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Journal articles on the topic 'Blood platelets Platelet activation'

Author: Grafiati

Published: 4 June 2021

Last updated: 15 February 2022

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1

O'Sullivan, Brian P., Matthew D. Linden, Andrew L. Frelinger, et al. "Platelet activation in cystic fibrosis." Blood 105, no. 12 (2005): 4635–41. http://dx.doi.org/10.1182/blood-2004-06-2098.

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Abstract Cystic fibrosis (CF) is caused by a mutation of the gene encoding the cystic fibrosis transmembrane conductance regulator (CFTR). We examined platelet function in CF patients because lung inflammation is part of this disease and platelets contribute to inflammation. CF patients had increased circulating leukocyte-platelet aggregates and increased platelet responsiveness to agonists compared with healthy controls. CF plasma caused activation of normal and CF platelets; however, activation was greater in CF platelets. Furthermore, washed CF platelets also showed increased reactivity to

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2

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

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SummaryPlatelet activation and blood coagulation are complementary, mutually dependent processes in haemostasis and thrombosis. Platelets interact with several coagulation factors, while the coagulation product thrombin is a potent platelet-activating agonist. Activated platelets come in a procoagulant state after a prolonged elevation in cytosolic [Ca2+]i. Such platelets, e. g. when adhering to collagen via glycoprotein VI, expose phosphatidylserine (PS) at their outer surface and produce (PS-exposing) membrane blebs and microvesicles. Inhibition of aminophospholipid translocase and activatio

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3

DeHelian, Daniel, Shuchi Gupta, Jie Wu, et al. "RGS10 and RGS18 differentially limit platelet activation, promote platelet production, and prolong platelet survival." Blood 136, no. 15 (2020): 1773–82. http://dx.doi.org/10.1182/blood.2019003251.

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Abstract G protein–coupled receptors are critical mediators of platelet activation whose signaling can be modulated by members of the regulator of G protein signaling (RGS) family. The 2 most abundant RGS proteins in human and mouse platelets are RGS10 and RGS18. While each has been studied individually, critical questions remain about the overall impact of this mode of regulation in platelets. Here, we report that mice missing both proteins show reduced platelet survival and a 40% decrease in platelet count that can be partially reversed with aspirin and a P2Y12 antagonist. Their platelets ha

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Nolfi-Donegan, Deirdre, Sruti Shiva, and Cheryl A. Hillery. "HMGB1 As a Novel Platelet Agonist That Acts Synergistically with ADP to Activate Platelets in Sickle Cell Disease." Blood 132, Supplement 1 (2018): 1073. http://dx.doi.org/10.1182/blood-2018-99-110269.

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Abstract Background: Sickle cell disease (SCD) is a proinflammatory and prothrombotic disorder that exhibits increased platelet activation. High mobility group box 1 (HMGB1) is a nuclear protein that can mediate inflammation when released from inflammatory or ischemic cells. HMGB1 is increased in many inflammatory disease states including SCD. Recent data suggests HMGB1 activates platelets and may work synergistically with potent platelet agonists such as collagen and thrombin, but little is known regarding HMGB1-platelet interactions in combination with weaker agonists like ADP, or in isolate

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Nolfi-Donegan, Deirdre, Gowtham K. Annarapu, Cheryl A. Hillery, and Sruti Shiva. "HMGB1-Mediated Platelet Activation Is Independent of Platelet Mitochondrial Reactive Oxygen Species Generation." Blood 136, Supplement 1 (2020): 6. http://dx.doi.org/10.1182/blood-2020-141160.

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Background: Sickle cell disease (SCD) is a hemolytic disorder that exhibits pathologic platelet activation. Notably, hemolysis is tightly associated with platelet activation and thrombotic complications of SCD such as stroke, leg ulceration, and pulmonary hypertension. To this end, we and others have shown that free hemoglobin (Hb) released into the plasma via hemolysis directly activates healthy platelets ex vivo in a concentration-dependent manner. Treatment with Hb stimulates the production of mitochondrial reactive oxygen species (mtROS) within the platelet, resulting in thrombotic activat

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6

Sadoul, Karin, Jin Wang, Boubou Diagouraga, et al. "HDAC6 controls the kinetics of platelet activation." Blood 120, no. 20 (2012): 4215–18. http://dx.doi.org/10.1182/blood-2012-05-428011.

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Abstract HDAC6, a major cytoplasmic deacetylase, is shown here to fine-tune the kinetics of platelet activation, a process that must be precisely regulated to ensure hemostasis after blood vessel injury while preventing pathologic thrombus formation. The discoid shape of resting platelets in the circulation is maintained by several highly acetylated microtubules organized in a marginal band. During platelet activation, microtubules undergo major reorganizations, which contribute to the shape change of activating platelets. We show that, during these activation-induced shape changes, a dramatic

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7

Storrie, Brian, Sung W. Rhee, Irina D. Pokrovskaya, et al. "Platelet Activation State Intermixing in a Venous Puncture Model Indicates Novel Patterns of Thrombus Formation." Blood 134, Supplement_1 (2019): 9. http://dx.doi.org/10.1182/blood-2019-130805.

