaxCN Column which parameters were L×I.D. 25 cm×4.6 mm. Results. The maximal antithrombotic effect after the intravenous or per-oral administration of C-145 was observed after 4-6 hours. In particular clotting time in APTT-test in these blood plasma samples was prolonged trice and more (120 s against 46 s in control). Normalization of blood clotting was achieved after 24 hours after the injection. To develop a method for direct C-145 detection in blood plasma we selected samples with maximal prolongation of clotting time. For accurate analysis of blood plasma samples proteins were saturated by 10 % trichloroacetic acid. After neutralization by NaHCO3 samples were prepared using 12-port vacuum unit for solid-phase extraction (Agilent, USA) with a Bond-Elut C18 cartridge. Samples that contained C-145 were eluted by 100% methanol for the HPLC analysis performed on the phase cyano ZorbaxCN Column equilibrated with an acetonitrile solution (ddH2O:AcCN 99:1). Elution was performed using a combined gradient of acetonitrile (100 %) and citrate buffer (0.1 M, pH 6.0). The elution zone of C-145 was detected on the 128th minute at 280 nm. Conclusion. Application of the developed methods allowed us to confirm the direct antithrombotic effect of calix[4]arene C-145 on blood of experimental animals during intravenous administration. Also HPLC technique enabled to detect this substance in blood plasma and most likely could be applied for other biological solutions and could be modified for the quantitative analysis in the pharmacokinetic studies as well.

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12

Annunziata, Joseph F., and Govind Bhagat. "Posttransplant lymphoproliferative disorder: EBV− plasma cell myeloma with large multinucleated plasma cells." Blood 134, no. 12 (July 10, 2019): 992. http://dx.doi.org/10.1182/blood.2019001939.

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13

Son, Jun Ho, Sang Hun Lee, Soongweon Hong, Seung-min Park, Joseph Lee, Andrea M. Dickey, and Luke P. Lee. "Hemolysis-free blood plasma separation." Lab Chip 14, no. 13 (2014): 2287–92. http://dx.doi.org/10.1039/c4lc00149d.

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14

Vehar, G. A. "Bioengineering of Blood Plasma Proteins." Scandinavian Journal of Haematology 33, S40 (April 24, 2009): 45–51. http://dx.doi.org/10.1111/j.1600-0609.1984.tb02544.x.

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15

Batcha, Kathy. "Blood Products and Plasma Substitutes." Journal of Pharmacy Technology 1, no. 4 (July 1985): 158–61. http://dx.doi.org/10.1177/875512258500100406.

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16

Robinson, E. Angela E. "Plasma and blood component procurement." Plasma Therapy and Transfusion Technology 8, no. 3 (September 1987): 193–203. http://dx.doi.org/10.1016/s0278-6222(87)80053-0.

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17

&NA;. "Pravastatin reduces plasma/blood viscosity." Inpharma Weekly &NA;, no. 1262 (November 2000): 19. http://dx.doi.org/10.2165/00128413-200012620-00049.

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18

Inal, Jameel M., Uchini Kosgodage, Sarah Azam, Dan Stratton, Samuel Antwi-Baffour, and Sigrun Lange. "Blood/plasma secretome and microvesicles." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1834, no. 11 (November 2013): 2317–25. http://dx.doi.org/10.1016/j.bbapap.2013.04.005.

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19

Kruse, J. A., and R. W. Carlson. "Lactate measurement: Plasma or blood?" Intensive Care Medicine 16, no. 1 (January 1990): 1–2. http://dx.doi.org/10.1007/bf01706317.

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20

Sukbuntherng, Juthamas, Debra K. Martin, Yvonne Pak, and Michael Mayersohn. "Characterization of the Properties of Cocaine in Blood: Blood Clearance, Blood to Plasma Ratio, and Plasma Protein Binding." Journal of Pharmaceutical Sciences 85, no. 6 (June 1996): 567–71. http://dx.doi.org/10.1021/js960026h.

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21

Udovenko, A., Ye Makogonenko, O. Hornytska, G. Gogolinska,, O. Yusova,, and V. Chernyshenko. "Determination of thrombin and plasmin activity using the turbidimetric analysis of clot formation and dissolution in human blood plasma." Ukrainian Biochemical Journal 96, no. 2 (April 25, 2024): 19–26. http://dx.doi.org/10.15407/ubj96.02.019.

