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Статті в журналах з теми "PF4"

Автор: Grafiati

Опубліковано: 4 червня 2021

Оновлено: 11 березня 2023

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1

Esan, A. M., Z. Khan, R. Kiran, T. O. Omolekan, K. A. Aremu, and H. R. Y. Adeyemi. "Ameliorative Effects of Pseudomonas fluorescence Strains on Growth and Antioxidant Potential of Okra (Abelmoschus esculentus) Plant under Nematode Infection." European Journal of Biology and Biotechnology 2, no. 3 (June 5, 2021): 50–56. http://dx.doi.org/10.24018/ejbio.2021.2.3.168.

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Meloidogyne incognita is a plant pathogen causing root-knot nematodes disease in many crops worldwide. Due to the environmental threat on the use of chemical fumigants, there is a need for a biological control method using microbial antagonists on root-knot nematodes disease. Therefore, this study was conducted to screen and evaluate the biocontrol potential of P. fluorescens strains against root-knot nematodes. The effectiveness of six P. fluorescens strains viz., Pf1, Pf2, Pf3, Pf4, Pf5and Pf6 were tested in vitro and also in pots experiment for their inhibitory activities and biocontrol pot

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2

González-Serrano, Diego J., Milad Hadidi, Matin Varcheh, Aniseh Zarei Jelyani, Andres Moreno, and Jose M. Lorenzo. "Bioactive Peptide Fractions from Collagen Hydrolysate of Common Carp Fish Byproduct: Antioxidant and Functional Properties." Antioxidants 11, no. 3 (March 6, 2022): 509. http://dx.doi.org/10.3390/antiox11030509.

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Collagen isolated from byproducts of common carp was hydrolyzed with alcalase enzyme to obtain peptide fractions. The resulting >30 kDa (PF1), 10–30 kDa (PF2), 3–10 kDa (PF3) and <1 kDa (PF4) fractions were studied for their antioxidant and functional properties. All peptide fractions illustrated antioxidant activity at different concentrations (1, 5, and 10 mg/mL). Although PF4 indicated the highest DPPH radical-scavenging activity (87%) at a concentration of 1 mg/mL, the highest reducing power (0.34) and hydroxyl radical scavenging activity (95.4%) were also observed in PF4 at a concen

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3

Kakkar, Preeti Handa, R. M. Saxena, and Mamta Joshi. "Histopathological analysis of liver in Puntius ticto exposed to water soluble fraction (WSF) of petrol." Journal of Applied and Natural Science 2, no. 2 (December 1, 2010): 290–92. http://dx.doi.org/10.31018/jans.v2i2.136.

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The fresh water fish Puntius ticto were exposed to lethal concentration of water soluble fraction (WSF) of petrol (5%-PF1, 10%-PF2, 15%-PF3, 20%-PF4 and 25%-PF5) for 96 hours. The exposure of WSF produced some conspicuous histopathological changes in liver. The swelling of hepatocytes, degeneration, necrosis, hemolysis, dilation, congestion and fibrosis in blood sinusoids were the prominent changes observed. The histological analysis showed increasing damages dose-dependents and time-dependents.

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4

FELLOWES, R. A., A. G. MAULE, N. J. MARKS, T. G. GEARY, D. P. THOMPSON, and D. W. HALTON. "Nematode neuropeptide modulation of the vagina vera of Ascaris suum: in vitro effects of PF1, PF2, PF4, AF3 and AF4." Parasitology 120, no. 1 (January 2000): 79–89. http://dx.doi.org/10.1017/s0031182099005260.

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Ascaris suum possesses a large number of FMRFamide-related peptides (FaRPs) of which KNEFIRFamide (AF1), KHEYLRFamide (AF2) and KSAYMRFamide (AF8/PF3) have been shown to modulate the intrinsic, rhythmic activity of the vagina vera of A. suum in vitro. In the present study, the effects of the nematode FaRPs, SDPNFLRFamide (PF1), SADPNFLREamide (PF2) and KPNFIRFamide (PF4) (from Panagrellus redivivus) and AVPGVLRFamide (AF3) and GDVPGVLRFamide (AF4) (from A. suum) on the in vitro activity of the vagina vera were examined. The effects of each of the peptides were qualitatively and quantitatively

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5

Lecomte-Raclet, Laurence, Mònica Alemany, Anabelle Sequeira-Le Grand, Jean Amiral, Gérard Quentin, Anne Marie Vissac, Jacques P. Caen, and Zhong Chao Han. "New Insights Into the Negative Regulation of Hematopoiesis by Chemokine Platelet Factor 4 and Related Peptides." Blood 91, no. 8 (April 15, 1998): 2772–80. http://dx.doi.org/10.1182/blood.v91.8.2772.2772_2772_2780.

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Platelet factor 4 (PF4) has been recognized as an inhibitor of myeloid progenitors. However, the mechanism of action of this chemokine remains poorly understood. The present study was designed to determine its structure/function relationship. A series of peptides overlapping the C-terminal and central regions of PF4 were analyzed in vitro for their action on murine hematopoietic progenitor growth to assess the minimal sequence length required for activity. The peptides p17-58 and p34-58 possessed an increased hematopoietic inhibitory activity when compared with PF4, whereas the shorter peptide

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6

Karuppaija, Sinthuja, Kapilan Ranganathan, and Vasantharuba Seevaratnam. "Characterization of best naringinase producing fungus strain isolated from palmyrah (Borrasus flabellifer) fruit pulp." International Journal of Biological Research 4, no. 2 (July 19, 2016): 97. http://dx.doi.org/10.14419/ijbr.v4i2.6289.

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Анотація:

Background: The Palmyrah (Borrasus flabellifer L.) fruit pulp has the bitter compound flabelliferin (a tetraglycoside) which can be hydrolyzed by naringinase enzyme. The diverse groups of filamentous fungi and bacteria that live in different substrates have the capacity of producing extracellular naringinase enzyme which is of tremendous industrial value.Objective: The objective of the study was to isolate the naringinase producing fungal strains from Palmyrah and to identify the best naringinase producer under liquid and solid state fermentation systems.Methods: Fungal strains isolated from P

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7

PURCELL, J., A. P. ROBERTSON, D. P. THOMPSON, and R. J. MARTIN. "The time-course of the response to the FMRFamide-related peptide PF4 in Ascaris suum muscle cells indicates direct gating of a chloride ion-channel." Parasitology 124, no. 6 (June 2002): 649–56. http://dx.doi.org/10.1017/s0031182002001695.