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Introduction: Platelet recruitment to generate a thrombus is key to bleeding cessation. That recruitment is dependent on a series of platelet activation processes that include adhesion to the exposed vessel matrix, platelet-platelet adhesion and platelet granule release. How platelet activation is patterned to generate a thrombus has previously been studied by intravital light microscopy, two-photon microscopy and scanning electron microscopy at resolutions insufficient to infer platelet activation at the level of the individual platelet. Here, we present a collaborative effort to stratify spa

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Annarapu, Gowtham K., Deirdre Nolfi-Donegan, Anuradha Bharara Singh, Michael Reynolds, and Sruti Shiva. "Heme Induced Platelet Mitochondrial Oxidant Production Regulates Thrombospondin-1 Release from Platelets." Blood 136, Supplement 1 (2020): 30. http://dx.doi.org/10.1182/blood-2020-142640.

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Background: Sickle Cell Disease (SCD) patients develop chronic vasculopathy leading to conditions such as pulmonary hypertension (PH), a major cause of morbidity and mortality. Vasculopathy is tightly associated with hemolysis in SCD. We and others have shown that in SCD, hemolysis activates platelets, and activated platelets are implicated in vasculopathy through their release of vasoactive molecules, such as thrombosponding-1 (TSP1), from storage granules. In SCD, free heme is accumulated in the circulation as a consequence of oxidative degradation of hemoglobin secondary to intravascular he

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9

Zhang, Guoying, Binggang Xiang, Anping Dong, et al. "Biphasic roles for soluble guanylyl cyclase (sGC) in platelet activation." Blood 118, no. 13 (2011): 3670–79. http://dx.doi.org/10.1182/blood-2011-03-341107.

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AbstractNitric oxide (NO) stimulates cGMP synthesis by activating its intracellular receptor, soluble guanylyl cyclase (sGC). It is a currently prevailing concept that No and cGMP inhibits platelet function. However, the data supporting the inhibitory role of NO/sGC/cGMP in platelets have been obtained either in vitro or using whole body gene deletion that affects vessel wall function. Here we have generated mice with sGC gene deleted only in megakaryocytes and platelets. Using the megakaryocyte- and platelet-specific sGC-deficient mice, we identify a stimulatory role of sGC in platelet activa

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10

Mosnier, Laurent O., Paula Buijtenhuijs, Pauline F. Marx, Joost C. M. Meijers, and Bonno N. Bouma. "Identification of thrombin activatable fibrinolysis inhibitor (TAFI) in human platelets." Blood 101, no. 12 (2003): 4844–46. http://dx.doi.org/10.1182/blood-2002-09-2944.

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AbstractThrombin activatable fibrinolysis inhibitor (TAFI) is a carboxypeptidase B-like proenzyme that after activation down-regulates fibrinolysis. Platelets are known to contain antifibrinolytic factors that are secreted during platelet activation. Therefore, the presence of TAFI in platelets was analyzed. TAFI was identified in platelets in a concentration of about 50 ng/1 × 109 platelets and was secreted on platelet activation. Thrombin-mediated activation of platelet-derived TAFI resembled that of plasma-derived TAFI with respect to stimulation by thrombomodulin and spontaneous loss of ac

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Weng, Zhen, Ding Li, Lin Zhang, et al. "PTEN regulates collagen-induced platelet activation." Blood 116, no. 14 (2010): 2579–81. http://dx.doi.org/10.1182/blood-2010-03-277236.

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Abstract Phosphatidylinositol 3-kinase (PI3K) has been shown to play an important role in collagen-induced platelet activation, but the role(s) of PTEN, a major regulator of the PI3K/Akt signaling pathway, has not been examined in platelets. Here, we report that Pten−/− mouse blood contains 25% more platelets than Pten+/+ blood and that PTEN deficiency significantly shortened the bleeding time, increased the sensitivity of platelets to collagen-induced activation and aggregation, and enhanced phosphorylation of Akt at Ser473 in response to collagen. Furthermore, we found that PP2, and the comb

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12

Lagarrigue, Frederic, David S. Paul, Alexandre R. Gingras, et al. "Talin-1 is the principal platelet Rap1 effector of integrin activation." Blood 136, no. 10 (2020): 1180–90. http://dx.doi.org/10.1182/blood.2020005348.

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Abstract Ras-related protein 1 (Rap1) is a major convergence point of the platelet-signaling pathways that result in talin-1 binding to the integrin β cytoplasmic domain and consequent integrin activation, platelet aggregation, and effective hemostasis. The nature of the connection between Rap1 and talin-1 in integrin activation is an important remaining gap in our understanding of this process. Previous work identified a low-affinity Rap1-binding site in the talin-1 F0 domain that makes a small contribution to integrin activation in platelets. We recently identified an additional Rap1-binding

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13

Jobe, Shawn M., Katina M. Wilson, Lorie Leo, et al. "Critical role for the mitochondrial permeability transition pore and cyclophilin D in platelet activation and thrombosis." Blood 111, no. 3 (2008): 1257–65. http://dx.doi.org/10.1182/blood-2007-05-092684.

