Effects Of Hemostatic Agents On Platelet Aggregation

1981 ◽  
Author(s):  
P N Sawyer ◽  
G Schwann ◽  
B Stanczewski ◽  
M T Jones
Keyword(s):  
Platelet Aggregation ◽  
Blood Clotting ◽  
Thrombus Formation ◽  
Coagulation System ◽  
Thrombin Time ◽  
Hemostatic Agents ◽  
Adp Release ◽  
Enzymatic Mechanisms ◽  
Derived Data ◽  
Primary Platelet

Several new collagen derived hemostatic agents have been introduced into the surgical armamentarium. The presumption is they produce platelet aggregation, ADP release and blood clotting through the intrinsic system.Studies of interreaction of these new hemostatic agents with both blood and platelets suggests that the type of reaction with whole blood is not known or due to primary platelet activation. Avitene interreacts in part by platelet aggregation but also by interreacting with other components in blood including fibrinogen.The available evidence with a new dissolving collagenous hemostat, “Superstat”™ indicates probable activation of the extrinsic coagulation system, directly converting prothrombin to thrombin, and fibrinogen to fibrin. Thrombin time ratios (experimental vs. control) are Superstat 1% - 0.81 ± 0.16/0.93 ± 0.06, Superstat 2% - 0.84 ± 0.11/0.93 ± 0.06, Superstat 3% - 0.61 ± 0.15/0.71 ± 0.02. Comparative studies have been completed on several other agents, among them, Kollagen Haemo. Vlies - 0.66 ± 0.1/0.71 ± 0.02, Gelfoam - 0.75 ± 0.15/0.71 ± 0.02, Surgicel - 0.73 ± 0.4/ 0.71 ± 0.02, Avitene - 0.75 ± 0.3/0.71 ± 0.02, Collatamp - 0.73 ± 0.4/0.71 ± 0.02. Derived data from thrombin times, clotting times and, when possible, platelet aggregation displays widely different rates of thrombus formation. We believe the enzymatic mechanisms for these reactions are currently only partially known.The fact that clinically useful hemostatic agents each appear to produce hemostasis by several routes, and do not all use the same route, is of extreme interest in basic thrombosis studies as well as in clinical surgery.

scholarly journals Biomechanical thrombosis: the dark side of force and dawn of mechano-medicine

2019 ◽  
Vol 5 (2) ◽  
pp. 185-197 ◽  
Author(s):  
Yunfeng Chen ◽  
Lining Arnold Ju
Keyword(s):  
Platelet Aggregation ◽  
Blood Clotting ◽  
Thrombus Formation ◽  
Dark Side ◽  
Atherosclerotic Plaques ◽  
Excessive Bleeding ◽  
Glycoprotein Vi ◽  
Device Implantation ◽  
Platelet Binding ◽  
Platelet Thrombus

Arterial thrombosis is in part contributed by excessive platelet aggregation, which can lead to blood clotting and subsequent heart attack and stroke. Platelets are sensitive to the haemodynamic environment. Rapid haemodynamcis and disturbed blood flow, which occur in vessels with growing thrombi and atherosclerotic plaques or is caused by medical device implantation and intervention, promotes platelet aggregation and thrombus formation. In such situations, conventional antiplatelet drugs often have suboptimal efficacy and a serious side effect of excessive bleeding. Investigating the mechanisms of platelet biomechanical activation provides insights distinct from the classic views of agonist-stimulated platelet thrombus formation. In this work, we review the recent discoveries underlying haemodynamic force-reinforced platelet binding and mechanosensing primarily mediated by three platelet receptors: glycoprotein Ib (GPIb), glycoprotein IIb/IIIa (GPIIb/IIIa) and glycoprotein VI (GPVI), and their implications for development of antithrombotic ‘mechano-medicine’ .