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Based on the turbidimetric curve of formation and dissolution of a blood plasma clot initiated by the activated partial thromboplastin time reagent, a method for determining the coagulation component of thrombin activity and fibrinolytic activity of plasmin is proposed. The activity of thrombin was calculated by the value of the lag period, and plasmin by its amidase activity at the moment of complete dissolution of the clot. At the end of the lag period, about 0.45% of the available prothrombin was activated, and at the moment of complete dissolution of the clot 1.05% of the available plasminogen was activated. This method makes it possible to determine the ratio of the thrombin generation rate to that of plasmin, the time of clot formation to the time of its dissolution, as well as the overall hemostasis potential and coagulation and fibrinolytic components and their ratio. Keywords: coagulation, fibrinolysis, global hemostasis assay, plasmin generation, thrombin generation

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22

van den Besselaar, A. M. H. P., A. Tripodi, C. Shiach, J. Jespersen, L. Poller, M. Keown, N. Chauhan, et al. "European Concerted Action on Anticoagulation." Thrombosis and Haemostasis 87, no. 05 (2002): 859–66. http://dx.doi.org/10.1055/s-0037-1613097.

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SummaryA procedure for using citrated fresh plasmas for International Sensitivity Index (ISI) calibration of two types of whole blood point-of-care test (POCT) prothrombin time (PT) monitor systems has been assessed in a multicentre study.The CoaguChek Mini and TAS PT-NC systems gave higher ISI with whole blood samples than with fresh plasma calibrations. However, there was good agreement between whole blood and fresh plasma monitor system International Normalised Ratio (INR) and the reference INR of target samples.Reliable INR can therefore be obtained with both whole blood and plasma samples on these two POCT systems based on their respective ISI. With the CoaguChek Mini system, the plasma calibration ISI can also be used to derive reliable INR with whole blood PT results. This was not possible with the TAS PT-NC system.

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23

Chang, Mei, Peggy A. Nakagawa, Shirley A. Williams, Michael R. Schwartz, Karen L. Imfeld, Jeffrey S. Buzby, and Diane J. Nugent. "Immune thrombocytopenic purpura (ITP) plasma and purified ITP monoclonal autoantibodies inhibit megakaryocytopoiesis in vitro." Blood 102, no. 3 (August 1, 2003): 887–95. http://dx.doi.org/10.1182/blood-2002-05-1475.

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Abstract To determine if megakaryocytes are targeted by immune thrombocytopenic purpura (ITP) autoantibodies, as are platelets, we have studied the effects of ITP plasma on in vitro megakaryocytopoiesis. Umbilical cord blood mononuclear cells were incubated in the presence of thrombopoietin and 10% plasma from either ITP patients (n = 53) or healthy donors. The yield of megakaryocytic cells, as determined by flow cytometry, was significantly reduced in the presence of ITP plasma containing antiplatelet glycoprotein Ib (GPIb) autoantibodies (P < .001) as compared with both the control and patient plasma with no detectable anti-GPIIb/IIIa or anti-GPIb autoantibodies. Platelet absorption of anti-GPIb autoantibodies in ITP plasmas resulted in double the megakaryocyte production of the same plasmas without absorption, whereas platelet absorption of control plasma had no effect on megakaryocyte yield. Furthermore, 2 human monoclonal autoantibodies isolated from ITP patients, 2E7, specific for human platelet glycoprotein IIb heavy chain, and 5E5, specific for a neoantigen on glycoprotein IIIa expressed on activated platelets, had significant inhibitory effects on in vitro megakaryocytopoiesis (P < .001). Taken together, these data indicate that autoantibodies against either platelet GPIb or platelet GPIIb/IIIa in ITP plasma not only are involved in platelet destruction, but may also contribute to the inhibition of platelet production.

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24

Ullah, Hashmat, and Muhammad Farid Khan. "BLOOD." Professional Medical Journal 22, no. 03 (March 10, 2015): 365–69. http://dx.doi.org/10.29309/tpmj/2015.22.03.1358.

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All forms of mercury are global pollutants having no environmental limits.Human exposure to mercury occurs basically through food chain due to accumulation oforganic forms of mercury in fish. Objectives: The purpose of the present study was to analyzethe effect of phenyl mercuric acetate on plasma and cytosolic fraction GSH. Study Design:Experimental Study. Setting: Department of Pharmaceutical Chemistry, Faculty of Pharmacy,Gomal University, Dera Ismail Khan. Period: 29 January 2011 to 11 march 2012 .StatisticalAnalysis: One-way ANOVA followed by Dunnet’s HSD test. Results: For the estimation ofthiols Ellman’s method was used and was found statistically significant (p < 0.001) decreasein plasma and cytosolic fraction GSH which was dose and time dependent. The plasma GSHcontents drop in 0 to 120 minutes by various concentrations of phenyl mercuric acetate were64.45%, 59.33%, 50.89%, 41.56%, 33.63% and 32.99% while drop in cytosolic fraction GSHlevel from 0 to 120 minutes by different concentrations of phenyl mercuric acetate (PMA) was53.86%, 48.60%, 45.41%, 36.11%, 29.38% and 27.06%.Conclusions: It is clear that duringorganic mercury toxicity the blood components are also affected which is proved from ourresults. With the increase of time ,the mercury toxicity would be more harmful so detoxificationof organic mercury should be done on emergency bases at the earliest with the help of suitablechelating agents along with antioxidant therapy.