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Abstract Many of the cellular responses that occur in activated platelets resemble events that take place following activation of cell-death pathways in nucleated cells. We tested the hypothesis that formation of the mitochondrial permeability transition pore (MPTP), a key signaling event during cell death, also plays a critical role in platelet activation. Stimulation of murine platelets with thrombin plus the glycoprotein VI agonist convulxin resulted in a rapid loss of mitochondrial transmembrane potential (Δψm) in a subpopulation of activated platelets. In the absence of cyclophilin D (Cyp

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14

Larson, Mark K., Hong Chen, Mark L. Kahn, et al. "Identification of P2Y12-dependent and -independent mechanisms of glycoprotein VI–mediated Rap1 activation in platelets." Blood 101, no. 4 (2003): 1409–15. http://dx.doi.org/10.1182/blood-2002-05-1533.

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Glycoprotein (GP) VI is a critical platelet collagen receptor, yet the steps involved in GPVI-mediated platelet activation remain incompletely understood. Because activation of Rap1, an abundant small guanosine triphosphatase (GTPase) in platelets, contributes to integrin αIIbβ3 activation, we asked whether and how GPVI signaling activates Rap1 in platelets. Here we show that platelet Rap1 is robustly activated upon addition of convulxin, a GPVI-specific agonist. Using a reconstituted system in RBL-2H3 cells, we found that GPVI-mediated Rap1 activation is dependent on FcRγ but independent of a

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15

O'Brien, Kelly A., Aleksandra Stojanovic-Terpo, Nissim Hay, and Xiaoping Du. "An important role for Akt3 in platelet activation and thrombosis." Blood 118, no. 15 (2011): 4215–23. http://dx.doi.org/10.1182/blood-2010-12-323204.

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Abstract The Akt family of serine/threonine kinases includes Akt1, Akt2, and Akt3 isoforms. Prior studies have reported that Akt1 and Akt2, but not Akt3, are expressed in platelets. Here, we show that Akt3 is expressed in substantial amounts in platelets. Akt3−/− mouse platelets selectively exhibit impaired platelet aggregation and secretion in response to low concentrations of thrombin receptor agonists and thromboxane A2 (TXA2), but not collagen or VWF. In contrast, platelets from Akt1−/− or Akt2−/− mice are defective in platelet activation induced by thrombin, TXA2, and VWF, but only Akt1−/

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16

Marjanovic, Jasna, Brad Rumancik, Luke Weber, et al. "Phosphatidylinositol-3,4-Bisphosphate-Akt Signaling Pathway Promotes Platelet Activation." Blood 132, Supplement 1 (2018): 1131. http://dx.doi.org/10.1182/blood-2018-99-115066.

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Abstract Phosphatidylinositol-3,4-bisphosphate (PtdIns(3,4)P2) is a messenger that accumulates in platelets in a phosphoinositide 3-kinase and platelet aggregation-dependent manner. PtdIns(3,4)P2 is broken down by inositol polyphosphate 4-phosphatases, type I (INPP4A) and type II (INPP4B). These enzymes do not catalyze hydrolysis of phosphoinositides other than PtdIns(3,4)P2, and therefore provide unique means for studying the role of this lipid in platelet activation. We have found that the dominant isoform of 4-phosphatases expressed in platelets is INPP4A and we have generated radiation chi

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17

Panes, Olga, M. Francisca Becerra, Roger Valle та ін. "Gpibα Engagement Induces Activation of Human Platelet TF and Association with Constitutively Platelet Surface-Bound FVIIa". Blood 134, Supplement_1 (2019): 2337. http://dx.doi.org/10.1182/blood-2019-126359.

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The membranes of activated platelets assemble clotting protein complexes and enzymatic reactions needed for hemostasis and causing pathological thrombosis. Several reports have shown that human platelets contain TF, but controversies remain on the functional contributions of platelet TF to coagulation initiation. Here, we delineate the mechanism that converts platelet-associated TF to a procoagulant molecule. By combining specific inhibitors with human platelets from normal probands or patients with Glanzmann thrombasthenia or homozygous GPVI deficiency, we analyzed the procoagulant activation

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Prete, Alexander, Alexander Urtula, and Renata Grozovsky. "Sialic Acid Content on Platelet Surface Glycoproteins Modulates Thrombin-Induced Activation." Blood 132, Supplement 1 (2018): 3730. http://dx.doi.org/10.1182/blood-2018-99-119303.

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Abstract Platelets are fundamentally important in normal hemostasis and pathological thrombosis (i.e. cardiovascular diseases, stroke, etc.). Platelets mediate the initial first-step in hemostasis through surface glycoproteins like the GPIb-IX-V complex and integrin αIIbβ3 (GPIIbIIIa). Although the functions of platelet surface glycoproteins are well known, the roles of posttranslational modifications on those surface glycoproteins are poorly understood. We have recently shown that sialic acid is a key regulator of platelet survival. As platelets circulate and age in blood, they lose sialic ac

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19

Chen, Xi, Shuchi Gupta, Matthew Cooper, et al. "GRK6 Regulates the Hemostatic Response to Injury through Its Rate-Limiting Effects on GPCR Signaling in Platelets." Blood 134, Supplement_1 (2019): 3611. http://dx.doi.org/10.1182/blood-2019-129175.