A Locally Administered Novel Heparin Complex Attenuates Collagen-Induced Platelet Activation and Thrombosis In Vivo,

Blood ◽  
2011 ◽  
Vol 118 (21) ◽  
pp. 3361-3361
Author(s):  
Riitta Lassila ◽  
Annukka Jouppila ◽  
Ulla M Marzec ◽  
Stephen R Hanson
Keyword(s):  
Blood Flow ◽  
Platelet Aggregation ◽  
Thrombus Formation ◽  
Ptfe Graft ◽  
Thrombin Time ◽  
Thrombosis Model ◽  
Baboon Model ◽  
Induced Aggregation

Abstract Abstract 3361 We have developed a semi-synthetic antithrombotic heparin complex, APL001, to mimic mast cell-derived natural heparin proteoglycans (HepPG). HepPG attenuate platelet-collagen interactions under blood flow by inhibiting VWF- and GPIIb/IIIa -mediated platelet aggregation. In addition, rat-derived HepPG arrest platelet thrombus growth on collagen surfaces or at vascular injury sites, both in vitro and in vivo (Lassila et al.ATVB 1997, Kauhanen et al. ATVB 2000, Olsson et al. Thromb Haemost 2002). Our objective was to study the inhibitory capacity of APL001 for preventing human platelet aggregation in vitro and acute thrombosis in a baboon model in vivo. The effects of unfractionated heparin (UFH) and APL001 were compared in relevant coagulation assays (APTT, PT, thrombin time, anti-FXa activity, fibrinogen, FVIII:C and VWF activity (VWF:RCo) and antigen). Additionally, agonist-induced (collagen, ristocetin and ADP) platelet aggregation in citrate or hirudin-anticoagulated whole blood (Multiplate®) (n=10 healthy subjects), and platelet function analysis (PFA100®) in citrated platelet rich plasma (PRP) were assessed. In a well-established baboon thrombosis model a collagen-coated PTFE graft (length 2 cm, lumen 4 mm) was placed in an arterio-venous shunt. Prior to blood contact the thrombogenic surface was treated for 10 min with UFH or APL001 (both at 4 mg/mL). Thrombus formation was initiated by exposing the surface to blood flow (100 mL/min, shear rate 265−1), and the deposition of 111-In-labeled platelets and of fibrin was quantified continuously over 1h. Fibrin thrombus accumulation was assessed from the incorporation of circulating 125-I-fibrinogen. In the heparin-relevant coagulation tests APL001 was comparable or 20–30% more potent than UFH while FVIII, fibrinogen and VWF variables remained unaltered. In contrast to UFH, APL001 (300 μg/mL) consistently inhibited collagen- and ristocetin-induced platelet aggregation, whereas UFH had only a modest effect in comparison with PBS control (Table). ADP-induced aggregation was unaffected. Comparable results were observed in the PRP aggregation assay. PFA100 testing also demonstrated inhibitory effects. In the in vivo thrombosis model (n=4) APL001 reduced platelet deposition on collagen (vs. the results with UFH) by 34% (p=0.01), while platelet accumulation in distal propagated thrombus was reduced by 61% (p=0.16). APL001-treated surfaces accumulated 45% less fibrin than the UFH-treated surfaces (p=0.008). In conclusion, when compared with UFH APL001 inhibited both collagen- and ristocetin-induced platelet aggregation in human blood, while anticoagulant properties were comparable. In the absence of systemic antithrombotic drugs, exposure of APL001 to a highly thrombogenic collagen surface arrested thrombus formation in an in vivo baboon model. This finding suggests that locally administered APL001 alone, due to its dual antiplatelet and anticoagulant effects, may limit the growth and size of thrombus and thereby prevent subsequent thrombo-occlusion.TableAnticoagulantInhibition-% of platelet aggregation ± SDConc. 300 μg/mLnColl (3.2 μg/mL)Ristocetin (0.77 mg/mL)ADP (6.4 μM)CitrateAPL0011033 ± 1543 ± 166 ± 24UFH1011 ± 1323 ± 153 ± 7p value0.0030.0100.700HirudinAPL0011032 ± 1043 ± 178 ± 10UFH108 ± 1116 ± 166 ± 9p value0.0000.0020.600 Disclosures: Lassila: Aplagon: Chief Scientific Advisor.

scholarly journals The effects of fructose diphosphate on routine coagulation tests in vitro

2022 ◽  
Vol 12 (1) ◽  
Author(s):  
Tongqing Chen ◽  
Duan Chen ◽  
Lu Chen ◽  
Zhengxu Chen ◽  
Baolong Wang ◽  
...  
Keyword(s):  
Platelet Aggregation ◽  
Blood Coagulation ◽  
Detection System ◽  
Coagulation System ◽  
Thrombin Time ◽  
Aggregation Rate ◽  
Coagulation Testing ◽  
Coagulation Tests ◽  
Routine Coagulation

