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Journal articles on the topic 'Blood platelets – Activation'

Author: Grafiati

Published: 4 June 2021

Last updated: 5 February 2022

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1

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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2

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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3

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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4

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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5

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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6

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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7

Dasgupta, Swapan Kumar, and Perumal Thiagarajan. "Cofilin-1 Activation in Stored Platelets." Blood 132, Supplement 1 (2018): 1256. http://dx.doi.org/10.1182/blood-2018-99-119159.

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Abstract Background Platelets, harvested for transfusion, have a relatively short "shelf life" of 5 days. With increasing storage, platelets develop structural and functional changes called "platelet storage lesions". These changes result not only in reduced hemostatic response to agonists but also in an accelerated clearance from the circulation in vivo. The precise mechanisms of clearance of platelets aged in vitro (or vivo) are not known. There is an increased exposure of the anionic phospholipid phosphatidylserine (PS) on the cell surface of stored platelets. PS is a well-known tag for cle

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8

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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9

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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10

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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11

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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12

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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13

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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14

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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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

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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17

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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18

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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19

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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20

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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21

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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22

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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23

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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24

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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25

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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26

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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27

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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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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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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Ståhl, Anne-lie, Fariba Vaziri-Sani, Stefan Heinen, et al. "Factor H dysfunction in patients with atypical hemolytic uremic syndrome contributes to complement deposition on platelets and their activation." Blood 111, no. 11 (2008): 5307–15. http://dx.doi.org/10.1182/blood-2007-08-106153.

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AbstractAtypical hemolytic uremic syndrome (aHUS) may be associated with mutations in the C-terminal of factor H (FH). FH binds to platelets via the C-terminal as previously shown using a construct consisting of short consensus repeats (SCRs) 15 to 20. A total of 4 FH mutations, in SCR15 (C870R) and SCR20 (V1168E, E1198K, and E1198Stop) in patients with aHUS, were studied regarding their ability to allow complement activation on platelet surfaces. Purified FH-E1198Stop mutant exhibited reduced binding to normal washed platelets compared with normal FH, detected by flow cytometry. Washed platel

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31

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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32

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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33

Melki, Imene, Isabelle Allaeys, Nicolas Tessandier та ін. "FcγRIIA expression accelerates nephritis and increases platelet activation in systemic lupus erythematosus". Blood 136, № 25 (2020): 2933–45. http://dx.doi.org/10.1182/blood.2020004974.

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Abstract Systemic lupus erythematosus (SLE) is an autoimmune inflammatory disease characterized by deposits of immune complexes (ICs) in organs and tissues. The expression of FcγRIIA by human platelets, which is their unique receptor for immunoglobulin G antibodies, positions them to ideally respond to circulating ICs. Whereas chronic platelet activation and thrombosis are well-recognized features of human SLE, the exact mechanisms underlying platelet activation in SLE remain unknown. Here, we evaluated the involvement of FcγRIIA in the course of SLE and platelet activation. In patients with S

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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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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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Chen, Xi, Shuchi Gupta, Matthew Cooper, Daniel Dehelian, Lawrence F. Brass, and Peisong Ma. "Decoding Gq Signaling in Platelets." Blood 132, Supplement 1 (2018): 866. http://dx.doi.org/10.1182/blood-2018-99-111385.

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Abstract Most platelet agonists work through G protein coupled receptors (GPCRs), activating pathways that involve members of the Gq, Gi, and G12 families of heterotrimeric G proteins. Gq is critical for most functional responses during platelet activation. A defect in Gq expression in patients leads to impaired platelet secretion and aggregation, which is associated with bleeding diathesis. We have previously shown that the Regulators of G protein Signaling (RGS) proteins function as negative regulators for platelet activation by limiting G protein-dependent signaling, but much remains to be

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Kato, Hisashi, Nobuko Nishiura, Keigo Akuta та ін. "Platelet Integrin αIIbβ3 Activation Kinetics in Inherited Platelet Functional Disorders ∼ the Role of ADP Receptor P2Y12, Caldag-GEFI and Kindlin-3 αIIbβ3 Activation By inside-out Signaling". Blood 132, Supplement 1 (2018): 1136. http://dx.doi.org/10.1182/blood-2018-99-112852.

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Abstract Background and objectives Activation of platelet fibrinogen receptor integrin αIIbβ3 (GPIIb-IIIa) by inside-out signaling is essential for platelet aggregate formation. In αIIbβ3 activation, it has been established that CalDAG-GEFI-induced Rap1 activation is necessary to induce the direct interaction of β3 cytoplasmic tail with talin and kindlin-3. Agonist induced platelet and αIIbβ3 activation are generally assessed using platelet aggregation assay and flow cytometric analysis of monoclonal antibody specific for activated αIIbβ3, PAC-1, binding. However, we found that the results of

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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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Manne, Bhanu Kanth, Frederik Denorme, Elizabeth A. Middleton, et al. "Platelet gene expression and function in patients with COVID-19." Blood 136, no. 11 (2020): 1317–29. http://dx.doi.org/10.1182/blood.2020007214.