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Inappropriate platelet activation remains a major cause of cardiovascular and cerebrovascular diseases. Most agonists activate platelets through G protein-coupled receptors (GPCRs). However, questions remain about mechanisms that provide negative feedback towards activated GPCRs to limit platelet activation and thrombus formation. Here we provide the first evidence that GPCR kinase 6 (GRK6) serves this role in platelets, using GRK6-/- mice generated by CRISPR-Cas9 genome editing to examine the consequences of GRK6 knockout on GPCR-dependent signaling. Hemostatic thrombi formed in GRK6-/- mice

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Kulkarni, Suhasini, Kevin J. Woollard, Stephen Thomas, David Oxley, and Shaun P. Jackson. "Conversion of platelets from a proaggregatory to a proinflammatory adhesive phenotype: role of PAF in spatially regulating neutrophil adhesion and spreading." Blood 110, no. 6 (2007): 1879–86. http://dx.doi.org/10.1182/blood-2006-08-040980.

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Abstract The ability of platelets to provide a highly reactive surface for the recruitment of other platelets and leukocytes to sites of vascular injury is critical for hemostasis, atherothrombosis, and a variety of inflammatory diseases. The mechanisms coordinating platelet-platelet and platelet-leukocyte interactions have been well defined and, in general, it is assumed that increased platelet activation correlates with enhanced reactivity toward other platelets and neutrophils. In the current study, we demonstrate a differential role for platelets in supporting platelet and neutrophil adhes

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Gonzalez Pagan, Omayra, Min Soon Cho, and Vahid Afshar-Kharghan. "Platelets Promote Activation of the Complement System in Ovarian Cancer." Blood 132, Supplement 1 (2018): 4970. http://dx.doi.org/10.1182/blood-2018-99-116752.

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Abstract Platelets promote metastasis and growth of ovarian cancer. We have shown that platelets extravasate into the tumor microenvironment (TME) and increase proliferation and epithelial-mesenchymal transition (EMT) in ovarian cancer cells. We have also shown that activation of the complement system in TME of ovarian cancer enhances tumor growth. Ovarian cancer cells secrete complement proteins that upon activation in the TME increase proliferation of cancer cells and promote EMT via an autocrine pathway. The activators of the complement system in the TME have not been identified. We have de

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Tang, Hao, Meng Gao, Yunfeng Fu, Rong Gui, and Xianjun Ma. "The Effect of Autophagic Activity on the Function of Apheresis Platelets and on the Efficacy of Clinical Platelet Transfusion." Transfusion Medicine and Hemotherapy 47, no. 4 (2020): 302–13. http://dx.doi.org/10.1159/000504764.

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Platelet activation and survival jointly determine the efficacy of clinical platelet transfusion. This study aimed to discuss the effect of autophagic activity on activation and aggregation of apheresis platelets and on the efficacy of clinical platelet transfusion. In this study, we investigated the effects of autophagic activity of apheresis platelets for different blood types and after different storage durations on platelet activation and aggregation functions. By Western blot, immunofluorescence, and RT-qPCR detection, we found that with the prolongation of the storage duration, the expre

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Kim, Oleg V., Tatiana A. Nevzorova, Elmira R. Mordakhanova, et al. "Fatal Dysfunction and Fragmentation of Thrombin-Stimulated Platelets." Blood 132, Supplement 1 (2018): 521. http://dx.doi.org/10.1182/blood-2018-99-112703.

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Abstract Introduction: Platelets play a key role in formation of protective hemostatic blood clots and pathological obstructive thrombi. Under (patho)physiological conditions, chemically activated platelets change their morphology, express adhesive molecules, undergo aggregation, secrete procoagulant substances, and induce mechanical contraction (retraction) of the blood clots. Despite the vital importance of these platelet functions, the subsequent fate of activated platelets is largely unknown. We hypothesize that activated platelets undergo late alterations that determine their fate and may

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Novakovic, Valerie Anne, Madhumouli Chatterjee, and Gary E. Gilbert. "Cryopreserved Platelets Retain Agonist Responsiveness and Support for Factor VIII Function." Blood 136, Supplement 1 (2020): 3–4. http://dx.doi.org/10.1182/blood-2020-143366.

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Platelet activation supports procoagulant activity through phosphatidylserine exposure, secretion of procoagulant factors, and receptor conformational change. For example, thrombin-stimulated platelets bind factor VIII (fVIII) via a macromolecular complex including oligomeric fibrin and the active αIIbβ3 receptor (Phillips et al, JTH 2004; Gilbert et al, Blood 2015). Thus, coagulation assays in which phospholipid vesicles are substituted for platelets do not fully emulate modulators of fVIII activity. Indeed, inhibition of platelet-supported fVIII activity by a panel of mAbs against the C2 dom

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Amer, Johnny, and Eitan Fibach. "Oxidative Status of Platelets in Normal and Thalassemic Blood." Blood 104, no. 11 (2004): 3765. http://dx.doi.org/10.1182/blood.v104.11.3765.3765.

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Abstract Thromboembolic complications, possibly involving chronic platelet activation, are an important cause of morbidity and mortality in beta-thalassemia. Oxidative stress, with the generation of reactive oxygen species (ROS), has been suspected to play a role in the pathophysiology of thalassemia and cardiovascular disorders. Previous investigations demonstrated that ROS profoundly affect platelet function and promote platelet activation. Other studies have shown that platelets themselves produce ROS upon activation. In the present study, we adapted flow cytometric techniques to measure ox

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Jobe, Shawn M., Lorie Leo, Joshua S. Eastvold та ін. "Role of FcRγ and factor XIIIA in coated platelet formation". Blood 106, № 13 (2005): 4146–51. http://dx.doi.org/10.1182/blood-2005-03-1223.

