Integrin αIIbβ3

Plow, Edward F.; Pesho, Michelle M.; Ma, Yanqing

doi:10.1016/b978-012369367-9/50770-9

Cited by 17 publications

(13 citation statements)

References 176 publications

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“…The molecule has an elongated dimeric structure with two sets of three polypeptide chains [2]. The platelet integrin receptor αIIbβ3 recognizes and binds fibrinogen from solution only after the receptor is activated by agonists such as ADP or thrombin [3–5]. …”

Section: Introductionmentioning

confidence: 99%

Excess fibrinogen adsorption to monolayers of mixed lipids

Deshmukh¹,

Britt²,

Hlady³

2010

Colloids and Surfaces B: Biointerfaces

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Adsorption of fibrinogen to the monolayers of mixed lipids, dipalmitoyl phosphatidyl choline (DPPC) and eicosylamine (EA) was measured at a surface pressure of 20 mN/m by an in situ surface plasmon resonance technique. Pressure-area isotherms of DPPC+EA mixtures on water and buffer subphases indicated good lipid miscibility and some contraction of the monolayers at intermediate and higher surface pressures. Surface electric potential of the DPPC+EA monolayers showed excess values for intermediate DPPC:EA ratios. Fibrinogen adsorption and its adsorption rates from a dilute solution (0.03 mg/ml) were proportional to the fraction of EA in the monolayer indicating that protein binding was primarily driven by electrostatic interactions between positive EA charges in the monolayer and a net negative protein charge. At a higher protein concentration (0.06 mg/ml) both the fibrinogen adsorbed amount and its maximum adsorption rate showed excess values relative to the pure EA for 1:1, 2:1 and 3:1 DPPC+EA monolayers. This excess adsorption could be explained, in part, by the contraction of the monolayers with intermediate DPPC:EA ratios which resulted in an excess surface electric potential.

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Section: Introductionmentioning

confidence: 99%

Excess fibrinogen adsorption to monolayers of mixed lipids

Deshmukh¹,

Britt²,

Hlady³

2010

Colloids and Surfaces B: Biointerfaces

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“…Fourteen of those proteins are either signaling or cytoskeletal, and nine of them are known to play a major role in platelet activation by αIIbβ3 and/or GPVI receptors ( Figure 3 ). More precisely, eight of them play a relevant role in integrin αIIbβ3 signaling: α-actinin-1, ADAP (adhesion- and degranulation promoting adapter protein) – also known as FYB or SLAP-130 - and Src [12] ; filamin-A [16] , F-actin capping protein [17] , zyxin [17] , ILK [18] , and talin-1 [19] . Interestingly, ILK was also shown to interact with SPARC ( Secreted Protein Acidic and Rich in Cysteine ) ( Fig.…”

Section: Resultsmentioning

confidence: 99%

Proteins Involved in Platelet Signaling Are Differentially Regulated in Acute Coronary Syndrome: A Proteomic Study

et al. 2010

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BackgroundPlatelets play a fundamental role in pathological events underlying acute coronary syndrome (ACS). Because platelets do not have a nucleus, proteomics constitutes an optimal approach to follow platelet molecular events associated with the onset of the acute episode.Methodology/Principal FindingsWe performed the first high-resolution two-dimensional gel electrophoresis-based proteome analysis of circulating platelets from patients with non-ST segment elevation ACS (NSTE-ACS). Proteins were identified by mass spectrometry and validations were by western blotting. Forty protein features (corresponding to 22 unique genes) were found to be differentially regulated between NSTE-ACS patients and matched controls with chronic ischemic cardiopathy. The number of differences decreased at day 5 (28) and 6 months after the acute event (5). Interestingly, a systems biology approach demonstrated that 16 of the 22 differentially regulated proteins identified are interconnected as part of a common network related to cell assembly and organization and cell morphology, processes very related to platelet activation. Indeed, 14 of those proteins are either signaling or cytoskeletal, and nine of them are known to participate in platelet activation by αIIbβ3 and/or GPVI receptors. Several of the proteins identified participate in platelet activation through post-translational modifications, as shown here for ILK, Src and Talin. Interestingly, the platelet-secreted glycoprotein SPARC was down-regulated in NSTE-ACS patients compared to stable controls, which is consistent with a secretion process from activated platelets.Conclusions/SignificanceThe present study provides novel information on platelet proteome changes associated with platelet activation in NSTE-ACS, highlighting the presence of proteins involved in platelet signaling. This investigation paves the way for future studies in the search for novel platelet-related biomarkers and drug targets in ACS.

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“…Platelet surface receptor GPIIbIIIa plays a key role in platelet aggregation, hemostasis, and thrombosis. 30,31 However, as shown in Table 1, data from a murine model of immune thrombocytopenia demonstrate that GPIIbIIIa may be directly involved in PL-Apo, since strong thrombocytopenia induced by injection into mice of anti-GPIIb antibody, resulting in a reduction of platelet count by approximately 75%, was associated with increase in ΔΨm depolarization, caspase-3 activation, and PS exposure. 32 Furthermore, clinical studies have shown that pediatric acute immune thrombocytopenia (often associated with GPIIbIIIa autoantibodies) was also associated with increased ΔΨm depolarization, caspase-3, -9, -8 activation, PS exposure, and MP formation.…”

Section: Platelet Apoptosis Mediated By Glycoprotein Iibiiia (Gpiibiiia)mentioning

confidence: 99%

“…Platelet surface receptor GPIIbIIIa plays a key role in platelet aggregation, hemostasis, and thrombosis. 30,31 However, as [20][21][22][23][24][25]28,29 ; (b) [30][31][32][33] ; (c) [34][35][36] ; (d) [22][23][24][37][38][39][40] ; (e) [22][23][24][37][38][39][40] .…”

Section: Platelet Apoptosis Mediated By Protease-activated Receptor-1 (Par-1) Of Thrombinmentioning

confidence: 99%

Platelet Apoptosis Can Be Triggered Bypassing the Death Receptors

Leytin

Gyulkhandanyan

Freedman

2019

Clin Appl Thromb Hemost

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In nucleated cells, the extrinsic pathway of the programmed cell death (apoptosis) is triggered by interaction of death ligands of the tumor necrosis factor superfamily with the death receptors on external cell surface membrane. In this review, we present evidence that, in contrast to nucleated cells, apoptosis in anucleate platelets can be induced through bypassing the death receptors, using instead specific receptors on the platelet surface mediating platelet activation, aggregation, and blood coagulation. These platelet surface receptors include the protease-activated receptor 1 of thrombin and glycoproteins IIbIIIa and Ibα, receptors of fibrinogen, and von Willebrand factor. The pro-apoptotic BH3 mimetic ABT-737 and calcium ionophore A23187 also trigger platelet apoptosis without using death receptors. These agents induce the intrinsic pathway of platelet apoptosis by direct targeting mitochondrial and extra-mitochondrial apoptotic responses.

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Integrin αIIbβ3

Cited by 17 publications

References 176 publications

Excess fibrinogen adsorption to monolayers of mixed lipids

Excess fibrinogen adsorption to monolayers of mixed lipids

Proteins Involved in Platelet Signaling Are Differentially Regulated in Acute Coronary Syndrome: A Proteomic Study

Platelet Apoptosis Can Be Triggered Bypassing the Death Receptors

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