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25

Jonsson, V., J. E. Bock, and J. B. Nielsen. "Significance of plasma skimming and plasma volume expansion." Journal of Applied Physiology 72, no. 6 (June 1, 1992): 2047–51. http://dx.doi.org/10.1152/jappl.1992.72.6.2047.

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The organs associated with plasma volume expansion, i.e., the red bone marrow, the enlarged spleen, and the uteroplacental complex, are arteriovenous shunts with an interposed sinusoidal stroma able to skim off plasma-rich blood. In the spleen, plasma separation is an integral part of the hemoconcentration. In the red bone marrow, plasma skimming might provide a washout mechanism for the many newly formed erythrocytes and platelets from the sinusoids to the peripheral blood circulation. In the uteroplacental complex, skimming of plasma-rich blood is beneficial in increasing blood flow in the myometrium, kidneys, and skeletal musculature. The hypervolemic status with anemia will simulate a negative iron balance, which speeds up the absorption of iron. Thus a conceptual unit seems to exist in which rheological factors influence such functions as transport of newly formed blood cells into the circulation (in the red bone marrow), hemoconcentration (in the spleen), and iron balance during pregnancy (in the uteroplacental complex).

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26

Tobian, Aaron A. R., and Beth H. Shaz. "Earlier the better: convalescent plasma." Blood 136, no. 6 (August 6, 2020): 652–54. http://dx.doi.org/10.1182/blood.2020007638.

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27

Murphy, Michael F., and Sunny Dzik. "COVID-19, plasma, and hypogammaglobulinemia." Blood 136, no. 20 (November 12, 2020): 2245–46. http://dx.doi.org/10.1182/blood.2020008963.

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28

Corre, Jill, and Murielle Roussel. "Crowded bone marrow plasma cells." Blood 135, no. 1 (January 2, 2020): 79. http://dx.doi.org/10.1182/blood.2019003098.

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29

Irace, Concetta, Claudio Carallo, Faustina Scavelli, Teresa Esposito, Maria Serena De Franceschi, Cesare Tripolino, and Agostino Gnasso. "Influence of blood lipids on plasma and blood viscosity." Clinical Hemorheology and Microcirculation 57, no. 3 (2014): 267–74. http://dx.doi.org/10.3233/ch-131705.

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30

Cheng, Jih-Fei. "Cold Blood." Radical History Review 2021, no. 140 (May 1, 2021): 143–50. http://dx.doi.org/10.1215/01636545-8841718.

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Abstract This article historicizes viral transmissions through the global supply chain of blood plasma between the United States and the People’s Republic of China (PRC). Since the 1941 initiation of plasma donation to serve US armed forces, privately exported US blood products have contributed significantly to a globalized industry, valuing $21 billion in sales by 2017. Although maintaining a blood surplus has been crucial for treating illnesses and traumatic injuries, blood banking has been a source for massive viral transmissions, including HIV and hepatitis C. Examining the news, activism, and state responses to blood-borne outbreaks across the United States and PRC, this essay outlines a constellation of viral infections derived from plasma coerced from US prisoners and PRC rural villagers. Viruses archive the structural violences of the global pharmaceutical and blood biotechnology industries. They point to the cyclical relations between persistent class-based racial and ethnic disparities, technoscientific experimentation, and viral epidemics across polities.

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31

Sousa, Vera, Ana T. P. C. Gomes, Américo Freitas, Maria A. F. Faustino, Maria G. P. M. S. Neves, and Adelaide Almeida. "Photodynamic Inactivation of Candida albicans in Blood Plasma and Whole Blood." Antibiotics 8, no. 4 (November 13, 2019): 221. http://dx.doi.org/10.3390/antibiotics8040221.

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The few approved disinfection techniques for blood derivatives promote damage in the blood components, representing risks for the transfusion receptor. Antimicrobial photodynamic therapy (aPDT) seems to be a promising approach for the photoinactivation of pathogens in blood, but only three photosensitizers (PSs) have been approved, methylene blue (MB) for plasma and riboflavin and amotosalen for plasma and platelets. In this study, the efficiency of the porphyrinic photosensitizer Tri-Py(+)-Me and of the porphyrinic formulation FORM was studied in the photoinactivation of Candida albicans in plasma and in whole blood and the results were compared to the ones obtained with the already approved PS MB. The results show that FORM and Tri-Py(+)-Me are promising PSs to inactivate C. albicans in plasma. Although in whole blood the inactivation rates obtained were higher than the ones obtained with MB, further improvements are required. None of these PSs had promoted hemolysis at the isotonic conditions when hemolysis was evaluated in whole blood and after the addition of treated plasma with these PSs to concentrates of red blood cells.