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Platelet activation in response to dual stimulation with collagen and thrombin results in the formation of a subpopulation of activated platelets known as coated platelets. Coated platelets are characterized by high surface levels of α-granule proteins and phosphatidylserine, which support the assembly of procoagulant protein complexes. Using murine models, we tested the hypothesis that the collagen receptor-associated molecule FcRγ and the transglutaminase factor XIIIA are required for the formation of coated platelets. Following dual stimulation with the collagen receptor agonist convulxin a

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Hansen, Caroline E., Yongzhi Qiu, Owen J. T. McCarty, and Wilbur A. Lam. "Platelet Mechanotransduction." Annual Review of Biomedical Engineering 20, no. 1 (2018): 253–75. http://dx.doi.org/10.1146/annurev-bioeng-062117-121215.

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The vasculature is a dynamic environment in which blood platelets constantly survey the endothelium for sites of vessel damage. The formation of a mechanically coherent hemostatic plug to prevent blood loss relies on a coordinated series of ligand–receptor interactions governing the recruitment, activation, and aggregation of platelets. The physical biology of each step is distinct in that the recruitment of platelets depends on the mechanosensing of the platelet receptor glycoprotein Ib for the adhesive protein von Willebrand factor, whereas platelet activation and aggregation are responsive

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Rinder, Henry M., Jayne L. Tracey, Christine S. Rinder, David Leitenberg, and Brian R. Smith. "Neutrophil but not Monocyte Activation Inhibits P-Selectin-Mediated Platelet Adhesion." Thrombosis and Haemostasis 72, no. 05 (1994): 750–56. http://dx.doi.org/10.1055/s-0038-1648953.

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SummarySelectins are Ca2+-dependent glycoprotein receptors that mediate the adhesion of activated platelets or endothelial cells to unstimulated leukocytes. Using purified cell fractions, we examined activated neutrophil adhesion to P-selectin-expressing platelets and found that phorbol 12-myristate 13-acetate (PMA), platelet activating factor C16 (PAF), and n-formyl-met-leu-phe (fMLP) pretreatment of neutrophils inhibited activated platelet adhesion. Furthermore, PMA and PAF were capable of dissociating established resting neutrophil-activated platelet conjugates. Since L-selectin is downregu

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Huynh, Angela, Donald M. Arnold, James W. Smith, et al. "Fluid-Phase Immune Complexes Can Assemble and Activate Platelets in Heparin-Induced Thrombocytopenia." Blood 132, Supplement 1 (2018): 3746. http://dx.doi.org/10.1182/blood-2018-99-115037.

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Abstract Introduction: Heparin-induced thrombocytopenia (HIT) is a complication of heparin therapy that is caused by antibodies to complexes of platelet factor 4 (PF4) and heparin. Several studies have reported that in order for these immune complexes to be pathogenic, they must assemble on the platelet surface. When bound to the platelet surface, the conformation of PF4 allows for optimal presentation of the epitope for antibody binding and subsequent activation of Fc-receptors on platelets and monocytes. To what degree pathogenic HIT immune complexes can form and activate platelets in fluid-

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Vogler, Meike, Hassan A. Hamali, Xiao-Ming Sun, et al. "BCL2/BCL-XL inhibition induces apoptosis, disrupts cellular calcium homeostasis, and prevents platelet activation." Blood 117, no. 26 (2011): 7145–54. http://dx.doi.org/10.1182/blood-2011-03-344812.

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Abstract Apoptosis in megakaryocytes results in the formation of platelets. The role of apoptotic pathways in platelet turnover and in the apoptotic-like changes seen after platelet activation is poorly understood. ABT-263 (Navitoclax), a specific inhibitor of antiapoptotic BCL2 proteins, which is currently being evaluated in clinical trials for the treatment of leukemia and other malignancies, induces a dose-limiting thrombocytopenia. In this study, the relationship between BCL2/BCL-XL inhibition, apoptosis, and platelet activation was investigated. Exposure to ABT-263 induced apoptosis but r

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Alugupalli, Kishore R., Alan D. Michelson, Isabelle Joris, et al. "Spirochete-platelet attachment and thrombocytopenia in murine relapsing fever borreliosis." Blood 102, no. 8 (2003): 2843–50. http://dx.doi.org/10.1182/blood-2003-02-0426.

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Abstract Thrombocytopenia is common in persons infected with relapsing fever Borreliae. We previously showed that the relapsing fever spirochete Borrelia hermsii binds to and activates human platelets in vitro and that, after platelet activation, high-level spirochete-platelet attachment is mediated by integrin αIIbβ3, a receptor that requires platelet activation for full function. Here we established that B hermsii infection of the mouse results in severe thrombocytopenia and a functional defect in hemostasis caused by accelerated platelet loss. Disseminated intravascular coagulation, immune

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Vyshynska, M. B. "Changes in the functional state of platelets in patients with polytrauma." EMERGENCY MEDICINE 17, no. 1 (2021): 27–32. http://dx.doi.org/10.22141/2224-0586.17.1.2021.225716.