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We investigated the effects of PF4 on Ascaris suum somatic muscle cells using a 2 electrode current-clamp technique. PF4 is a FaRP (FMRFamide-related peptide), originally isolated from the free-living nematode Panagrellus redivivus. PF4 caused hyperpolarization and an increase in chloride ion conductance when it was applied to the muscle cells of the Ascaris body wall. The delay between the application of the peptide and the appearance of the response was measured and compared with that of gamma-amino butyric acid (GABA), a compound that directly gates ion channels, and with PF1, a FaRP that a

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8

Bokka, Chandra Sekhar, Ganesh Kumar Veeramachaneni, V. B. S. C. Thunuguntla, Janakiram Bobbillapati, and Jayakumar Singh Bondili. "Peptide Mapping, In Silico and In Vivo Analysis of Allergenic Sorghum Profilin Peptides." Medicina 55, no. 5 (May 21, 2019): 178. http://dx.doi.org/10.3390/medicina55050178.

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Background and objectives: Nearly 20–30% of the world’s population suffers from allergic rhinitis, among them 15% are progressing to asthma conditions. Sorghum bicolor profilin (Sorb PF), one of the panallergens, was identified, but the allergen specificity is not yet characterized. Materials and Methods: To map the antigenic determinants responsible for IgE binding, the present study is focused on in silico modeling, simulation of Sorb PF and docking of the Sorb PF peptides (PF1-6) against IgG and IgE, followed by in vivo evaluation of the peptides for its allergenicity in mice. Results: Pept

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9

Ismail, Muhammad Hafiz, Katharine A. Michie, Yu Fen Goh, Parisa Noorian, Staffan Kjelleberg, Iain G. Duggin, Diane McDougald, and Scott A. Rice. "The Repressor C Protein, Pf4r, Controls Superinfection of Pseudomonas aeruginosa PAO1 by the Pf4 Filamentous Phage and Regulates Host Gene Expression." Viruses 13, no. 8 (August 15, 2021): 1614. http://dx.doi.org/10.3390/v13081614.

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It has been shown that the filamentous phage, Pf4, plays an important role in biofilm development, stress tolerance, genetic variant formation and virulence in Pseudomonas aeruginosa PAO1. These behaviours are linked to the appearance of superinfective phage variants. Here, we have investigated the molecular mechanism of superinfection as well as how the Pf4 phage can control host gene expression to modulate host behaviours. Pf4 exists as a prophage in PAO1 and encodes a homologue of the P2 phage repressor C and was recently named Pf4r. Through a combination of molecular techniques, ChIPseq an

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10

Hara, Francisco Adilson dos Santos, and Luiz Antonio de Oliveira. "Características fisiológicas e ecológicas de isolados de rizóbios oriundos de solos ácidos e álicos de Presidente Figueiredo, Amazonas." Acta Amazonica 34, no. 3 (September 2004): 343–57. http://dx.doi.org/10.1590/s0044-59672004000300002.

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Alguns isolados de rizóbio, além de fixarem o N2, são capazes de solubilizar fosfatos pouco solúveis, disponibilizando o P para as plantas e para si mesmos. No entanto, o Al e a acidez dos solos da Amazônia podem diminuir a população desses microrganismos. O presente trabalho avaliou a capacidade nodulífera, a tolerância à acidez e ao Al tóxico, bem como a capacidade de solubilizar fosfatos de Ca e de Al de 88 isolados de rizóbio de solos agrícolas, do município de Presidente Figueiredo, AM. Amostras de solo sob cultivos agrícolas foram coletadas e utilizadas como fontes de inóculo para planta

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11

Webb, Jeremy S., Mathew Lau, and Staffan Kjelleberg. "Bacteriophage and Phenotypic Variation in Pseudomonas aeruginosa Biofilm Development." Journal of Bacteriology 186, no. 23 (December 1, 2004): 8066–73. http://dx.doi.org/10.1128/jb.186.23.8066-8073.2004.

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ABSTRACT A current question in biofilm research is whether biofilm-specific genetic processes can lead to differentiation in physiology and function among biofilm cells. In Pseudomonas aeruginosa, phenotypic variants which exhibit a small-colony phenotype on agar media and a markedly accelerated pattern of biofilm development compared to that of the parental strain are often isolated from biofilms. We grew P. aeruginosa biofilms in glass flow cell reactors and observed that the emergence of small-colony variants (SCVs) in the effluent runoff from the biofilms correlated with the emergence of p

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12

Rucinski, Boguslaw, Stefan Niewiarowski, Marian Strzyzewski, John C. Holt, and Kevin H. Mayo. "Human Platelet Factor 4 and Its C-Terminal Peptides: Heparin Binding and Clearance from the Circulation." Thrombosis and Haemostasis 63, no. 03 (1990): 493–98. http://dx.doi.org/10.1055/s-0038-1645072.

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SummaryHuman platelet factor 4 (PF4), a high affinity heparin binding protein, is released from stimulated platelets and stored at vascular sites, predominantly in liver, from where it can be brought back into circulation by heparin. We attempted to define structural requirements for PF4 binding to heparin and for the pattern of its clearance from the circulation. Intact PF4 bound strongly to heparin agarose and was eluted at 1.4 M NaCl, while reduced PF4 and PF4 C-terminal peptides PF4 (47-70) and PF4 (58-70) bound weakly and were eluted at 0.2-0.5 M NaCl. 125I-radiolabeled intact PF4, reduce

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13

Lambert, Michele P., Lubica Rauova, Matthew Bailey, Martha C. Sola-Visner, M. Anna Kowalska, and Mortimer Poncz. "Platelet factor 4 is a negative autocrine in vivo regulator of megakaryopoiesis: clinical and therapeutic implications." Blood 110, no. 4 (August 15, 2007): 1153–60. http://dx.doi.org/10.1182/blood-2007-01-067116.

