Further Investigations of the Effects of Anti-β<sub>2</sub>GP1 Antibodies on Collagen-Induced Platelet Aggregation

Ho, Yik C; Ahuja, Kiran; Adams, Murray J.

doi:10.1177/1076029617736384

Cited by 4 publications

(1 citation statement)

References 27 publications

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“…When collagen was used, affinity purified rabbit anti-β 2 GP1 antibodies [99] enhanced platelet aggregation. However, no effect was demonstrated using patient-derived IgG fractions (containing aCL and anti-β 2 GP1 antibodies) [106] and affinity-purified goat anti-β 2 GP1 antibodies [107]. Based on these results, it is difficult to arrive at a consensus due to the variable effects possibly caused by anti-β 2 GP1 antibodies with different structure and binding specificities.…”

Section: Anti-β2gp1-β2gp1 Complexes and Plateletsmentioning

confidence: 99%

β2GP1, Anti-β2GP1 Antibodies and Platelets: Key Players in the Antiphospholipid Syndrome

Ahuja

Körner

et al. 2016

Antibodies

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Anti-beta 2 glycoprotein 1 (anti-β 2 GP1) antibodies are commonly found in patients with autoimmune diseases such as the antiphospholipid syndrome (APS) and systemic lupus erythematosus (SLE). Their presence is highly associated with increased risk of vascular thrombosis and/or recurrent pregnancy-related complications. Although they are a subtype of anti-phospholipid (APL) antibody, anti-β 2 GP1 antibodies form complexes with β 2 GP1 before binding to different receptors associated with anionic phospholipids on structures such as platelets and endothelial cells. β 2 GP1 consists of five short consensus repeat termed “sushi” domains. It has three interchangeable conformations with a cryptic epitope at domain 1 within the molecule. Anti-β 2 GP1 antibodies against this cryptic epitope are referred to as ‘type A’ antibodies, and have been suggested to be more strongly associated with both vascular and obstetric complications. In contrast, ‘type B’ antibodies, directed against other domains of β 2 GP1, are more likely to be benign antibodies found in asymptomatic patients and healthy individuals. Although the interactions between anti-β 2 GP1 antibodies, β 2 GP1, and platelets have been investigated, the actual targeted metabolic pathway(s) and/or receptor(s) involved remain to be clearly elucidated. This review will discuss the current understanding of the interaction between anti-β 2 GP1 antibodies and β 2 GP1, with platelet receptors and associated signalling pathways.

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Section: Anti-β2gp1-β2gp1 Complexes and Plateletsmentioning

confidence: 99%

β2GP1, Anti-β2GP1 Antibodies and Platelets: Key Players in the Antiphospholipid Syndrome

Ahuja

Körner

et al. 2016

Antibodies

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IgG fractions from patients with antiphospholipid syndrome and systemic lupus erythematosus bind to platelets, but do not affect collagen-induced platelet activation

Brake

Ahuja

et al. 2022

Biotechnic & Histochemistry

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Shedding of soluble glycoprotein VI is neither affected by animal-derived antibeta-2-glycoprotein 1 antibodies nor IgG fractions from patients with systemic lupus erythematosus

Ahuja

Andrews

et al. 2020

Blood Coagulation &Amp; Fibrinolysis

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Antibeta-2-glycoprotein 1 (antiβ2GP1) antibodies are associated with increased risk of thrombosis in patients with systemic lupus erythematosus (SLE). The specific effect(s) of antiβ2GP1 antibodies on platelets are unclear. Platelet activation in response to antiplatelet antibodies has been shown to induce shedding of the ectodomain of the platelet collagen receptor, glycoprotein VI (GPVI), releasing soluble GPVI (sGPVI). The aim of this study was to therefore determine whether antiβ2GP1 antibodies, and/or purified IgG fractions, from patients with SLE shed sGPVI from platelets. We determined sGPVI levels in platelet poor plasma from SLE patients with/without antiβ2GP1 antibodies (n = 37), as well as in platelet-rich plasma from healthy donors treated with either SLE-derived IgG fractions containing antiβ2GP1, animal-derived antiβ2GP1, or isotype control antibodies. Levels of sGPVI were higher in three SLE-derived platelet poor plasma with antiβ2GP1 antibodies (103.52 ± 12.32 ng/ml) compared with those without (28.11 ± 12.73 ng/ml). Neither SLE-derived IgG fractions containing antiβ2GP1 antibodies, nor animal-derived antiβ2GP1 antibodies induced significant shedding of sGPVI from healthy donor platelets compared with isotype controls. These results suggest that antiβ2GP1 antibodies do not affect shedding of sGPVI, and therefore collagen-mediated platelet signalling pathways. The shedding activity in SLE patients may be due to factors other than antiβ2GP1 antibodies, for example, metalloproteinases.

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Further Investigations of the Effects of Anti-β₂GP1 Antibodies on Collagen-Induced Platelet Aggregation

Cited by 4 publications

References 27 publications

β2GP1, Anti-β2GP1 Antibodies and Platelets: Key Players in the Antiphospholipid Syndrome

β2GP1, Anti-β2GP1 Antibodies and Platelets: Key Players in the Antiphospholipid Syndrome

IgG fractions from patients with antiphospholipid syndrome and systemic lupus erythematosus bind to platelets, but do not affect collagen-induced platelet activation

Shedding of soluble glycoprotein VI is neither affected by animal-derived antibeta-2-glycoprotein 1 antibodies nor IgG fractions from patients with systemic lupus erythematosus

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Further Investigations of the Effects of Anti-β2GP1 Antibodies on Collagen-Induced Platelet Aggregation

Cited by 4 publications

References 27 publications

β2GP1, Anti-β2GP1 Antibodies and Platelets: Key Players in the Antiphospholipid Syndrome

β2GP1, Anti-β2GP1 Antibodies and Platelets: Key Players in the Antiphospholipid Syndrome

IgG fractions from patients with antiphospholipid syndrome and systemic lupus erythematosus bind to platelets, but do not affect collagen-induced platelet activation

Shedding of soluble glycoprotein VI is neither affected by animal-derived antibeta-2-glycoprotein 1 antibodies nor IgG fractions from patients with systemic lupus erythematosus

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Further Investigations of the Effects of Anti-β₂GP1 Antibodies on Collagen-Induced Platelet Aggregation