Targeting platelet inhibition receptors for novel therapies: PECAM-1 and G6b-B

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Soriano Jerez, E. M., Gibbins, J. M. orcid id iconORCID: https://orcid.org/0000-0002-0372-5352 and Hughes, C. E. orcid id iconORCID: https://orcid.org/0000-0002-9790-5820 (2021) Targeting platelet inhibition receptors for novel therapies: PECAM-1 and G6b-B. Platelets, 32 (6). pp. 761-769. ISSN 0953-7104 doi: 10.1080/09537104.2021.1882668

Abstract/Summary

While current oral antiplatelet therapies benefit many patients, they deregulate the haemostatic balance leaving patients at risk of systemic side-effects such as haemorrhage. Dual antiplatelet treatment is the standard approach, combining aspirin with P2Y12 blockers. These therapies mainly target autocrine activation mechanisms (TxA2, ADP) and, more recently, the use of thrombin or thrombin receptor antagonists have been added to the available approaches. Recent efforts to develop new classes of anti-platelet drugs have begun to focus on primary platelet activation pathways such as through the immunoreceptor tyrosine-based activation motif (ITAM)-containing collagen receptor GPVI/FcR-chain complex. There are already encouraging results from targeting GPVI, with reduced aggregation and smaller arterial thrombi, without major bleeding complications, likely due to overlapping activation signalling pathways with other receptors such as the GPIb–V–IX complex. An alternative approach to reduce platelet activation could be to inhibit this signalling pathway by targeting the inhibitory pathways intrinsic to platelets. Stimulation of endogenous negative modulators could provide more specific inhibition of platelet function, but is this feasible? In this review, we explore the potential of the two major platelet immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing inhibitory receptors, G6b-B and PECAM-1, as antithrombotic targets.

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Item Type Article
URI https://reading-clone.eprints-hosting.org/id/eprint/95978
Identification Number/DOI 10.1080/09537104.2021.1882668
Refereed Yes
Divisions Life Sciences > School of Biological Sciences > Biomedical Sciences
Publisher Taylor & Francis
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