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Abstract Platelet factor 4 (PF4) is a negative regulator of megakaryopoiesis in vitro. We have now examined whether PF4 regulates megakaryopoiesis in vivo by studying PF4 knockout mice and transgenic mice that overexpress human (h) PF4. Steady-state platelet count and thrombocrit in these animals was inversely related to platelet PF4 content. Growth of megakaryocyte colonies was also inversely related to platelet PF4 content. Function-blocking anti-PF4 antibody reversed this inhibition of megakaryocyte colony growth, indicating the importance of local PF4 released from developing megakaryocyte

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14

Greinacher, Andreas, Birte Holtfreter, Krystin Krauel, Daniela Gätke, Claudia Weber, Till Ittermann, Sven Hammerschmidt, and Thomas Kocher. "Association of natural anti-platelet factor 4/heparin antibodies with periodontal disease." Blood 118, no. 5 (August 4, 2011): 1395–401. http://dx.doi.org/10.1182/blood-2011-03-342857.

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Abstract Platelet factor 4 (PF4) and heparin (H) form PF4/H complexes, the target of the immune reaction in heparin-induced thrombocytopenia (HIT). HIT seems to be a secondary immune response as anti-PF4/H-IgG antibodies occur as early as day 4 of heparin treatment. This study investigated whether prevalent infections such as periodontitis may induce the PF4/H immune response as: (1) natural anti-PF4/H Abs are present in the normal population; (2) PF4 bound to bacteria exposes the same antigen(s) as PF4/H complexes; and (3) sepsis induces PF4/H Abs in mice. We found PF4 bound to periodontal pa

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15

Krauel, Krystin, Christian Pötschke, Claudia Weber, Wolfram Kessler, Birgitt Fürll, Till Ittermann, Stefan Maier, Sven Hammerschmidt, Barbara M. Bröker, and Andreas Greinacher. "Platelet factor 4 binds to bacteria, inducing antibodies cross-reacting with the major antigen in heparin-induced thrombocytopenia." Blood 117, no. 4 (January 27, 2011): 1370–78. http://dx.doi.org/10.1182/blood-2010-08-301424.

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AbstractA clinically important adverse drug reaction, heparin-induced thrombocytopenia (HIT), is induced by antibodies specific for complexes of the chemokine platelet factor 4 (PF4) and the polyanion heparin. Even heparin-naive patients can generate anti-PF4/heparin IgG as early as day 4 of heparin treatment, suggesting preimmunization by antigens mimicking PF4/heparin complexes. These antibodies probably result from bacterial infections, as (1) PF4 bound charge-dependently to various bacteria, (2) human heparin-induced anti-PF4/heparin antibodies cross-reacted with PF4-coated Staphylococcus

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16

Turrentine, Tiffany, Jennine Dawicki McKenna, Ann Rux, Daniel Rader, Anna Kowalska, and Bruce Sachais. "Elimination of platelet factor 4 (PF4) from platelets reduces atherosclerosis in C57Bl/6 and apoE-/- mice." Thrombosis and Haemostasis 98, no. 11 (2007): 1108–13. http://dx.doi.org/10.1160/th07-04-0271.

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SummaryActivated platelets, which release platelet factor 4 (PF4) are present in patients with atherosclerosis. To date, no direct invivo evidence exists for the involvement of PF4 in atherogenesis. In the current study, we tested the hypothesis that PF4 is atherogenic, and that genetic elimination of PF4 would protect mice from atherosclerosis. We have bred PF4-/- mice onto two athero-susceptible backgrounds, WT-C57Bl/6(WT) and apoE-/- to examine the importance of PF4 in atherogenesis. In order to induce atherosclerosis, WT and PF4-/- mice were fed an atherogenic diet for 30 weeks, while apoE

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17

Hong, Shu, Zhongji Gu, Ling Chen, Ping Zhu, and Hailan Lian. "Synthesis of phenol formaldehyde (PF) resin for fast manufacturing laminated veneer lumber (LVL)." Holzforschung 72, no. 9 (September 25, 2018): 745–52. http://dx.doi.org/10.1515/hf-2017-0184.

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AbstractPhenol formaldehyde (PF) resin is a well-tried adhesive for manufacturing laminated veneer lumber (LVL). PF has a high bonding strength, good cold pressing property and contributes a lot to the high production efficiency of LVL. In the present paper, PFs were synthesized at three different alkaline condition levels with a molar formaldehyde to phenol (F/P) ratio of 2.25. The bonding strength of PFs was not influenced by the alkalinity. Compared with PFs synthesized under alkalinity of 1 and 4%, PF with 8% alkalinity formed a resin with a high mole mass (MM), uniform mole mass distribut

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18

Lambert, Michele P., Ronghua Meng, Dawn Harper, Liqing Xiao, Michael S. Marks, and Mortimer Poncz. "Megakaryocytes Exchange Significant Levels of Their Alpha-Granular PF4 with Their Environment." Blood 124, no. 21 (December 6, 2014): 1432. http://dx.doi.org/10.1182/blood.v124.21.1432.1432.

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Abstract Platelet factor 4 (PF4, CXCL4) is a major chemokine in megakaryocytes (megs). It is synthesized almost exclusively by megs during their development and may have important roles in regulating both hematopoietic stem cell and megakaryocyte proliferation. We now show that megs both release significant amounts of PF4 into their environment as well as take up PF4 into alpha granules. This PF4 is then available for release by thrombin activation. We examined PF4 recycling during megakaryopoiesis based on the observation that in vitro-cultured human meg hematopoietic precursors release signi

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19

Krauel, Krystin, Claudia Weber, Sven Brandt, Ulrich Zähringer, Uwe Mamat, Andreas Greinacher, and Sven Hammerschmidt. "Platelet factor 4 binding to lipid A of Gram-negative bacteria exposes PF4/heparin-like epitopes." Blood 120, no. 16 (October 18, 2012): 3345–52. http://dx.doi.org/10.1182/blood-2012-06-434985.

