Localization and characterization of an alpha-thrombin-binding site on platelet glycoprotein Ib alpha.

Marco, Luigi De; Mazzucato, M.; Masotti, Adriana; Ruggeri, Zaverio M.

doi:10.1016/s0021-9258(17)37396-9

Cited by 136 publications

(19 citation statements)

References 38 publications

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“…Although PAR4 is not activated at this concentration of thrombin, 27 residual aggregation may be explained by the action of thrombin on non-PAR receptors, such as glycoprotein Ib. 21 The specificity of the PAR1 antagonist peptide was confirmed by a lack of effect on platelet aggregation induced by collagen, epinephrine, and ADP (data not shown). Similar results were obtained with a distinct PAR1 antagonist peptide, MSRPACN, isolated from a random phage display library 22 (data not shown).…”

Section: Resultsmentioning

confidence: 85%

“…18,19 In addition to PAR1, platelets possess other thrombin receptors, including PAR4 and glycoprotein Ib. 20,21 The PAR1 component of the platelet response to thrombin or other PAR receptor agonists, such as SFLLRN or trypsin, can be defined in vitro through the use of PAR1-specific antagonistic peptides that competitively block the binding of tethered ligand and thereby prevent receptor activation. 18,22 In the present article, we have used such peptides to initially define in washed platelets the PAR1 dependence of platelet activation in response to thrombin and trypsin.…”

mentioning

confidence: 99%

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The antithrombotic effect of aprotinin: actions mediated via the protease-activated receptor 1

Poullis

Manning

Laffan

et al. 2000

The Journal of Thoracic and Cardiovascular Surgery

112

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Section: Resultsmentioning

confidence: 85%

mentioning

confidence: 99%

The antithrombotic effect of aprotinin: actions mediated via the protease-activated receptor 1

Poullis

Manning

Laffan

et al. 2000

The Journal of Thoracic and Cardiovascular Surgery

112

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“…The extracellular domain comprises the binding site for vWF, P-selectin, and Mac-1 (Table 1). In addition to its dynamic role in platelet recruitment onto vWF, the GPIb membrane complex functions as a receptor for coagulation factor XII [17], XI [18], thrombin [19,20], and HK (high-molecular-weight kininogen) [21]. Hence, GPIb is a receptor linking primary and secondary hemostasis [7].…”

Section: Gpib-ix-v Complexmentioning

confidence: 99%

Molecular Aspects of Pathophysiology of Platelet Receptors

Poddar¹,

Banerjee²

2020

Platelets

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Receptor is a dynamic instrumental surface protein that helps to interact with specific molecules to respond accordingly. Platelet is the smallest in size among the blood components, but it plays many pivotal roles to maintain hemostasis involving its surface receptors. It (platelet) has cell adhesion receptors (e.g., integrins and glycoproteins), leucine-rich repeats receptors (e.g., TLRs, glycoprotein complex, and MMPs), selectins (e.g., CLEC, P-selectin, and CD), tetraspanins (e.g., CD and LAMP), transmembrane receptors (e.g., purinergic—P2Y and P2X1), prostaglandin receptors (e.g., TxA2, PGH2, and PGI2), immunoglobulin superfamily receptors (e.g., FcRγ and FcεR), etc. on its surface. The platelet receptors (e.g., glycoproteins, protease-activated receptors, and GPCRs) during platelet activation are over expressed and their granule contents are secreted (including neurotransmitters, cytokines, and chemokines) into circulation, which are found to be correlated with different physiological conditions. Interestingly, platelets promote metastasis through circulation protecting from cytolysis and endogenous immune surveillance involving several platelets receptors. The updated knowledge about different types of platelet receptors in all probable aspects, including their inter- and intra-signaling mechanisms, are discussed with respect to not only its (platelets) receptor type but also under different pathophysiological conditions.

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“…GPIb-IX also binds thrombin and is important for low dose thrombin-induced platelet activation (78,95,242). This function of GPIb-IX requires the thrombin binding sites around three sulfated tyrosine residues (Y 276 DYY) (27,48,55,143) in the ligand-binding domain of GPIb␣, which is distinct from the VWF binding site (27,47,48,55,143). It is important to note that, under conditions where thrombosis is induced by limited vascular injury (such as the laser-induced arterial injury model), only low concentrations of thrombin are detectable, which, however, are critical for platelet thrombus formation in vivo (57).…”

mentioning

confidence: 99%

New Concepts and Mechanisms of Platelet Activation Signaling

2017

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Upon blood vessel injury, platelets are exposed to adhesive proteins in the vascular wall and soluble agonists, which initiate platelet activation, leading to formation of hemostatic thrombi. Pathological activation of platelets can induce occlusive thrombosis, resulting in ischemic events such as heart attack and stroke, which are leading causes of death globally. Platelet activation requires intracellular signal transduction initiated by platelet receptors for adhesion proteins and soluble agonists. Whereas many platelet activation signaling pathways have been established for many years, significant recent progress reveals much more complex and sophisticated signaling and amplification networks. With the discovery of new receptor signaling pathways and regulatory networks, some of the long-standing concepts of platelet signaling have been challenged. This review provides an overview of the new developments and concepts in platelet activation signaling.

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Localization and characterization of an alpha-thrombin-binding site on platelet glycoprotein Ib alpha.

Cited by 136 publications

References 38 publications

The antithrombotic effect of aprotinin: actions mediated via the protease-activated receptor 1

The antithrombotic effect of aprotinin: actions mediated via the protease-activated receptor 1

Molecular Aspects of Pathophysiology of Platelet Receptors

New Concepts and Mechanisms of Platelet Activation Signaling

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