AbstractTo evaluate the effects of fructose diphosphate (FDP) on routine coagulation tests in vitro, we added FDP into the mixed normal plasma to obtain the final concentration of 0, 1, 2, 3, 4, 5, 6, 10, 15, 20, 25, 30 and 35 mg/mL of drug. Prothrombin time (PT), activated partial thromboplastin time (aPTT), fibrinogen (FBG) and thrombin time (TT) of samples were analyzed with blood coagulation analyzers from four different manufacturers(Sysmex, Stago, SEKISUI and Werfen) and their corresponding reagents, respectively. Before the experiment, we also observed whether there were significant differences in coagulation test results of different lots of reagents produced by each manufacturer. At the same time as the four routine clotting tests, the Sysmex blood coagulation analyzer and its proprietary analysis software were used to detect the change of maximum platelet aggregation rate in platelet-rich plasma after adding FDP (0, 1, 2, 3, 4, 5 and 6 mg/mL). The results of PT, aPTT and TT showed a FDP (0–35 mg/mL) concentration-dependent increase and a FBG concentration-dependent decrease. The degree of change (increase or decrease) varied depending on the assay system, with PT and aPTT being more affected by the Sysmex blood coagulation testing instrument reagent system and less affected by CEKISUI, TT less affected by CEKISUI and more affected by Stago, and FBG less affected by Stago and more affected by Sysmex. The results of PT, aPTT and TT were statistically positively correlated with their FDP concentrations, while FBG was negatively correlated. The correlation coefficients between FDP and the coagulation testing systems of Sysmex, Stago, Werfen and SEKISUI were 0.975, 0.988, 0.967, 0.986 for PT, and 0.993, 0.989, 0.990 and 0.962 for aPTT, 0.994, 0.960, 0.977 and 0.982 for TT, − 0.990, − 0.983, − 0.989 and − 0.954 for FBG, respectively. Different concentrations of FDP (0, 1, 2, 3, 4, 5 and 6 mg/mL) had different effects on the maximum aggregation rate of platelet induced by the agonists of adenosine diphosphate (ADP, 5 µmol/L), arachidonic acid (Ara, 1 mmol/L), collagen (Col, 2.5 µg/mL) and epinephrine (Epi,10 µmol/L), but the overall downward trend was consistent, that is, with the increase of FDP concentration, the platelet aggregation rate decreased significantly. Our experimental study demonstrated a possible effect of FDP on the assays of coagulation and Platelet aggregation, which may arise because the drug interferes with the coagulation and platelet aggregation detection system, or it may affect our in vivo coagulation system and Platelet aggregation function, the real mechanism of which remains to be further verified and studied.

Effect of Shear Rate on Thrombus Growth

2010 ◽  
Author(s):  
Elham Tolouei ◽  
Andreas Fouras ◽  
Josie Carberry
Keyword(s):  
Platelet Aggregation ◽  
Shear Rate ◽  
Blood Clotting ◽  
Thrombus Formation ◽  
Measurement Techniques ◽  
Clotting Factors ◽  
Critical Height ◽  
Local Shear ◽  
Blood Clotting Factors

In this study micro and nano scale measurement techniques are applied to platelet studies and determination of factors in platelet aggregation and thrombus formation. Conventionally it has been assumed that platelets are stimulated by blood clotting factors and platelet activators to aggregate and form a thrombus at sites of vascular injury. We have recently shown that a primary factor in initiating platelet aggregation is hemodynamic shear. This paper presents the effect of shear rate on the time evolution of thrombus formation and the final geometry of a mature thrombus. A relationship between maximum mature thrombus height and local shear rate is formulated. We have shown that the shear rate is not only an important factor in initiating platelet aggregation but is also one of the main inhibitors of platelet aggregation and thrombus formation. We propose that when the platelets reach a critical height, they encounter a specific local hemodynamic range, which prevents further thrombus growth.

scholarly journals Comparative analysis of hemostasis system state indicators in severe COVID-19

2022 ◽  
Vol 20 (4) ◽  
pp. 87-94
Author(s):  
I. A. Tikhomirova ◽  
M. M. Ryabov
Keyword(s):  
Platelet Aggregation ◽  
Whole Blood ◽  
Fibrinolytic Activity ◽  
Blood Clotting ◽  
Platelet Reactivity ◽  
Thrombus Formation ◽  
Venous Blood ◽  
Clot Lysis ◽  
Hemostasis System ◽  
D Dimer