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AbstractThe positively charged chemokine platelet factor 4 (PF4) forms immunogenic complexes with heparin and other polyanions. Resulting antibodies can induce the adverse drug effect heparin-induced thrombocytopenia. PF4 also binds to bacteria, thereby exposing the same neoantigen(s) as with heparin. In this study, we identified the negatively charged lipopolysaccharide (LPS) as the PF4 binding structure on Gram-negative bacteria. We demonstrate by flow cytometry that mutant bacteria with progressively truncated LPS structures show increasingly enhanced PF4 binding activity. PF4 bound stronge

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20

Braga, Diego De Ávila Martins, Juarez Lopes Donzele, Rita Flávia Miranda de Oliveira Donzele, Matheus Faria de Sousa, Evandro Ferreira Cardoso, Igor De Freitas Donzeles, João Paulo de Oliveira, and Jessica Mansur Siqueira Furtado. "Evaluation of the standardized ileal digestible lysine requirement of nursery pigs from 28 to 63 d of age in a three-phase feeding program." Semina: Ciências Agrárias 39, no. 2 (March 15, 2018): 719. http://dx.doi.org/10.5433/1679-0359.2018v39n2p719.

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The objective of this study was to determine the standardized ileal digestible lysine (SID Lys) requirement of nursery pigs from 28 to 63 d of age fed a multi-phase feeding (PF) program and its possible adaptation to SID Lys-deficient diets. Ninety-six commercial hybrid piglets (Topigs Norsvin, 46 castrated males and 50 females) that had been weaned at 28 d of age with an initial body weight of 8.82 ± 0.28 kg were distributed in a randomized block design composed of four treatments, with eight replicates per treatment and three animals per replicate. The treatments were as follows: PF1, SID Ly

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21

Brandt, Sven, Krystin Krauel, Miriam Jaax, Thomas Renné, Christiane A. Helm, Sven Hammerschmidt, Mihaela Delcea, and Andreas Greinacher. "Polyphosphates form antigenic complexes with platelet factor 4 (PF4) and enhance PF4-binding to bacteria." Thrombosis and Haemostasis 114, no. 12 (2015): 1189–98. http://dx.doi.org/10.1160/th15-01-0062.

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SummaryShort chain polyphosphates (polyP) are pro-coagulant and pro-inflammatory platelet released inorganic polymers. The platelet chemokine platelet factor 4 (PF4) binds to lipid A on bacteria, inducing an antibody mediated host defense mechanism, which can be misdirected against PF4/heparin complexes leading to the adverse drug reaction heparin-induced thrombocytopenia (HIT). Here, we demonstrate that PF4 complex formation with soluble short chain polyP contributes to host defense mechanisms. Circular dichroism spectroscopy and isothermal titration calorimetry revealed that PF4 changed its

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22

Fiore, Martine Marie, and Ian J. Mackie. "Dual Effect of Platelet Factor Four on the Activities of Factor Xa." Blood 112, no. 11 (November 16, 2008): 1034. http://dx.doi.org/10.1182/blood.v112.11.1034.1034.

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Abstract Platelet Factor 4 (PF4) is a cationic molecule that binds to heparin with high affinity and neutralises the activity of the latter. Our recent studies indicate that heparin can promote an interaction of fXa with PF4 since neutralization of heparin activity by PF4 was dependent on the concentration of protease. To examine the contribution of PF4 in protease function, fXa activity was determined in chromogenic assays. Upon preincubation with fXa and heparin, PF4 (at a concentration of 100 nM) decreased the kcat of S2765 peptide hydrolysis 4-fold and that of prothrombin activation about

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23

Kowalska, M. Anna, Karine Amirikian, Laurent O. Mosnier, Hartmut Weiler, Sriram Krishnaswamy, and Mortimer Poncz. "Structural and Functional Studies to Define the Molecular Basis by Which Platelet Factor 4 (PF4) Increases Survival of Mice in Lipopolysaccharide (LPS)-Induced Endotoxicity." Blood 112, no. 11 (November 16, 2008): 19. http://dx.doi.org/10.1182/blood.v112.11.19.19.

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Abstract Our previous studies have demonstrated that platelet-released PF4 (chemokine CXCL4) promotes survival in a murine LPS-induced endotoxicity model, although the molecular basis for PF4’s protective effects was not fully defined. We hypothesized that enhanced generation of cytoprotective activated protein C (APC) by PF4 might contribute to the molecular mechanism of PF4’s beneficial effects in vivo, based on the observation that PF4 stimulates protein C (PC) activation by the thrombin/thrombomodulin complex both in vitro and in vivo. Here we show that PF4 in vitro affects human (h) PC ac

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24

Mosnier, Laurent O., Rachel L. Ochoa, and John H. Griffin. "Platelet Factor 4 (PF4) Modulation of Endothelial Protein C Receptor and Thrombomodulin Enhancements of Protein C Activation and TAFI Activation by Thrombin." Blood 108, no. 11 (November 16, 2006): 1791. http://dx.doi.org/10.1182/blood.v108.11.1791.1791.

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Abstract Protein C (PC) activation by thrombin on endothelial cells normally involves thrombomodulin (TM) and the endothelial cell protein C receptor (EPCR), and dysfunction of this mechanism is implicated in a variety of pathologies. Platelet factor 4 (PF4), a releasable platelet alpha-granule protein, stimulates PC activation in vitro and in vivo; PF4 stimulates PC activation in the presence but not in the absence of TM and this requires the PC Gla-domain (Slungaard et al). In contrast to PC activation, we found that thrombin/TM-mediated activation of thrombin-activatable fibrinolysis inhibi

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25

Warkentin, Theodore E., Richard J. Cook, Victor J. Marder, Jo-Ann I. Sheppard, Jane C. Moore, Bengt I. Eriksson, Andreas Greinacher, and John G. Kelton. "Anti–platelet factor 4/heparin antibodies in orthopedic surgery patients receiving antithrombotic prophylaxis with fondaparinux or enoxaparin." Blood 106, no. 12 (December 1, 2005): 3791–96. http://dx.doi.org/10.1182/blood-2005-05-1938.