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32

Kawano, Yawara, Takeshi Masuda, Shiho Fujiwara, Junzhe Bai, Nao Nishimura, Hiroto Ohguchi, and Jun-ichirou Yasunaga. "Proteomic Analysis of Monoclonal Plasma Cells from Plasma Cell Dyscrasias." Blood 142, Supplement 1 (November 28, 2023): 4776. http://dx.doi.org/10.1182/blood-2023-188213.

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Introduction. Novel agents including Anti-CD38 monoclonal antibodies, proteasome inhibitors and immunomodulatory drugs have improved the therapeutic outcome of plasma cell dyscrasias such as multiple myeloma (MM) and systemic light chain (AL) amyloidosis. Additionally, Next-generation sequencing (NGS) has greatly improved the ability to detect genomic aberrations occurring in monoclonal plasma cells. However, NGS data has not been made use for treatment decisions of plasma cell dyscrasias. Also, mechanisms of resistance to therapeutic agents have not been clearly shown in patient samples. Moreover, in-depth differences of monoclonal plasma cells among plasma cell dyscrasias are yet to be known. In the current study, we analyzed the protein expression in monoclonal plasma cells derived from patients with MM or AL amyloidosis by mass spectrometry to understand the biological differences in cells among those diseases and changes according to treatment. Materials and methods. Bone marrow samples from 47 newly diagnosed plasma cell dyscrasia patients (30 MM patients, 17 AL amyloidosis patients) and 9 relapsed and refractory patients diagnosed at Kumamoto University Hospital and Kumamoto Shinto General Hospital were examined. Patients provided written informed consent in accordance with the Declaration of Helsinki and the institutional ethics policy. Monoclonal plasma cells were obtained from bone marrow aspirates by CD138 magnetic beads selection. Sample preparation for proteomic analysis was performed using the PTS method, and digested peptides were desalted with SDB-XC tip. An Orbitrap Fusion Tribrid was used for peptide analysis, and peptide sequence information was acquired in data independent acquisition mode. Protein identification and quantification were performed by DIA-NN 18.1. Statistical and pathway analyses were performed using ExpressAnalyst, MetaboAnalyst and Metascape. Results. Monoclonal plasma cells from plasma cell dyscrasia patients were statistically divided into 3 groups (Group 1, 2 and 3) according to protein expression. Group 1 samples had enrichment of the Endocytosis and the MAPK signaling, while samples in Group 3 were enriched with the Ribosome pathway. Group 2 seemed to have intermediate phenotype of Group 1 and 3. All the samples in Group 1 and 50% of the samples in Group 2 were from AL amyloidosis, while majority of samples in group 3 were from MM. MM cases belonging to Group 3 tend to have higher R-ISS staging and CD56 positive monoclonal plasma cells compared to Group 2 cases. Among AL amyloidosis samples, all Group 3 cases had cardiac involvement of amyloidosis, proven by significantly higher BNP expression, while Group 2 cases tend to have kidney involvement, indicated by low serum albumin. Serial analysis of samples before and after daratumumab therapy showed reduced expression of CD38 and SLAMF7 in post treatment samples. Proteins related to focal adhesion were decreased in post-daratumumab treated samples compared to pre-daratumumab samples. Samples from carfilzomib refractory patients had higher expression of cell cycle related proteins compared to their pre-treatment samples. Conclusions. Proteomic analysis revealed differences between MM and AL amyloidosis-derived monoclonal plasma cells. While MM samples tend to belong to Group 3, which showed the activation of the Ribosome pathway, AL amyloidosis samples were mainly divided into Group 1 or 2, accompanying high enrichment of the Endocytosis and the MAPK signaling. Comparison of pre- and post-treatment samples showed distinct protein expression patterns according to therapeutic agents (daratumumab and carfilzomib). The current results may contribute to the understanding of differences between each plasma cell dyscrasias and mechanisms of resistance to therapeutic agents.

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33

Sun, Siyu, Joke Konings, Rolf T. Urbanus, Dana Huskens, Frauke Swieringa, Romy De Laat-Kremers, Jinmi Zou, et al. "Diversity of Plasmatic Thrombin Pools Regulate Thrombin Generation and Blood Clotting: Interference By a Novel Nanobody." Blood 142, Supplement 1 (November 28, 2023): 3978. http://dx.doi.org/10.1182/blood-2023-185665.