Introduction. Clinical experience in managing patients with a new coronavirus infection caused by the SARS-CoV-2 allowed to identify specific hemostasis disorders, and enables to introduce the concept of COVID-associated coagulopathy. The aim of the study was to assess the direction of coagulogram parameter changes, whole blood clotting parameters and characteristics of platelet and plasma hemostasis in patients with severe COVID-19. Materials and methods. The parameters of the hemostasis system were assessed using venous blood of 12 patients with severe COVID-19 and 16 healthy volunteers. The whole blood clotting process was investigated by low-frequency piezothromboelastography. The platelet count and indicators of spontaneous and ADP-induced platelet aggregation were estimated with the help of a laser platelet aggregation analyzer. Fibrinolytic activity of plasma, plasminogen activity, content of fibrinogen, D-dimer, PTT, APTT, PTI and INR were assessed. Results. An increased level of fibrinogen, a 6-fold increased D-dimer level, and increased PTT were found in patients with severe COVID-19. The patient platelets count was reduced by 51 % (p <0.05), spontaneous platelet aggregation remained at nearly normal level. Almost complete inhibition of ADP-induced platelet reactivity and inhibition of XIIa-dependent fibrinolysis was revealed, despite an increased by 19.3 % (p <0.05) plasminogen activity. Parameters of the whole blood coagulation process pointed a pronounced activation of platelet hemostasis, a significant intensification of the polymerization stage of clot formation and an increased intensity of clot lysis and retraction. Conclusion. The significant increase of D-dimer level and paradoxical inhibition of plasma fibrinolytic activity revealed by test of XIIa-dependent fibrinolysis (in contrast to the increased intensity of clot lysis when assessing the coagulation of whole blood) indicate the complex pathogenic mechanisms of coagulopathy caused by SARS-CoV-2 infection, and the involvement of blood cells and the vascular wall in the process of pathological thrombus formation.

Abstract 605: Activation of NLRP3 Inflammasome Complex Regulates the Onset of Hypoxia Induced Thrombosis

2015 ◽  
Vol 35 (suppl_1) ◽  
Author(s):  
Neha Gupta ◽  
Manish Sharma ◽  
Tathagata Chatterjee ◽  
Tarun Tyagi ◽  
Anita Sahu ◽  
...  
Keyword(s):  
Platelet Aggregation ◽  
Nlrp3 Inflammasome ◽  
Thrombus Formation ◽  
Vena Cava ◽  
Early Response ◽  
Sterile Inflammation ◽  
Coagulation System ◽  
Additional Risk Factor ◽  
Whole Transcriptome Analysis

Objective: Besides well known predisposing conditions such as cancer, diabetes, cardiovascular disease and surgery; hypoxia per se has been suggested to be an additional risk factor for venous thrombosis (VT). We have recently shown that hypoxia, either localized due to stasis, or systemic, due to environmental factors such as high altitude exposure, results in a prothrombotic milieu. The proteomic analysis implicated some novel plasma factors that could trigger thrombotic propensity; however, the exact mechanism involved still remains poorly understood. Methods & Results: Effect of hypoxia on coagulation system was analysed using inferior vena cava ligation and simulated hypobaric hypoxia rat models. Data demonstrated that hypoxia modulates both coagulation and fibrinolytic pathways and thrombus developed under hypoxic atmospheres is an aggravated form of thrombus progression under normoxic environments. Moreover, the whole transcriptome analysis using RNA sequencing approach implicated the novel role of NOD Like receptors3 (NLRP3) and inflammasome in thrombus formation suggesting the hypoxia induced thrombosis to be an episode of sterile inflammation. The cytokine array profiling and immunofloroscence data also supported the role of innate immune components. Both pharmacological inhibition and siRNA mediated knockdown of caspase-1 and NLRP-3 respectively reinforced that the activation of NLRP3-inflammasome complex critically regulates thrombogenesis in response to hypoxia. This complex is likely to be activated as an early response to hypoxia, which precedes the platelet aggregation and hence, onset of thrombosis. The translational implication of this novel finding was evident by activation of NLRP3 inflammasome components in human patients who developed VT under hypoxic environments. Conclusions: The current study reveals a novel role of NLRP3 inflammasome in thrombosis induced by localised as well as systemic hypoxic environments. Further, the production of IL-1β by NLRP3 inflammasome augments platelet aggregation, the key event for thrombogenesis.