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Анотація:

Heparin-induced thrombocytopenia (HIT) is caused by platelet-activating IgG antibodies that recognize platelet factor 4 (PF4) bound to heparin. Immunogenicity of heparins differs in that unfractionated heparin (UFH) induces more anti–PF4/heparin antibodies than low-molecular-weight heparin (LMWH) and UFH also causes more HIT. Fondaparinux, a synthetic anticoagulant modeled after the antithrombin-binding pentasaccharide, is believed to be nonimmunogenic. We tested 2726 patients for anti–PF4/heparin antibodies after they were randomized to receive antithrombotic prophylaxis with fondaparinux or

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26

Krauel, Krystin, Christine Hackbarth, Birgitt Fürll, and Andreas Greinacher. "Heparin-induced thrombocytopenia: in vitro studies on the interaction of dabigatran, rivaroxaban, and low-sulfated heparin, with platelet factor 4 and anti-PF4/heparin antibodies." Blood 119, no. 5 (February 2, 2012): 1248–55. http://dx.doi.org/10.1182/blood-2011-05-353391.

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Abstract Heparin is a widely used anticoagulant. Because of its negative charge, it forms complexes with positively charged platelet factor 4 (PF4). This can induce anti-PF4/heparin IgG Abs. Resulting immune complexes activate platelets, leading to the prothrombotic adverse drug reaction heparin-induced thrombocytopenia (HIT). HIT requires treatment with alternative anticoagulants. Approved for HIT are 2 direct thrombin inhibitors (DTI; lepirudin, argatroban) and danaparoid. They are niche products with limitations. We assessed the effects of the DTI dabigatran, the direct factor Xa-inhibitor

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27

K. Ahmed, Dua'a, and Balkis A. Kamal. "Formulation and Optimization of Oral Fast Dissolving Prochloperazine Maleate Tablets." Iraqi Journal of Pharmaceutical Sciences ( P-ISSN 1683 - 3597 E-ISSN 2521 - 3512) 21, no. 1 (March 28, 2017): 46–55. http://dx.doi.org/10.31351/vol21iss1pp46-55.

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Prochloperazine maleate (PCM) is one of the most prescribed phenothiazine. The purpose of the present research was to develop fast dissolving tablets of PCM with Î²-cyclodextrin inclusion complex. Tablets prepared by wet granulation with sublimation and by using different superdisintegrants type [ low-hydroxypropylcellulose LH21 (L-HPC LH21), carboxymethylcellulose calcium (ECG505), crospovidone (CP)], and different type of subliming agents (urea and ammonium bicarbonate (AB)). Tablets evaluated for its % friability, disintegration time, wetting time, hardness, content uniformity, weight varia

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Singh, Bandana, Adam Kanack, Antonios Bayas, Gemlyn George, Mouhamed Yazan Abou Abou-Ismail, Mindy Kohlhagen, Monika Christ, et al. "Monoclonal and Oligoclonal Anti-PF4 Antibodies Mediate VITT." Blood 138, Supplement 1 (November 5, 2021): 3220. http://dx.doi.org/10.1182/blood-2021-153307.

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Abstract Background: ChAdOx1 nCoV-19 (AstraZeneca) and Ad26.COV2.S (Janssen Johnson & Johnson) vaccines against COVID-19 have been associated with thrombotic thrombocytopenic reactions referred to as vaccine-induced immune thrombotic thrombocytopenia (VITT) characterized by the presence of platelet-activating, anti-PF4 antibodies. While VITT shares key clinical features with a similar but separate entity, Heparin-induced thrombocytopenia (HIT), there appear to be important differences: 1) VITT patients have extremely high thrombosis rates and are very strongly positive in PF4-polyanion ELI

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Meyer, Sara C., Eva Steinmann, Thomas Lehmann, Patricia Muesser, Jakob R. Passweg, Radek C. Skoda, and Dimitrios A. Tsakiris. "Anti-Platelet Factor 4/Heparin Antibody Formation Occurs Endogenously and at Unexpected High Frequency in Polycythemia Vera." BioMed Research International 2017 (2017): 1–13. http://dx.doi.org/10.1155/2017/9876819.

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Background.Myeloproliferative neoplasms (MPN) encounter thromboses due to multiple known risk factors. Heparin-induced thrombocytopenia (HIT) is a thrombotic syndrome mediated by anti-platelet factor 4 (PF4)/heparin antibodies with undetermined significance for thrombosis in MPN. We hypothesized that anti-PF4/heparin Ab might occur in MPN and promote thrombosis.Methods.Anti-PF4/heparin antibodies were analyzed in 127 MPN patients including 76 PV and 51 ET. Screening, validation testing, and isotype testing of anti-PF4/heparin Ab were correlated with disease characteristics.Results.Anti-PF4/hep

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Pongas, Georgios, Swapan Dasgupta, and Perumal Thiagarajan. "Anti-Platelet Factor 4/Heparin Antibodies in Patients with Gram Negative Bacteremia." Blood 120, no. 21 (November 16, 2012): 3391. http://dx.doi.org/10.1182/blood.v120.21.3391.3391.

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Abstract Abstract 3391 Introduction The anti-platelet factor 4(PF4)/heparin antibodies, arising as a result of previous heparin exposure, are causally related to the procoagulant state due to platelet and monocyte activation. Formation of these antibodies with subsequent thrombocytopenia or thrombosis has also been described in patients, who have not been previously exposed to heparin. The presence of anti-PF4/heparin antibodies in individuals correlates with the severity of periodontal disease, implying that their occurrence may be triggered by periodontal pathogens. In this study, we determi

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von Hundelshausen, Philipp, Rory R. Koenen, Markus Sack, Sebastian F. Mause, Wencke Adriaens, Amanda E. I. Proudfoot, Tilman M. Hackeng, and Christian Weber. "Heterophilic interactions of platelet factor 4 and RANTES promote monocyte arrest on endothelium." Blood 105, no. 3 (February 1, 2005): 924–30. http://dx.doi.org/10.1182/blood-2004-06-2475.

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AbstractThe chemokines platelet factor 4 (PF4) and RANTES (regulated on activation normal T cell expressed and secreted) are secreted by activated platelets and influence multiple cell types and biologic processes. For instance, PF4 inhibits progenitor cell proliferation and angiogenesis, while platelet-derived RANTES is involved in vascular recruitment of monocytes. However, little is known about functional interactions of PF4 and RANTES. Here we show that the presence of PF4 enhanced the arrest of RANTES-stimulated monocytes and monocytic cells on activated endothelial cells under flow condi

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Liu, Chao Yan, Rhonda A. Geoffrey, Qi-Hong Sun, and Gian Paolo Visentin. "Identification of Critical Amino Acids in Human Platelet Factor 4 (PF4) Required for Its Modulatory Effects on CD4+CD25+ Regulatory T Cells." Blood 104, no. 11 (November 16, 2004): 1339. http://dx.doi.org/10.1182/blood.v104.11.1339.1339.