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Background: Thrombin has a multitude of roles in the initiation and propagation of (anti)coagulation, in platelet activation and fibrin clot formation. The assessment of thrombin generation (TG) and thrombin-dynamics, combined with multi-omics data, has provided in-depth understanding of the plasma factors contributing to the (in)activation of thrombin in triggered plasma and whole-blood. By default, the generated thrombin is considered to act as a single pool. Here, we present evidence for at least two major proteolytically active thrombin pools with non-overlapping functions in blood clotting. Methods: A novel Syn-Nb-AF106 anti-fibrin nanobody (Nb106) was characterized, targeting a species-conserved thrombin-binding site exposed by fibrinopeptide A cleavage from fibrinogen (Sun et al, this meeting). Thrombin generation was assessed by calibrated automated thrombography using various triggers with control (multi-donor) and (reconstituted) coagulation factor-deficient plasmas, platelet-rich plasma or whole blood. Fibrin clot formation was evaluated by scanning electron microscopy (SEM). Clot retraction was macroscopically assessed. Results: In tissue factor-triggered thrombin generation,we discovered that Nb106 dose-dependently reduced the thrombin peak level and endogenous thrombin potential (ETP) to 54-62%, without affecting kinetic thrombin generation parameters. We observed a similar reduction in platelet-free plasma, platelet-rich plasma and whole blood. Biochemically, Nb106 displaced thrombin from a binding site on cleaved fibrinogen (Sun et al., abstract). Nb106 inhibited tissue factor-induced thrombin generation, using plasma deficient in factor IX, XI or XII, but not using plasmas deficient in fibrinogen or antithrombin. Reconstitution experiments showed that the inhibition depended on the fibrinogen concentration. A-specific control nanobodies were without effect. Together, the fibrin(ogen)-dependent and thrombin-inhibiting effect indicated that Nb106 operates by releasing proteolytically-active thrombin from fibrin to allow inactivation by antithrombin. Time-dependent, late spiking experiments revealed that Nb106 reduced the generation of thrombin only when added at 0-15 minutes after trigger, but no longer after 30 minutes, suggesting that the inhibitory capacity was due to a shortened thrombin binding to fibrin rather than to a continued protection towards antithrombin. In plasmas from a cohort of 64 healthy subjects, application of Nb106 showed a consistent reducing effect on the parameters peak and ETP, with a moderate positive correlation with the fibrinogen level. Nb106 suppressed the thrombin generation amplitude, but not the kinetics in the presence of a panel of direct oral anticoagulants (DOAC). Strikingly, brightfield microscopy and SEM indicated that Nb106, but not control nanobodies, in triggered plasma, platelet-rich plasma and whole-blood, fully abrogated the formation of elongating fibrin fibers. In agreement with this, it strongly suppressed whole-blood clot retraction. Conclusion: Collectivity, these data point to the existence of two major pools of proteolytically active thrombin, both of which contributing to thrombin generation, that are formed upon plasma and blood coagulation. One pool of soluble thrombin steers the proteolytic coagulation cascade, while another pool is bound to growing fibrin fibers. The latter pool still cleaves the conventional AMC thrombin substrate, is temporarily protected against antithrombin, and is required for fibrin fiber extension and blood clotting and clot retraction. The Nb106, replacing thrombin from its binding site on fibrin, selectively annuls the second pool, thereby blocking the clotting process. The replacement ensures thrombin inactivation by antithrombin. Perspective: The novel anti-fibrin nanobody Syn-Nb-AF106 or a derivative has the potential to act as an alternative anticoagulant in thrombotic diseases with pathological fibrin formation.

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34

Fraser, Steven R., Nuala A. Booth, and Nicola J. Mutch. "The antifibrinolytic function of factor XIII is exclusively expressed through α2-antiplasmin cross-linking." Blood 117, no. 23 (June 9, 2011): 6371–74. http://dx.doi.org/10.1182/blood-2011-02-333203.

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Abstract Factor XIII (FXIII) generates fibrin-fibrin and fibrin-inhibitor cross-links. Our flow model, which is sensitive to cross-linking, was used to assess the effects of FXIII and the fibrinolytic inhibitor, α2-antiplasmin (α2AP) on fibrinolysis. Plasma model thrombi formed from FXIII or α2AP depleted plasma lysed at strikingly similar rates, 9-fold faster than pooled normal plasma (PNP). In contrast, no change was observed on depletion of PAI-1 or thrombin activatable fibrinolysis inhibitor (TAFI). Inhibition of FXIII did not further enhance lysis of α2AP depleted thrombi. Addition of PNP to FXIII or α2AP depleted plasmas normalized lysis. Lysis rate was strongly inversely correlated with total cross-linked α2AP in plasma thrombi. Reconstitution of FXIII into depleted plasma stabilized plasma thrombi and normalized γ-dimers and α-polymers formation. However, the presence of a neutralizing antibody to α2AP abolished this stabilization. Our data show that the antifibrinolytic function of FXIII is independent of fibrin-fibrin cross-linking and is expressed exclusively through α2AP.

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35

Vesel, Alenka, Metod Kolar, Karin Stana-Kleinschek, and Miran Mozetic. "Etching rates of blood proteins, blood plasma and polymer in oxygen afterglow of microwave plasma." Surface and Interface Analysis 46, no. 10-11 (January 19, 2014): 1115–18. http://dx.doi.org/10.1002/sia.5394.