Abstract 13183: A Novel Model of in vivo Platelet Thrombus Imaging Using CD41-ZsGreen1 Transgenic Rats

Circulation ◽  
2015 ◽  
Vol 132 (suppl_3) ◽  
Author(s):  
Makoto Mizuno ◽  
Atsuyuki Tomizawa ◽  
Kousaku Ohno ◽  
Joseph A. Jakubowski ◽  
Atsuhiro Sugidachi
Keyword(s):  
Platelet Aggregation ◽  
Blood Clotting ◽  
Thrombus Formation ◽  
Green Fluorescence Protein ◽  
In Vivo Models ◽  
Thrombus Imaging ◽  
Vehicle Treatment ◽  
Platelet Dynamics ◽  
Thrombotic Diseases

Introduction: Platelets play important roles in both hemostasis and thrombotic diseases including myocardial and cerebral infarction, and stent thrombosis. While mice models of in vivo fluorescence imaging have been described, there are few suitable in vivo models for platelet imaging in rats which are commonly used as thrombosis models. The objective of this study was to generate fluorescent platelets and assess their dynamics in injured arteries in rats. Methods: We generated CD41-ZsGreen1 transgenic (TG) rats, in which the green fluorescence protein ZsGreen1 was expressed specifically in megakaryocytes and thus platelets, and evaluated platelet dynamics in in vivo thrombus imaging experiments. Hematological, including platelet aggregation and blood clotting time, and biochemical parameters were analysed. In the imaging experiments, saphenous arteries of TG rats were injured with 10% FeCl 3 , and thrombus formation was evaluated as fluorescence accumulation using confocal microscopy. The effect of prasugrel, a thienopyridine ADP receptor antagonist, on thrombus formation was also evaluated. Results: The CD41-ZsGreen1 TG rats exhibited normal hematological and biochemical values with the exception of body weight and erythroid parameters, which were significantly lower than those in wild type (WT) rats. Platelet aggregation, induced by 20 μM ADP or 10 μg/mL collagen, and blood clotting times (APTT and PT) were not significantly different between TG and WT rats. In thrombus formation experiments, FeCl 3 application caused a time-dependent increase in fluorescence intensity in the injured artery in vehicle-treated rats. Prasugrel at an oral dose of 3 mg/kg, treated 2 h before the FeCl 3 application, significantly inhibited fluorescence accumulation compared to the vehicle-treatment group (14.9±2.4 vs 5.4±0.4 arbitrary fluorescence unit at 30 min for vehicle and prasugrel groups, respectively, n=8, p=0.0037). Conclusions: CD41-ZsGreen1 TG rats represent a useful animal for the in vivo imaging of platelet participation in thrombus formation and the evaluation of antithrombotic agents.

Characterization of the Anticoagulant and Antithrombotic Properties of the Sphingosine 1-Phosphate Mimetic FTY720

2016 ◽  
Vol 137 (1) ◽  
pp. 1-6 ◽  
Author(s):  
Zhen Zhao ◽  
Ruixue Wang ◽  
Zhijun Huo ◽  
Chunlei Li ◽  
Zhiyong Wang
Keyword(s):  
Myocardial Infarction ◽  
Platelet Aggregation ◽  
Thrombus Formation ◽  
Vena Cava ◽  
Adenosine Diphosphate ◽  
Inhibitory Effect ◽  
Thrombin Time ◽  
Highly Active ◽  
Sphingosine 1 Phosphate

Sphingosine 1-phosphate (S1P) is a highly active lysophospholipid implicated in various cardiocerebrovascular events such as coagulation, myocardial infarction and stroke. However, as the functional S1P receptor antagonist, whether the S1P mimetic FTY720 can modulate coagulation and/or thrombotic formation remains largely unknown. We investigated the effects of FTY720 on adenosine diphosphate (ADP)-induced platelet aggregation, coagulation parameters and thrombus formation in rats. Pretreatment with FTY720 (2.5 mg/kg) inhibited platelet aggregation induced by ADP, elongated the thrombin time and decreased the fibrinogen levels. However, FTY720 produced no significant effects on the arteriovenous bypass thrombus formation or the FeCl3-induced thrombus formation in the inferior vena cava and the common carotid artery. Our data suggest that FTY720 can exert an inhibitory effect on platelet aggregation and coagulation-related parameters. These characteristics of FTY720 could be useful as an adjunct in the treatment of ischemic diseases such as ischemic stroke and myocardial infarction.