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Abstract Human platelet factor 4 (PF4; CXCL4), a heparin-binding CXC chemokine contained in platelet α-granules, is secreted upon activation of platelets. Several reports have identified PF4 as an inhibitor of hematopoietic progenitor and endothelial cell proliferation and angiogenesis. Furthermore, PF4 has been shown to strongly inhibit T cell proliferation as well as IFN-γ and IL-2 release by activated T cells. We have recently reported that human PF4 inhibits the proliferative response of human CD4+CD25− T cells, while inducing expansion of CD4+CD25+ T regulatory (Tr) cells stimulated by an

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Kowalska, M. Anna, Lubica Rauova, Vincent Hayes, Douglas B. Cines, Daniel W. Bougie, Richard H. Aster, Sriram Krishnaswamy, and Mortimer Poncz. "Heparin-Induced Thrombocytopenia Antibodies Inhibit PF4-Dependent Enhancement of Activated Protein C Formation by Binding to Antigenic Complexes Formed with the Chondroitin Sulfate Side-Chain of Thrombomodulin." Blood 116, no. 21 (November 19, 2010): 721. http://dx.doi.org/10.1182/blood.v116.21.721.721.

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Abstract Abstract 721 Previous studies have shown that platelet factor 4 (PF4) increases activated protein C (aPC) generation both in vitro and in vivo. PF4 increase of aPC generation by thrombin (IIa) and thrombomodulin (TM) complex followed a bell-shaped curve when tested in solution, on human TM expressing HEK293 and on endothelial cells. PF4 failed to enhance aPC in the presence of chondroitin sulfate (CS)-free TM. These results were consistent with PF4 binding to the CS on the TM glycosaminoglycan (GAG) domain and forming complexes that are similar to PF4/GAG antigenic complexes seen in h

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Krauel, Krystin, Patricia Preuße, Theodore E. Warkentin, Catja Trabhardt, Sven Brandt, Inga Jensch, Martin Mandelkow, Elke Hammer, Sven Hammerschmidt, and Andreas Greinacher. "Fibronectin modulates formation of PF4/heparin complexes and is a potential factor for reducing risk of developing HIT." Blood 133, no. 9 (February 28, 2019): 978–89. http://dx.doi.org/10.1182/blood-2018-05-850370.

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Abstract Heparin-induced thrombocytopenia (HIT) is caused by platelet-activating anti–platelet factor 4 (PF4)/heparin antibodies. Platelet activation assays that use “washed” platelets are more sensitive for detecting HIT antibodies than platelet-rich plasma (PRP)–based assays. Moreover, heparin-exposed patients vary considerably with respect to the risk of PF4/heparin immunization and, among antibody-positive patients, the risk of subsequent “breakthrough” of clinical HIT with manifestation of thrombocytopenia. We used washed platelets and PRP, standard laboratory HIT tests, and physicochemic

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Sartori, Maria Teresa, Chiara Zurlo, Maria Bon, Antonella Bertomoro, Raffaele Bendo, Irene Bertozzi, Claudia Maria Radu, Elena Campello, Paolo Simioni, and Fabrizio Fabris. "Platelet-Derived Microparticles Bearing PF4 and Anti-GAGS Immunoglobulins in Patients with Sepsis." Diagnostics 10, no. 9 (August 24, 2020): 627. http://dx.doi.org/10.3390/diagnostics10090627.

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PF4 is a megakaryocyte-derived cationic chemokine that plays a part in innate immunity through its activity on the macrophages. In bacterial sepsis, PF4 binds to glycosaminoglycans (GAGs) on the surface of aerobic bacteria, giving rise to an antigenic complex that induces the early formation of anti-PF4 IgG-IgA-IgM. This triggers the immune response in patients receiving heparin therapy who develop heparin-induced thrombocytopenia (HIT). These antibodies have also been identified in patients with chronic Gram-negative infections. Given the complexity of this innate immune response network, our

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Sachais, Bruce S., Tiffany Turrentine, Jeanine M. Dawicki-McKenna, Daniel J. Rader, and M. Anna Kowalska. "Elimination of Platelet Factor 4 (PF4) from Platelets Reduces Atherosclerosis and Increases HDL Cholesterol in C57Bl/6 and ApoE−/− Mice." Blood 108, no. 11 (November 16, 2006): 418. http://dx.doi.org/10.1182/blood.v108.11.418.418.

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Abstract There is a presence of circulating, activated platelets in blood of patients with atherosclerosis, coronary disease and hypercholesterolemia. Upon activation, platelets release a large amount of platelet factor 4 (PF4), a platelet specific chemokine. Our laboratory has previously demonstrated several potentially proatherogenic properties of PF4 including alteration of LDL metabolism and cellular trafficking, and activation of NFkB, a proinflammatory transcription factor involved in atherosclerosis. We have also localized PF4 to human atherosclerotic lesions. However, to date, no direc

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37

Podolnikova, Nataly P., Valentin P. Yakubenko, and Tatiana P. Ugarova. "Platelet Factor 4 Induces Leukocyte Responses through Integrin Mac-1 (CD11b/CD18)." Blood 128, no. 22 (December 2, 2016): 2529. http://dx.doi.org/10.1182/blood.v128.22.2529.2529.

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Abstract The proteins/peptides secreted from α-granules of activated platelets not only aid in thrombus formation and blood coagulation, but also exert various immune-modulating effects. Among many secreted products, Platelet Factor 4 (PF4), a chemokine that belongs to the CXC family, is one of the most abundant platelet proteins. While PF4 assignment to the chemokine family is based on its structural similarity with other CXC chemokines and chemotactic activity, to date no receptor for PF4 on leukocytes has been identified. Our recent elucidation of the recognition specificity of a major leuk

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38

Green, C. J., R. S. Charles, B. F. Edwards, and P. H. Johnson. "Identification and characterization of PF4varl, a human gene variant of platelet factor 4." Molecular and Cellular Biology 9, no. 4 (April 1989): 1445–51. http://dx.doi.org/10.1128/mcb.9.4.1445-1451.1989.