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Background. Polytrauma remains the leading cause of global morbidity and mortality and is the cause of more than 10 % of deaths. The purpose of this research was to study the literature data about changes in vascular platelet hemostasis, to investigate the dynamics of the morphofunctional state of platelets, to analyze changes in intravascular platelet activation in patients with polytrauma. Results. Normal blood clotting requires at least 4 components — blood vessels, platelets, the ability of blood to coagulate and fibrinolysis. Determination of components such as indicators of intravascula

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Van de Walle, Gerlinde R., Anne Schoolmeester, Brecht F. Iserbyt та ін. "Activation of αIIbβ3 is a sufficient but also an imperative prerequisite for activation of α2β1 on platelets". Blood 109, № 2 (2006): 595–602. http://dx.doi.org/10.1182/blood-2005-11-011775.

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Abstract Platelet integrins α2β1 and αIIbβ3 play critical roles in platelet adhesion and thrombus formation after vascular injury. On resting platelets, both integrins are in a low-affinity state. However, agonist stimulation results in conformational changes that enable ligand binding that can be detected with conformation dependent monoclonal antibodies (mAbs). By using such conformation-dependent mAbs, we could demonstrate that activation of integrin αIIbβ3 is not only sufficient, but also a prerequisite for α2β1 activation. Compared with platelets in plasma, stimulation of washed platelets

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Hottz, Eugenio D., Isaclaudia G. Azevedo-Quintanilha, Lohanna Palhinha, et al. "Platelet activation and platelet-monocyte aggregate formation trigger tissue factor expression in patients with severe COVID-19." Blood 136, no. 11 (2020): 1330–41. http://dx.doi.org/10.1182/blood.2020007252.

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Abstract Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an emergent pathogen responsible for the coronavirus disease 2019 (COVID-19). Since its emergence, the novel coronavirus has rapidly achieved pandemic proportions causing remarkably increased morbidity and mortality around the world. A hypercoagulability state has been reported as a major pathologic event in COVID-19, and thromboembolic complications listed among life-threatening complications of the disease. Platelets are chief effector cells of hemostasis and pathological thrombosis. However, the participation of platel

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Boylan, Brian, Cunji Gao, Vipul Rathore, Joan C. Gill, Debra K. Newman та Peter J. Newman. "Identification of FcγRIIa as the ITAM-bearing receptor mediating αIIbβ3 outside-in integrin signaling in human platelets". Blood 112, № 7 (2008): 2780–86. http://dx.doi.org/10.1182/blood-2008-02-142125.

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AbstractImmunoreceptor tyrosine-based activation motif (ITAM)–containing proteins have recently been demonstrated in macrophages and neutrophils to be required for cell surface integrins to transmit activation signals into the cell. To identify ITAM-bearing proteins that mediate signaling via the platelet-specific integrin αIIbβ3, fibrinogen binding was induced by (1) allowing platelets to spread directly on immobilized fibrinogen, or (2) activating the PAR1 thrombin receptor on platelets in suspension. Both initiated strong, ligand binding–dependent tyrosine phosphorylation of the ITAM-bearin

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Shiva, Sruti. "The Mitochondrion: A Link Between Hemolysis and Platelet Activation." Blood 134, Supplement_1 (2019): SCI—39—SCI—39. http://dx.doi.org/10.1182/blood-2019-121112.

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Patients with Sickle Cell Disease (SCD) demonstrate characteristics of chronic hemostatic activation including elevated baseline platelet activation. While it is well established that platelet activation is positively correlated with the magnitude of erythrocytic hemolysis in these patients, the mechanisms linking hemolysis to platelet activation remain unclear. In this study, we investigate the role of the platelet mitochondrion as the molecular link between hemolysis and downstream platelet activation. Using extracellular flux analysis, we demonstrate that platelets isolated from patients wi

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Garcia, Analia, Todd M. Quinton, Robert T. Dorsam, and Satya P. Kunapuli. "Src family kinase–mediated and Erk-mediated thromboxane A2 generation are essential for VWF/GPIb-induced fibrinogen receptor activation in human platelets." Blood 106, no. 10 (2005): 3410–14. http://dx.doi.org/10.1182/blood-2005-05-1933.

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AbstractThe binding of von Willebrand factor (VWF) to the platelet membrane glycoprotein Ib-IX (GPIb-IX) results in platelet activation. In this study, we sought to clarify previous conflicting reports and to elucidate the mechanism of activation and the precise role of extracellular signal-regulated kinase (Erk) in VWF-induced platelet activation. Erk2 is activated in platelets on stimulation with VWF/ristocetin in a time-dependent manner. VWF-induced Erk2 phosphorylation and thromboxane A2 (TXA2) release were completely blocked by PP2, an Src family kinase inhibitor, suggesting that Erk is d

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38

Welles, E. G., C. Bourne, J. W. Tyler, and M. K. Boudreaux. "Detection of Activated Feline Platelets in Platelet-rich Plasma by Use of Fluorescein-labeled Antibodies and Flow Cytometry." Veterinary Pathology 31, no. 5 (1994): 553–60. http://dx.doi.org/10.1177/030098589403100507.

