Human Platelets
인간 혈소판

Human Platelets(인간 혈소판)란 무엇입니까?

Human Platelets 인간 혈소판 - We also noted species specific differences in levels of hemostatic, secretory, and inflammatory regulators in ground squirrel platelets relative to human platelets. ^[1] Currently, multiple discoveries have allowed the identification and characterization of PMPs (platelet microbicidal proteins) and opened the way to identify kinocidins and CHDPs (cationic host defense peptides) in human platelets. ^[2] Human platelets were treated with protease-activated receptor 1 (PAR-1)-activating peptide in the presence or absence of S1P, S1PR agonists or antagonists, and sphingosine kinases inhibitors. ^[3] Besides, PD increased phosphorylation of phosphoinositide 3-kinase (PI3K), protein kinase B (PKB or Akt), and glycogen synthase kinase 3β (GSK3β) in human platelets. ^[4] This paper describes a detailed study of spectral and time-resolved photoprocesses in human platelets and their complexes with platinum (Pt) nanoparticles (NPs). ^[5] Conclusion: Clinically relevant concentrations of adrenaline may significantly augment responses of human platelets in the presence of subthreshold concentrations of collagen, which should be considered during therapies involving adrenaline infusion. ^[6] Human platelets were stimulated with different levels of shear stress (500, 750, 1000 dynes/cm2) over a range of exposure times (10, 20, and 30 min) within capillary tubes made of various polymeric materials. ^[7] Pimpinellin pretreatment suppressed adhesion and spreading of human platelets on the fibrinogen coated surface. ^[8] Human platelets were treated with matrine (0–1 mg/ml) for 1 h at 37°C followed by measuring platelet aggregation, granule secretion, receptor expression by flow cytometry, spreading and clot retraction. ^[9] Human platelets do not express any antigens of the Rhesus system. ^[10] Using cocultures of human platelets and human colon adenocarcinoma cells (line HT29) and LC-MS/MS, we investigated the impact of platelets on cancer cell biosynthesis of 12S-HETE and its esterification into PLs and whether platelet ability to transfer its molecular cargo might play a role. ^[11] While activation of human platelets by human von Willebrand factor (vWF) requires vWF activation by shear stress, contact between human platelets and porcine vWF (pvWF) leads to spontaneous platelet adhesion and activation. ^[12] We show that (1) key platelet proteins are modified by arginine methylation; (2) incubation of human platelets with PRMT inhibitors for 4 h results in impaired capacity of platelets to aggregate in response to thrombin and collagen, with IC50 values in the μM range; and (3) treatment with PRMT inhibitors leads to decreased membrane expression and reduced activation of the critical platelet integrin αIIbβ3. ^[13] In human platelets, we identified phosphorylated tyrosines mapped to luminal or extracellular domains of transmembrane and secreted proteins implicated in the regulation of platelet activation. ^[14] Cytokine-converting growth factor-b (TGF-b) is initially purified from human platelets, a rich source of this protein. ^[15] On the other hand, human platelets are recognized as the principal components affecting the onset and progression of AD. ^[16] Here we tested the reliability of a protocol designed to study mitochondrial respiratory control in human platelets (PLTs) in field studies, using high-resolution respirometry (HRR). ^[17] All tested lipid fractions showed strong anti-platelet-activating factor (PAF) and antithrombin activities in human platelets (half maximal inhibitory concentration (IC50) values ranging ~25–200 μg of lipid) with the highest activities in glyco- and phospho-lipid fractions. ^[18] in vitroAnti-platelet aggregation was determined using human platelets. ^[19] Human platelets were used in the present study. ^[20] METHODS The platelet aggregation was performed using a Lumi-aggregometer; the inhibitory activity of 16 compounds were evaluated by inducing the aggregation of human platelets (250 × 103/μl) with epinephrine (10 µM), collagen (2 µg / ml) or ADP (10 µM). ^[21] OBJECTIVES To investigate the expression of proteins involved in the extrinsic apoptosis pathway, including the death receptors, adaptor and regulator proteins in human platelets. ^[22] Without a nucleus, there is a limited range of experimental manipulations that are possible with human platelets to study the molecular basis of integrin signaling in these primary cells. ^[23] Interestingly, cilostazol specifically reduced the release of phosphatidylserine-positive extracellular vesicles (EVs) from human platelets while not affecting total EV release. ^[24] By using this antibody as a tool, we showed that protein kinase C (PKC)-mediated Dab2-pSer24 was a conservative signaling event when human platelets were activated by the platelet agonists such as thrombin, collagen, ADP, 12-O-tetradecanoylphorbol-13-acetate, and the thromboxane A2 activator U46619. ^[25] Here we describe the validation of a TE assay for ABBV-151 using human platelets to measure receptor occupancy (RO) and binding saturation, that will inform dosing decisions during a first-in-human Phase I dose escalation study. ^[26] In order to define new anti-metastasis therapies exhibiting a high specificity for the pathological tumor cell-platelet interactions without abrogating normal platelet functions we developed a high throughput assay that showed that pharmacological blockade of cysteinyl leukotriene receptor 1 (CysLT1) with two already FDA-approved drugs in asthma (Zarfirlukast and Montelukast), dose-dependently inhibited the mitogenic action of human platelets on human MDA-B02/Luc breast cancer cells. ^[27] Human platelets were treated with various types of pMSCs either directly or with their secretome, and their effect on agonist‐mediated platelet activation and functional characteristics were evaluated. ^[28] In the present study, we described a microengineered microfluidic system that contained a drug concentration generator, cancer cell culture chip, and three-dimensional (3D) circular microvascular model covered with a confluent endothelial layer and perfused with human platelets at a stable flow rate. ^[29] Also, the adhesion of platelet and albumin on the three DESs was assessed by an in-vitro flow loop model using human platelets under aspirin SAPT and fluorescent albumin, respectively. ^[30] In this study, curcumin did not activate caspase 3-dependent apoptosis of human platelets, but rather induced the formation of procoagulant platelets. ^[31] The aim of our study was to identify the toxicity of aluminum-silicon sorbents modified with carbon nanomaterial for human platelets. ^[32] Contrary to mice, human platelets are unique in their expression of the FcγRIIA/CD32A receptor, suggesting that our understanding of the pathogenesis of antibody-mediated TRALI is partial, since the current murine models incompletely recapitulate the human immunology. ^[33] Evidence for shear-mediated Ca entry through mechanosensitive cation channels in human platelets and a megakaryocytic cell line. ^[34] There is controversy about the effect of BTZ on human platelets, so we set out to determine its effect on various types of platelet samples. ^[35] Results: We show that PI3K Class IA inhibitors potently block calcium mobilization in human platelets. ^[36] We investigated phosphorylation of PKCδ following glycoprotein VI-mediated and PAR4-mediated platelet activation and found that Y311 is selectively phosphorylated when PAR4 is activated in human platelets. ^[37] Human platelets were activated with convulxin (CVX), thrombin (THR) or protease-activated receptor (PARs) agonists, epinephrine (EPI), and combination thereof. ^[38] Methods The uptake of anti-VEGF agents with or without VEGF treatment was investigated using immunofluorescence and immunogold staining in human platelets. ^[39] This method was validated in cultured cells and was applied in HeLa cells and human platelets of coronary artery disease patients. ^[40] Previous reports of cadherin‐6 on human platelets have demonstrated its role in platelet aggregation and thrombus formation. ^[41] In cocultures of human platelets and myofibroblasts, platelet TXA2 induced profibrotic gene expression, including TGF-β1.