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Abstract There is an urgent need to understand the pathogenesis of coronavirus disease 2019 (COVID-19). In particular, thrombotic complications in patients with COVID-19 are common and contribute to organ failure and mortality. Patients with severe COVID-19 present with hemostatic abnormalities that mimic disseminated intravascular coagulopathy associated with sepsis, with the major difference being increased risk of thrombosis rather than bleeding. However, whether severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection alters platelet function to contribute to the pathophysiol

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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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Lian, Lurong, Yanfeng Wang, Julia Draznin та ін. "The relative role of PLCβ and PI3Kγ in platelet activation". Blood 106, № 1 (2005): 110–17. http://dx.doi.org/10.1182/blood-2004-05-2005.

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Stimulation of platelet G protein–coupled receptors results in the cleavage of phosphatidylinositol 4,5-trisphosphate (PIP2) into inositol 1,4,5-trisphosphate and 1,2-diacylglycerol by phospholipase C (PLCβ). It also results in the phosphorylation of PIP2 by the γ isoform of phosphatidylinositol 3-kinase (PI3Kγ) to synthesize phosphatidylinositol 3,4,5-trisphosphate. To understand the role of PIP2 in platelet signaling, we evaluated knock-out mice lacking 2 isoforms of PLCβ (PLCβ2 and PLCβ3) or lacking the Gβγ-activated isoform of PI3K (PI3Kγ). Both knock-out mice were unable to form stable th

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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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Tao, Derrick L., Samuel Tassi Yunga, Craig D. Williams, and Owen J. T. McCarty. "Aspirin and antiplatelet treatments in cancer." Blood 137, no. 23 (2021): 3201–11. http://dx.doi.org/10.1182/blood.2019003977.

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Abstract Platelets have been hypothesized to promote certain neoplastic malignancies; however, antiplatelet drugs are still not part of routine pharmacological cancer prevention and treatment protocols. Paracrine interactions between platelets and cancer cells have been implicated in potentiating the dissemination, survival within the circulation, and extravasation of cancer cells at distant sites of metastasis. Signals from platelets have also been suggested to confer epigenetic alterations, including upregulating oncoproteins in circulating tumor cells, and secretion of potent growth factors

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Moraes, Leonardo A., Mark J. Paul-Clark, Alice Rickman, Roderick J. Flower, Nicolas J. Goulding, and Mauro Perretti. "Ligand-specific glucocorticoid receptor activation in human platelets." Blood 106, no. 13 (2005): 4167–75. http://dx.doi.org/10.1182/blood-2005-04-1723.

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Few studies have addressed the effects of classical anti-inflammatory glucocorticoids on platelet function. Here, we report for the first time that human platelets contain the glucocorticoid receptor (GR) as identified by a combination of biochemical and functional techniques. Ligand-binding studies revealed the presence of a high- and low-affinity binding site for [3H]-dexamethasone in platelets. The 2 GR ligands prednisolone and dexamethasone competed for [3H]-dexamethasone binding, as did the mineralocorticoid aldosterone. However, while prednisolone (1-10 μM) reduced adenosine diphosphate

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Raslan, Zaher, and Khalid M. Naseem. "The control of blood platelets by cAMP signalling." Biochemical Society Transactions 42, no. 2 (2014): 289–94. http://dx.doi.org/10.1042/bst20130278.

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Blood platelet activation must be tightly regulated to ensure a balance between haemostasis and thrombosis. The cAMP signalling pathway is the most powerful endogenous regulator of blood platelet activation. PKA (protein kinase A), the foremost effector of cAMP signalling in platelets, phosphorylates a number of proteins that are thought to modulate multiple aspects of platelet activation. In the present mini-review, we outline our current understanding of cAMP-mediated platelet inhibition and discuss some of the issues that require clarification.

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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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Saluk-Bijak, Joanna, Angela Dziedzic, and Michal Bijak. "Pro-Thrombotic Activity of Blood Platelets in Multiple Sclerosis." Cells 8, no. 2 (2019): 110. http://dx.doi.org/10.3390/cells8020110.

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The available data, including experimental studies, clearly indicate an excessive intravascular activation of circulating platelets in multiple sclerosis (MS) and their hyper-responsiveness to a variety of physiological activators. Platelet activation is manifested as an increased adhesion and aggregation and is accompanied by the formation of pro-thrombotic microparticles. Activated blood platelets also show an expression of specific membrane receptors, synthesis many of biomediators, and generation of reactive oxygen species. Epidemiological studies confirm the high risk of stroke or myocard

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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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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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Flevaris, Panagiotis, Zhenyu Li, Guoying Zhang, Yi Zheng, Junling Liu, and Xiaoping Du. "Two distinct roles of mitogen-activated protein kinases in platelets and a novel Rac1-MAPK–dependent integrin outside-in retractile signaling pathway." Blood 113, no. 4 (2009): 893–901. http://dx.doi.org/10.1182/blood-2008-05-155978.

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Abstract Mitogen-activated protein kinases (MAPK), p38, and extracellular stimuli-responsive kinase (ERK), are acutely but transiently activated in platelets by platelet agonists, and the agonist-induced platelet MAPK activation is inhibited by ligand binding to the integrin αIIbβ3. Here we show that, although the activation of MAPK, as indicated by MAPK phosphorylation, is initially inhibited after ligand binding to integrin αIIbβ3, integrin outside-insignaling results in a late but sustained activation of MAPKs in platelets. Furthermore, we show that the early agonist-induced MAPK activation

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