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36

Douglas, Colin, Tara Quinton, Ellinore Cabanban, Karen Black, and Ali Sadeghi-Khomami. "A Standardized Kit for a Chromogenic Modified Nijmegen-Bethesda Assay: Repeatability, Reproducibility, and Analytical Sensitivity." Blood 132, Supplement 1 (November 29, 2018): 1201. http://dx.doi.org/10.1182/blood-2018-99-119491.

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Abstract Antibody-based inhibitor response to Factor VIII replacement therapy is one of the most common complications in the treatment of persons with hemophilia A (PwHA). Accordingly, accurate quantification of FVIII inhibitor antibody titer is essential in guiding patient treatment. Testing for FVIII inhibitors is not standardized; typically, FVIII inhibitor titers are measured using non-standardized LDTs (Laboratory Developed Tests). These LDTs vary in the processing of patient plasma, the reagents used to perform the assay, and the method of FVIII activity measurement. Here we report the development of a standardized set of reagents to perform a chromogenic modified Nijmegen-Bethesda assay (MNBA). The kit consists of imidazole-buffered pooled normal plasma (IB-PNP) with a consistent normal level of FVIII activity, and an imidazole-buffered bovine serum albumin solution (IB-BSA) as a diluent. Also included in the kit are a positive FVIII inhibitor plasma control (1.2 - 1.8 BU/mL) and an inhibitor-free negative plasma control. To perform the assay, test plasma was heat inactivated at 56 °C for 30 minutes to minimize residual FVIII activity. The inactivated plasma was then centrifuged (2700 x g,5 min.) and the supernatant used to make a series of two-fold serial dilutions with IB-BSA. The dilutions were each mixed with an equal volume of IB-PNP to form test mixes and incubated in a 37 °C water bath to allow time for the inhibitor antibodies from the patient plasma to inactivate FVIII in the IB-PNP. After two hours, the reaction was halted by cooling the test mixes in an ice bath. The FVIII activity of the test mixes was then measured using a Siemens FVIII Chromogenic Assay on a Siemens BCS XP analyzer. The residual FVIII activity of each test mix was calculated by comparing its FVIII activity to the activity of a control mix containing no test plasma (1:1 mixture of IB-BSA and IB-PNP). Here we report the use of this kit to perform a comprehensive study examining the repeatability, reproducibility, and analytical sensitivity of a chromogenic MNBA performed according to CLSI guidelines (CLSI EP05 and EP17). Inhibitor-negative and inhibitor-positive plasma from PwHA were combined to yield a panel of test plasmas at four different levels of inhibitor: below cutoff level (~0.3 BU/mL), low positive (~1.2 BU/mL), mid positive (~5 BU/mL) and a high positive (~8 BU/mL). To assess the repeatability of the assay, we measured each of these test plasmas using three lots of MNBA kit and one lot of FVIII chromogenic kit for a total of 240 titer determinations (3 lots × 20 days × 2 runs × 2 replicates). Inhibitor measurements of the panel of test plasmas showed within-lot precision of less than 10% (CV), and the kit controls were identified correctly each time. The reproducibility of the assay was determined in a study conducted across three different laboratories using different BCS XP analyzers and operators but the same panel of test plasmas. The limit of blank (LoB) and the limit of detection (LoD) of the assay were also determined using multiple low titer plasmas from unique donors. The assay system can reliably distinguish inhibitor titers as low as 0.2 BU/mL (LoD) in plasma from PwHA with no history of inhibitors. The chromogenic MNBA kit shows potential for labs seeking repeatable and reproducible FVIII inhibitor measurement that can otherwise vary significantly within or between labs. Standardization of reagents and protocol yields consistent results and is suitable for multi-center inhibitor studies in PwHA. Table Table. Disclosures No relevant conflicts of interest to declare.

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37

Malchesky, P. S., T. Horiuchi, M. Usami, M. Emura, and Y. Nose. "Blood Detoxification by Membrane Plasma Filtration." International Journal of Artificial Organs 9, no. 5 (September 1986): 349–54. http://dx.doi.org/10.1177/039139888600900518.

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The recognition of macromolecule abnormalities in various metabolic or immunologic related disease states has led to the use of plasma exchange for therapeutics. Limitations of plasma exchange, however, exist. Membrane plasma filtration provides a practical alternative. Solute removal can be made selective by the choice of operating conditions as temperature and the selection of the membrane/module design. The optimal temperature range is a function of the plasma type, solute concentrations and membrane system. Operation at below physiologic temperature (cryofiltration) is particularly suited for the removal of cold aggregative solutes, while operation at near or above physiologic temperature is more suited for the separation of solutes having large size differences at normal physiologic temperature. Membrane filtration is simple and safe to perform, is more selective than plasma exchange, does not require plasma product infusion and is more versatile than selective sorption in its applications.

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38

Christiansen, Victoria J., Kenneth W. Jackson, Kyung N. Lee, and Patrick A. McKee. "The effect of a single nucleotide polymorphism on human α2-antiplasmin activity." Blood 109, no. 12 (June 15, 2007): 5286–92. http://dx.doi.org/10.1182/blood-2007-01-065185.