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A synthetic DNA probe designed to detect coding sequences for platelet factor 4 and connective tissue-activating peptide III (two human platelet alpha-granule proteins) was used to identify several similar sequences in total human DNA. Sequence analysis of a corresponding 3,201-base-pair EcoRI fragment isolated from a human genomic library demonstrated the existence of a variant of platelet factor 4, designated PF4var1. The gene for PF4var1 consisted of three exons and two introns. Exon 1 coded for a 34-amino-acid hydrophobic leader sequence that had 70% sequence homology with the leader seque

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39

Green, C. J., R. S. Charles, B. F. Edwards, and P. H. Johnson. "Identification and characterization of PF4varl, a human gene variant of platelet factor 4." Molecular and Cellular Biology 9, no. 4 (April 1989): 1445–51. http://dx.doi.org/10.1128/mcb.9.4.1445.

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Анотація:

A synthetic DNA probe designed to detect coding sequences for platelet factor 4 and connective tissue-activating peptide III (two human platelet alpha-granule proteins) was used to identify several similar sequences in total human DNA. Sequence analysis of a corresponding 3,201-base-pair EcoRI fragment isolated from a human genomic library demonstrated the existence of a variant of platelet factor 4, designated PF4var1. The gene for PF4var1 consisted of three exons and two introns. Exon 1 coded for a 34-amino-acid hydrophobic leader sequence that had 70% sequence homology with the leader seque

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40

Joglekar, Manali V., Sanjay Khandelwal, Mortimer Poncz, Lubica Rauova, and Gowthami M. Arepally. "Understanding the Underlying Immune Response in HIT: Uptake of PF4/Heparin Complexes By Monocytes & Dendritic Cells." Blood 124, no. 21 (December 6, 2014): 4197. http://dx.doi.org/10.1182/blood.v124.21.4197.4197.

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Abstract Platelet Factor 4 (PF4), a strongly positive-charged small protein, and the negatively-charged polymer heparin (Hep) form ultra-large complexes (ULCs) that have several unusual features including their remarkable stability and their ability to elicit a robust antibody response in vivo (Rauova L; Blood 2005 and Suvarna S, Blood 2005). Recently, we and others have shown that similar complexes of another positively charged protein, protamine sulfate with heparin can also lead to a clinically relevant immune response. To better understand the cellular basis for PF4/Hep antibody formation,

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41

Xiao, Liqing, Mortimer Poncz, and Michele Lambert. "Platelet Factor 4 (PF4) Causes Cell Cycle Arrest in Megakaryocytes (Megs) by Inactivating CDC2 (CDK1) and CDK2." Blood 120, no. 21 (November 16, 2012): 1238. http://dx.doi.org/10.1182/blood.v120.21.1238.1238.

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Abstract Abstract 1238 PF4 (CXCL4), a platelet specific chemokine released in large amounts from activated platelet α -granules, is a negative regulator of megakaryopoiesis. In mouse studies, we have shown that PF4 levels regulate steady-state platelet count and impact chemotherapy and radiation-induced thrombocytopenia. In a clinical study in leukemia patients, we found that PF4 levels were inversely related to steady-state platelet count and to recovery after chemotherapy. The molecular basis for the effect of PF4 in megakaryopoiesis is largely unknown. Our studies in cell models suggested t

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42

Rauova, Lubica, Li Zhai, M. Anna Kowalska, Gowthami M. Arepally, Douglas B. Cines, and Mortimer Poncz. "Role of platelet surface PF4 antigenic complexes in heparin-induced thrombocytopenia pathogenesis: diagnostic and therapeutic implications." Blood 107, no. 6 (March 15, 2006): 2346–53. http://dx.doi.org/10.1182/blood-2005-08-3122.

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AbstractHeparin-induced thrombocytopenia (HIT) antibodies recognize complexes between heparin and platelet factor 4 (PF4). Heparin and PF4 bind HIT antibodies only over a narrow molar ratio. We explored the involvement of platelet surface–bound PF4 as an antigen in the pathogenesis of experimental HIT. We show that cell-surface PF4 complexes are also antigenic only over a restricted concentration range of PF4. Heparin is not required for HIT antibody binding but shifts the concentration of PF4 needed for optimal surface antigenicity to higher levels. These data are supported by in vitro studie

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Amiral, J., F. Bridey, M. Wolf, C. Boyer-Neumann, E. Fressinaud, A. M. Vissac, E. Peynaud-Debayle, M. Dreyfus, and D. Meyer. "Antibodies to Macromolecular Platelet Factor 4-Heparin Complexes in Heparin-induced Thrombocytopenia: a Study of 44 Cases." Thrombosis and Haemostasis 73, no. 01 (1995): 021–28. http://dx.doi.org/10.1055/s-0038-1651670.

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SummaryAs heparin-PF4 (H-PF4) complexes are the target for antibodies associated to heparin-induced thrombocytopenia (HIT), an ELISA has been developed and optimised for testing antibodies binding to H-PF4. This test was consistently negative in 50 healthy subjects (A492 <0.3) and 35 patients with other causes of thrombocytopenia (A492 <0.5). In contrast, 43 out of 44 HIT patients showed antibodies to H-PF4 (A492 = 1.70 ± 0.81) including 5 patients with a negative platelet aggregation test. In one patient with HIT, antibodies to H-PF4 were already present at day 7, whereas platelet count

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44

Dudek, Arkadiusz Z., Irina Nesmelova, Kevin Mayo, Catherine M. Verfaillie, Simon Pitchford, and Arne Slungaard. "Platelet factor 4 promotes adhesion of hematopoietic progenitor cells and binds IL-8: novel mechanisms for modulation of hematopoiesis." Blood 101, no. 12 (June 15, 2003): 4687–94. http://dx.doi.org/10.1182/blood-2002-08-2363.