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Platelets contribute to prethrombotic or thrombotic states; however, accepted evaluation methods (i.e., in vitro testing by use of an aggregometer) of platelet function in cats can be difficult because of the large volume of blood required from which platelets are isolated and the potential for platelet activation due to difficult venipunctures in sometimes uncooperative or excited animals. The activation problem also contributes to errors in platelet counts. Platelets from four domestic short haired cats (two males, two females, 2–3 years old) minimally restrained without sedation or anesthes

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Essex, David W., Mengru Li, Richard D. Feinman, and Anna Miller. "Platelet surface glutathione reductase-like activity." Blood 104, no. 5 (2004): 1383–85. http://dx.doi.org/10.1182/blood-2004-03-1097.

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Abstract We previously found that reduced glutathione (GSH) or a mixture of GSH/glutathione disulfide (GSSG) potentiated platelet aggregation. We here report that GSSG, when added to platelets alone, also potentiates platelet aggregation. Most of the GSSG was converted to GSH by a flavoprotein-dependent platelet surface mechanism. This provided an appropriate redox potential for platelet activation. The addition of GSSG to platelets generated sulfhydryls in the β subunit of the αIIbβ3 fibrinogen receptor, suggesting a mechanism for facilitation of agonist-induced platelet activation.

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Jian-ning, Zhang, Angela Bergeron, Qinghua Yu, et al. "Duration of exposure to high fluid shear stress is critical in shear-induced platelet activation-aggregation." Thrombosis and Haemostasis 90, no. 10 (2003): 672–78. http://dx.doi.org/10.1160/th03-03-0145.

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SummaryPlatelet functions are increasingly measured under flow conditions to account for blood hydrodynamic effects. Typically, these studies involve exposing platelets to high shear stress for periods significantly longer than would occur in vivo. In the current study, we demonstrate that the platelet response to high shear depends on the duration of shear exposure. In response to a 100 dyn/cm2 shear stress for periods less than 10-20 sec, platelets in PRP or washed platelets were aggregated, but minimally activated as demonstrated by P-selectin expression and binding of the activation-depend

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Stoller, Michelle L., Indranil Basak, James Alsobrooks, Paul F. Bray, and Robert A. Campbell. "Cathepsin G Cleavage of PAR4 Generates a Novel Tethered Ligand That Induces Platelet Activation." Blood 136, Supplement 1 (2020): 2. http://dx.doi.org/10.1182/blood-2020-134931.

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Atherosclerotic vessel injury induces recruitment of both platelets and neutrophils where multiple proteases induce platelet activation and aggregation. Platelets contain two protease activated receptors, PAR1 and PAR4, the cleavage of which results in exposure of a new amino terminus to serve as a tethered ligand. Released neutrophil cathepsin G (CatG) has been shown to be a physiologic modulator of platelet thrombus formation in mice. CatG activates PAR4 and not PAR1, presumably because CatG cleaves PAR1 by removing its tethered ligand. However, neither the CatG biochemical cleavage of PAR4

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42

Begonja, Antonija Jurak, Jörg Geiger, Natalia Rukoyatkina, Steffen Rauchfuss, Stepan Gambaryan, and Ulrich Walter. "Thrombin stimulation of p38 MAP kinase in human platelets is mediated by ADP and thromboxane A2 and inhibited by cGMP/cGMP-dependent protein kinase." Blood 109, no. 2 (2006): 616–18. http://dx.doi.org/10.1182/blood-2006-07-038158.

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Abstract p38 MAP kinase in human platelets is activated by platelet agonists including thrombin, thromboxane A2 (TxA2), ADP, and others. However, both upstream mechanisms of p38 MAP kinase activation, and their downstream sequelae, are presently controversial and essentially unclear. Certain studies report sequential activation of cGMP-dependent protein kinase (PKG) and p38/ERK pathways by platelet agonists, leading to integrin activation and secretion, whereas others establish an essential role of Src/ERK-mediated TxA2 generation for fibrinogen receptor activation in human platelets. Here, we

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Weng, Zhen, Ding Li, Lin Zhang, et al. "PTEN Regulates Collagen-Induced Platelet Activation." Blood 116, no. 21 (2010): 5126. http://dx.doi.org/10.1182/blood.v116.21.5126.5126.

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Abstract Abstract 5126 PI3K has been shown to play an important role in collagen-induced platelet activation, but the role(s) of PTEN, a major regulator of the PI3K/Akt signaling pathway, has not been examined in platelets. Here, we report that PTEN−/− mouse blood contains 25% more platelets than PTEN+/+ blood, and that PTEN deficiency significantly shortened the bleeding time, increased the sensitivity of platelets to collagen-induced activation and aggregation, and enhanced phosphorylation of Akt at Ser473 in response to collagen. Furthermore, we found that PP2, and the combination of apyras

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Maroney, Susan A., Sandra L. Haberichter, Paul Friese, et al. "Active tissue factor pathway inhibitor is expressed on the surface of coated platelets." Blood 109, no. 5 (2006): 1931–37. http://dx.doi.org/10.1182/blood-2006-07-037283.