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Abstract The primary inhibitor of plasmin, α2-antiplasmin (α2AP), is secreted by the liver into plasma with Met as the amino-terminus. During circulation, Met-α2AP is cleaved by antiplasmin-cleaving enzyme (APCE), yielding Asn-α2AP, which is crosslinked into fibrin approximately 13 times faster than Met-α2AP. The Met-α2AP gene codes for either Arg or Trp as the sixth amino acid, with both polymorphic forms found in human plasma samples. We determined the Arg6Trp genotype frequency in a healthy population and its effects on Met-α2AP cleavage and fibrinolysis. Genotype frequencies were RR 62.5%, RW 34.0%, and WW 3.5%. The polymorphism related to the percentage of Met-α2AP in plasma was WW (56.4%), RW (40.6%), and RR (23.6%). WW plasma tended to have shorter lysis times than RR and RW plasmas. APCE cleaved purified Met-α2AP(Arg6) approximately 8-fold faster than Met-α2AP(Trp6), which is reflected in Asn-α2AP/Met-α2AP ratios with time in RR, RW, and WW plasmas. Removal of APCE from plasma abrogated cleavage of Met-α2AP. We conclude that the Arg6Trp polymorphism is functionally significant, as it clearly affects conversion of Met-α2AP to Asn-α2AP, and thereby, the rate of α2AP incorporation into fibrin. Therefore, the Arg6Trp polymorphism may play a significant role in governing the long-term deposition/removal of intravascular fibrin.

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39

Germans, Sharon Koorse, and Olga Weinberg. "Plasma cell neoplasm: a unique morphology." Blood 138, no. 1 (March 24, 2021): 104. http://dx.doi.org/10.1182/blood.2021012034.

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40

Bloch, Evan M. "Convalescent plasma to treat COVID-19." Blood 136, no. 6 (August 6, 2020): 654–55. http://dx.doi.org/10.1182/blood.2020007714.

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41

Savelyeva, A. V., D. N. Bariakin, E. V. Kuligina, V. V. Morozov, V. A. Richter, and D. V. Semenov. "Circular RNAs of human blood cells, plasma, and plasma subfractions." Russian Journal of Bioorganic Chemistry 43, no. 2 (March 2017): 115–25. http://dx.doi.org/10.1134/s1068162017020133.

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42

Rakhe, Swapnil, Sunita R. Patel-Hett, Sheryl Bowley, John E. Murphy, and Debra D. Pittman. "The Tissue Factor Pathway Inhibitor Antibody, PF-06741086, Increases Thrombin Generation in Rare Bleeding Disorder and Von Willebrand Factor Deficient Plasmas." Blood 132, Supplement 1 (November 29, 2018): 2462. http://dx.doi.org/10.1182/blood-2018-99-119674.

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Abstract Hemophilia A and B are hereditary bleeding disorders that result from deficiencies in the intrinsic coagulation pathway leading to insufficient generation of Factor Xa (FXa) and thrombin to promote stable hemostasis. Coagulation defects are also observed in other inherited rare factor bleeding disorders. The extrinsic pathway of coagulation in these disorders cannot generate sufficient levels of FXa due to the regulation by Tissue Factor Pathway Inhibitor (TFPI). TFPI is a Kunitz-type serine protease inhibitor that negatively regulates thrombin generation by inhibiting the FXa/tissue factor (TF)/Factor VIIa (FVIIa) complex. PF-06741086, a fully human inhibitory monoclonal antibody, binds the Kunitz-2 domain and is currently under development as a potential prophylactic treatment to prevent bleeding episodes in hemophilia A and hemophilia B patients with and without inhibitors. The addition of PF-06741086 in vitro to donor plasma from both healthy normal volunteers and hemophilia patients promoted thrombin generation and restored hemostasis in vivo in murine hemophilia bleeding models. Pharmacological effects of PF-06741086 on thrombin generation were also observed in a healthy volunteer Phase 1 study. Other rare disease coagulopathies also result in the insufficient generation of thrombin. In this study, the potential of PF-06741086 to restore thrombin generation in rare disease plasma was explored. Thrombin generation was measured in citrated platelet poor Factor XI (FXI), Factor V (FV), FVII, von Willebrand Factor (vWF) deficient (Type 1, 2A, 2B and 3) congenital donor plasma following the in vitro addition of PF-06741086 (0, 1, 10 or 100 nM) or a human IgG1 antibody; initiated with 1 pM TF and 4 µM phospholipid. FXI, FV, and FVII donors had less than 1% coagulation factor activity. Non-hemophilic plasma from healthy donors alone was also included in the analysis. In FXI deficient plasmas, a concentration-dependent increase in peak thrombin and a shortening of the lag time was observed with the addition of PF-06741086 normalizing and restoring levels to those observed in the non-hemophilic plasma. A similar response was also observed in all of the vWF deficient plasmas. In one FVII deficient plasma, an increase in peak thrombin was observed at dose of 100 nM PF-06741086, however, the lag time (20 minutes) was significantly extended, relative to healthy volunteer non-hemophilic plasma. As expected, the addition of PF-06741086 to FV deficient plasma did not increase thrombin generation at any concentration. The in vitro addition of the TFPI antibody, PF-06741086, improved thrombin generation in selected coagulation factor deficient plasmas, including vWF deficiency, to the levels observed in normal plasma. This data suggestion that the inhibition of TFPI may promote hemostasis in rare bleeding disorders such as FXI deficiency and vWF deficiencies. Disclosures Rakhe: Pfizer: Employment. Patel-Hett:Pfizer: Employment. Bowley:Pfizer: Employment. Murphy:Pfizer: Employment. Pittman:Pfizer: Employment.