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AbstractPlatelet factor 4 (PF4) is an abundant platelet α-granule C-X-C chemokine that has weak chemotactic potency but strongly inhibits hematopoiesis through an unknown mechanism. We find that PF4 binds to human CD34+ hematopoietic progenitor cells (HPCs) with a median effective concentration of 1 μg/mL but not after exposure to chondroitinase ABC. PF4 enhances adhesion of HPCs to intact stroma. Committed progenitors also adhere avidly to immobilized PF4. This adhesion is time-dependent, requires metabolic activity, causes cytoskeletal rearrangement, and induces cell-cycle inhibition. Using

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45

Brandt, Sven, Krystin Krauel, Kay E. Gottschalk, Thomas Renné, Christiane A. Helm, Andreas Greinacher, and Stephan Block. "Characterisation of the conformational changes in platelet factor 4 induced by polyanions: towards in vitro prediction of antigenicity." Thrombosis and Haemostasis 112, no. 07 (2014): 53–64. http://dx.doi.org/10.1160/th13-08-0634.

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SummaryHeparin-induced thrombocytopenia (HIT) is the most frequent drug-induced immune reaction affecting blood cells. Its antigen is formed when the chemokine platelet factor 4 (PF4) complexes with polyanions. By assessing polyanions of varying length and degree of sulfation using immunoassay and circular dichroism (CD)-spectroscopy, we show that PF4 structural changes resulting in antiparallel β-sheet content >30% make PF4/polyanion complexes antigenic. Further, we found that polyphosphates (polyP-55) induce antigenic changes on PF4, whereas fondaparinux does not. We provide a model sugge

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Zheng, Yongwei, Wen Zhu, Dipica Haribhai, Calvin B. Williams, Richard H. Aster, Renren Wen, and Demin Wang. "Regulatory T Cells Control PF4/Heparin Antibody Production in Mice." Blood 132, Supplement 1 (November 29, 2018): 2542. http://dx.doi.org/10.1182/blood-2018-99-113049.

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Abstract Heparin-induced thrombocytopenia (HIT) is an immune-mediated disorder that can cause fatal arterial or venous thrombosis/thromboembolism. Immune complexes consisting of heparin, platelet factor 4 (PF4) and PF4/heparin-reactive antibodies are central to the pathogenesis of HIT. Regulatory T (Treg) cells are a subpopulation of CD4 T cells that modulate immune system by suppressing or down-regulating immune response and play an important role in immune homeostasis. However, the role of Treg cells in controlling PF4/heparin-specific antibody production is not known. Here we found that Fox

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47

Cini, Michela, Caterina Pili, Ottavio Boggian, Mirella Frascaro, Gualtiero Palareti, and Cristina Legnani. "Evaluation of a new automated panel of assays for the detection of anti-PF4/heparin antibodies in patients suspected of having heparin-induced thrombocytopenia." Thrombosis and Haemostasis 104, no. 08 (2010): 402–9. http://dx.doi.org/10.1160/th10-01-0002.

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SummaryHeparin-induced thrombocytopenia (HIT) is a life-threatening complication of heparin treatment; the prognosis depends on early and accurate diagnosis, and prompt start of alternative anticoagulants. Because of high sensitivity, the commercially available immunologic assays are widely used, though not suited to be run on single samples and with a turnaround time of 2–3 hours. We evaluated two new, rapid, automated, semi-quantitative chemiluminescent immunoassays in HIT suspected patients: HemosIL® AcuStar HIT-IgG(PF4-H) (specific for IgG anti- PF4/heparin antibodies) and HemosIL® AcuStar

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Lambert, Michele, Samriddhi S. Sharma, Liqing Xiao, Stephen Marcus, and Mortimer Poncz. "2-O, 3-O-Desulfated Heparin (ODSH) Mitigates Chemotherapy-Induced Thrombocytopenia (CIT) by Blocking the Negative Paracrine Effect of Platelet Factor 4 (PF4) On Megakaryopoiesis." Blood 120, no. 21 (November 16, 2012): 386. http://dx.doi.org/10.1182/blood.v120.21.386.386.

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Abstract Abstract 386 Thrombocytopenia is a significant complication of myelosuppressive chemotherapy treatments, which are a mainstay in cancer therapy. We and others have previously shown that PF4 is a negative paracrine affecting megakaryocyte number in culture. In murine studies we showed that platelet PF4 levels are inversely related to steady-state platelet counts and is a major contributor to the duration and severity of CIT. Recently, we have shown that PF4 influences both steady-state platelet count and platelet count recovery in pediatric patients treated for acute lymphoblastic leuk

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49

Levine, SP, LK Knieriem, and MA Rager. "Platelet factor 4 and the platelet secreted proteoglycan: immunologic characterization by crossed immunoelectrophoresis." Blood 75, no. 4 (February 15, 1990): 902–10. http://dx.doi.org/10.1182/blood.v75.4.902.902.

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Abstract Platelet factor 4 (PF4) is a hydrophobic, alpha-granule protein with potent antiheparin activity. It also binds to a chondroitin sulfate- containing proteoglycan (PG) isolated from platelets. In order to evaluate further the relationship between PF4 and the chondroitin sulfate-containing proteoglycan in resting platelets, the PF4-binding proteoglycan from human platelets has been purified using purified PF4 as an affinity ligand and used to prepare polyclonal antiserum. Two antisera have been characterized: one reacts primarily with chondroitin sulfate (CS), the other reacts with the

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50

Levine, SP, LK Knieriem, and MA Rager. "Platelet factor 4 and the platelet secreted proteoglycan: immunologic characterization by crossed immunoelectrophoresis." Blood 75, no. 4 (February 15, 1990): 902–10. http://dx.doi.org/10.1182/blood.v75.4.902.bloodjournal754902.

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Анотація:

Platelet factor 4 (PF4) is a hydrophobic, alpha-granule protein with potent antiheparin activity. It also binds to a chondroitin sulfate- containing proteoglycan (PG) isolated from platelets. In order to evaluate further the relationship between PF4 and the chondroitin sulfate-containing proteoglycan in resting platelets, the PF4-binding proteoglycan from human platelets has been purified using purified PF4 as an affinity ligand and used to prepare polyclonal antiserum. Two antisera have been characterized: one reacts primarily with chondroitin sulfate (CS), the other reacts with the protein c

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