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Abstract The incorporation of blood-borne forms of tissue factor (TF) into a growing blood clot is necessary for normal fibrin generation and stabilization of the blood clot. Tissue factor pathway inhibitor (TFPI) is the primary physiologic inhibitor of tissue factor and is present within platelets. Expression of TFPI on the platelet surface may be the optimal location for it to abrogate blood-borne TF activity that incorporates within the blood clot, balancing the need for adequate hemostasis while preventing development of occlusive thrombosis. TFPI is produced by megakaryocytes but is not e

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Stephens, Gillian, Yibing Yan, Martine Jandrot-Perrus, Jean-Luc Villeval, Kenneth J. Clemetson, and David R. Phillips. "Platelet activation induces metalloproteinase-dependent GP VI cleavage to down-regulate platelet reactivity to collagen." Blood 105, no. 1 (2005): 186–91. http://dx.doi.org/10.1182/blood-2004-07-2842.

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Abstract Glycoprotein (GP) VI, the primary collagen receptor on platelets, has been shown to have variable expression, possibly as a consequence of immune modulation. The present study was designed to determine the mechanism by which GP VI clearance occurs. We found that direct activation of GP VI both by a GP VI–specific antibody and by GP VI ligands (collagen and convulxin) reduced binding of biotinylated convulxin to the stimulated platelets. Analysis of immunoblots of platelets and supernatants showed that the stimulated platelets contained less GP VI, while the soluble fraction contained

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Maher, Kristin N., Xu Han, Keith B. Neeves, Marvin T. Nieman, and Jorge Di Paola. "Modulation of Thrombin-Induced Platelet Activation By Defibrotide." Blood 134, Supplement_1 (2019): 3614. http://dx.doi.org/10.1182/blood-2019-125945.

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Defibrotide is a mixture of single-stranded phosphodiester oligonucleotides 9-80 bases in length derived from mammalian tissue and it is the only medication that is FDA approved for the prevention and treatment of post-transplant veno-occlusive disease, also known as sinusoidal obstructive syndrome (VOD/SOS). The mechanism of action of defibrotide is not well understood. A better understanding of the molecular mechanism by which defibrotide prevents and reverses the microvascular occlusion seen in VOD/SOS will be critical in the development of novel therapeutics for VOD/SOS and other related d

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47

Pleines, Irina, Anita Eckly, Margitta Elvers, et al. "Multiple alterations of platelet functions dominated by increased secretion in mice lacking Cdc42 in platelets." Blood 115, no. 16 (2010): 3364–73. http://dx.doi.org/10.1182/blood-2009-09-242271.

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Abstract Platelet activation at sites of vascular injury is crucial for hemostasis, but it may also cause myocardial infarction or stroke. Cytoskeletal reorganization is essential for platelet activation and secretion. The small GTPase Cdc42 has been implicated as an important mediator of filopodia formation and exocytosis in various cell types, but its exact function in platelets is not established. Here, we show that the megakaryocyte/platelet-specific loss of Cdc42 leads to mild thrombocytopenia and a small increase in platelet size in mice. Unexpectedly, Cdc42-deficient platelets were able

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48

Revollo, Leila, Glenn Merrill-Skoloff, Karen De Ceunynck, et al. "The Secreted Tyrosine Kinase Vlk Is Essential for Normal Platelet Activation and Thrombus Formation." Blood 136, Supplement 1 (2020): 10–11. http://dx.doi.org/10.1182/blood-2020-137243.

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Tyrosine phosphorylation of proteins secreted into the extracellular space has been observed in cell cultures and in vivo, yet little is known about the role that phosphorylation of extracellular proteins serves in modulating cell function. An important reason for the gap in our knowledge of the functional significance of extracellular protein phosphorylation has been the delay in identifying extracellular kinases. Within the last decade, however, bioinformatic strategies to identify kinases with signal peptides, coupled with biochemical approaches to characterize kinases in the secretory path

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49

Zobel, Joachim, Tanja Strini, Martin Tischitz, et al. "Bile Acids Induce Platelet Activation Leading to Degranulation and a Prothrombotic Phenotype." Blood 134, Supplement_1 (2019): 4887. http://dx.doi.org/10.1182/blood-2019-126095.

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Background: Previous articles have identified the farnesoid X receptor (FXR) as an integral part in the formation of coated platelets. Coated platelets are preactivated platelets featuring degranulation, increased fibrinogen binding, and increased serine protease activity leading to fibrin generation. Furthermore, phosphatidylserine exposure is increased and integrin α2bβIII is inhibited - leading to a prothrombotic phenotype despite decreased platelet aggregation. We hypothesize that bile acids, as natural ligands of FXR, lead to a change of platelet phenotype and therefore play a pivotal rol

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50

Coxon, Carmen H., Mitchell J. Geer, and Yotis A. Senis. "ITIM receptors: more than just inhibitors of platelet activation." Blood 129, no. 26 (2017): 3407–18. http://dx.doi.org/10.1182/blood-2016-12-720185.

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Abstract Since their discovery, immunoreceptor tyrosine-based inhibition motif (ITIM)-containing receptors have been shown to inhibit signaling from immunoreceptor tyrosine-based activation motif (ITAM)-containing receptors in almost all hematopoietic cells, including platelets. However, a growing body of evidence has emerged demonstrating that this is an oversimplification, and that ITIM-containing receptors are versatile regulators of platelet signal transduction, with functions beyond inhibiting ITAM-mediated platelet activation. PECAM-1 was the first ITIM-containing receptor identified in

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