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43

HOWELL, N. K., and R. A. LAWRIE. "Functional aspects of blood plasma proteins." International Journal of Food Science & Technology 22, no. 2 (June 28, 2007): 145–51. http://dx.doi.org/10.1111/j.1365-2621.1987.tb00469.x.

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44

HOWELL, NAZLIN K., and R. A. LAWRIE. "Functional aspects of blood plasma proteins." International Journal of Food Science & Technology 18, no. 6 (June 28, 2007): 747–62. http://dx.doi.org/10.1111/j.1365-2621.1983.tb00313.x.

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45

HOWELL, NAZLIN K., and R. A. LAWRIE. "Functional aspects of blood plasma proteins." International Journal of Food Science & Technology 19, no. 3 (June 28, 2007): 289–95. http://dx.doi.org/10.1111/j.1365-2621.1984.tb00352.x.

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46

HOWELL, NAZLIN K., and R. A. LAWRIE. "Functional aspects of blood plasma proteins." International Journal of Food Science & Technology 19, no. 3 (June 28, 2007): 297–313. http://dx.doi.org/10.1111/j.1365-2621.1984.tb00353.x.

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47

Varchanis, S., Y. Dimakopoulos, C. Wagner, and J. Tsamopoulos. "How viscoelastic is human blood plasma?" Soft Matter 14, no. 21 (2018): 4238–51. http://dx.doi.org/10.1039/c8sm00061a.

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In this work, we evaluate for first time the viscoelastic properties of human blood plasma. Using computational rheology, a molecular-based constitutive model and experimental data, we predict accurately the rheological response of human blood plasma in strong extensional and constriction complex flows.

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48

Tomiyama, Yoshinobu, Johnny E. Brian, and Michael M. Todd. "Plasma viscosity and cerebral blood flow." American Journal of Physiology-Heart and Circulatory Physiology 279, no. 4 (October 1, 2000): H1949—H1954. http://dx.doi.org/10.1152/ajpheart.2000.279.4.h1949.

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We hypothesized that the response of cerebral blood flow (CBF) to changing viscosity would be dependent on “baseline” CBF, with a greater influence of viscosity during high-flow conditions. Plasma viscosity was adjusted to 1.0 or 3.0 cP in rats by exchange transfusion with red blood cells diluted in lactated Ringer solution or with dextran. Cortical CBF was measured by H2 clearance. Two groups of animals remained normoxic and normocarbic and served as controls. Other groups were made anemic, hypercapnic, or hypoxic to increase CBF. Under baseline conditions before intervention, CBF did not differ between groups and averaged 49.4 ± 10.2 ml · 100 g−1 · min−1 (±SD). In control animals, changing plasma viscosity to 1.0 or 3.0 cP resulted in CBF of 55.9 ± 8.6 and 42.5 ± 12.7 ml · 100 g−1 · min−1, respectively (not significant). During hemodilution, hypercapnia, and hypoxia with a plasma viscosity of 1.0 cP, CBF varied from 98 to 115 ml · 100 g−1 · min−1. When plasma viscosity was 3.0 cP during hemodilution, hypercapnia, and hypoxia, CBF ranged from 56 to 58 ml · 100 g−1 · min−1 and was significantly reduced in each case ( P < 0.05). These results support the hypothesis that viscosity has a greater role in regulation of CBF when CBF is increased. In addition, because CBF more closely followed changes in plasma viscosity (rather than whole blood viscosity), we believe that plasma viscosity may be the more important factor in controlling CBF.

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49

Diedrich, André, Sachin Y. Paranjape, and David Robertson. "Plasma and Blood Volume in Space." American Journal of the Medical Sciences 334, no. 1 (July 2007): 80–86. http://dx.doi.org/10.1097/maj.0b013e318065b89b.

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50

The Lancet Haematology. "The big business of blood plasma." Lancet Haematology 4, no. 10 (October 2017): e452. http://dx.doi.org/10.1016/s2352-3026(17)30183-7.

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