Oxidative Stress and Atherosclerosis: Its Relationship to Growth Factors, Thrombus Formation and Therapeutic Approaches

1999 ◽  
Vol 82 (S 01) ◽  
pp. 32-37 ◽  
Author(s):  
Karlheinz Peter ◽  
Wolfgang Kübler ◽  
Johannes Ruef ◽  
Thomas K. Nordt ◽  
Marschall S. Runge ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Growth Factors ◽  
Vessel Wall ◽  
Inflammatory Responses ◽  
Plaque Rupture ◽  
Thrombus Formation ◽  
Vascular Lesion ◽  
Coagulation System ◽  
Therapeutic Approaches ◽  
Causative Relationship

SummaryThe initiating event of atherogenesis is thought to be an injury to the vessel wall resulting in endothelial dysfunction. This is followed by key features of atherosclerotic plaque formation such as inflammatory responses, cell proliferation and remodeling of the vasculature, finally leading to vascular lesion formation, plaque rupture, thrombosis and tissue infarction. A causative relationship exists between these events and oxidative stress in the vessel wall. Besides leukocytes, vascular cells are a potent source of oxygen-derived free radicals. Oxidants exert mitogenic effects that are partially mediated through generation of growth factors. Mitogens, on the other hand, are potent stimulators of oxidant generation, indicating a putative self-perpetuating mechanism of atherogenesis. Oxidants influence the balance of the coagulation system towards platelet aggregation and thrombus formation. Therapeutic approaches by means of antioxidants are promising in both experimental and clinical designs. However, additional clinical trials are necessary to assess the role of antioxidants in cardiovascular disease.

Difference of [Ca2+]i Movements in Platelets Stimulated by Thrombin and TRAP: the Involvement of αIIbβ3-Mediated TXA2 Synthesis

1998 ◽  
Vol 79 (06) ◽  
pp. 1184-1190 ◽  
Author(s):  
Yoshiaki Tomiyama ◽  
Shigenori Honda ◽  
Kayoko Senzaki ◽  
Akito Tanaka ◽  
Mitsuru Okubo ◽  
...  
Keyword(s):  
Platelet Aggregation ◽  
Fibrinogen Binding ◽  
Adp Release ◽  
The Difference ◽  
Txa2 Receptor Antagonist ◽  
High Level ◽  
Inhibition Studies ◽  
Peak Increase ◽  
Second Peak ◽  
Assay Conditions

SummaryThis study investigated the difference of [Ca2+]i movement in platelets in response to thrombin and TRAP. The involvement of αIIbβ3 in this signaling was also studied. Stimulation of platelets with thrombin at 0.03 U/ml caused platelet aggregation and a two-peak increase in [Ca2+]i. The second peak of [Ca2+]i, but not the first peak was abolished by the inhibition of platelet aggregation with αIIbβ3 antagonists or by scavenging endogenous ADP with apyrase. A cyclooxygenase inhibitor, aspirin, and a TXA2 receptor antagonist, BM13505, also abolished the second peak of [Ca2+]i but not the first peak, although these regents did not inhibit aggregation. Under the same assay conditions, measurement of TXB2 demonstrated that αIIbβ3 antagonists and aspirin almost completely inhibited the production of TXB2. In contrast to thrombin-stimulation, TRAP caused only a single peak of [Ca2+]i even in the presence of platelet aggregation, and a high level of [Ca2+]i increase was needed for the induction of platelet aggregation. The inhibition of aggregation with αIIbβ3 antagonists had no effect on [Ca2+]i change and TXB2 production induced by TRAP. Inhibition studies using anti-GPIb antibodies suggested that GPIb may be involved in the thrombin response, but not in the TRAP. Our findings suggest that low dose thrombin causes a different [Ca2+]i response and TXA2 producing signal from TRAP. Endogenous ADP release and fibrinogen binding to αIIbβ3 are responsible for the synthesis of TXA2 which results in the induction of the second peak of [Ca2+]i in low thrombin- but not TRAP-stimulated platelets.

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