Abstract
Extensive study in integrin research has seen the platelet specific receptor αIIbβ3 (Glycoprotein GPIIb / IIIa) under much scrutiny, and provided vast information as to the workings of this integrin within the blood. Glanzmanns thrombasthenia, a rare autosomal recessive bleeding disorder, highlights the vital role played by this receptor in platelet function [1]. Glanzmanns thrombasthenic platelets fail to aggregate due to a lack of surface expression of functional aIIb or β3 on the platelet surface. However, little is known about the precise molecular mechanisms involved in the operation of this receptor on the platelet surface. Clinical trials using intravenous antagonists to this receptor have shown them to be effective anti-thrombotics. However the recent observations that the oral αIIbβ3 antagonists have failed to show benefits in the treatment of acute coronary syndromes, and in fact, increase mortality, underscores the necessity for a more complete understanding of aIIbb3 and its functions [2, 3]. A more profound knowledge of the precise nature of the platelet integrin-activation, along with an understanding of its interactions with cellular signaling proteins, will undoubtedly lead to the identification of novel strategies for the effective inhibition of platelet integrin function.
Keywords: anti-platelet therapies, integrin, glycoprotein, glanzmanns thrombasthenia, autosomal recessive bleeding disorder
Current Pharmaceutical Design
Title: Novel Integrin-Specific Targets for Anti-Platelet Therapies
Volume: 10 Issue: 14
Author(s): Aisling Robinson, Sarah O'Neill and Niamh Moran
Affiliation:
Keywords: anti-platelet therapies, integrin, glycoprotein, glanzmanns thrombasthenia, autosomal recessive bleeding disorder
Abstract: Extensive study in integrin research has seen the platelet specific receptor αIIbβ3 (Glycoprotein GPIIb / IIIa) under much scrutiny, and provided vast information as to the workings of this integrin within the blood. Glanzmanns thrombasthenia, a rare autosomal recessive bleeding disorder, highlights the vital role played by this receptor in platelet function [1]. Glanzmanns thrombasthenic platelets fail to aggregate due to a lack of surface expression of functional aIIb or β3 on the platelet surface. However, little is known about the precise molecular mechanisms involved in the operation of this receptor on the platelet surface. Clinical trials using intravenous antagonists to this receptor have shown them to be effective anti-thrombotics. However the recent observations that the oral αIIbβ3 antagonists have failed to show benefits in the treatment of acute coronary syndromes, and in fact, increase mortality, underscores the necessity for a more complete understanding of aIIbb3 and its functions [2, 3]. A more profound knowledge of the precise nature of the platelet integrin-activation, along with an understanding of its interactions with cellular signaling proteins, will undoubtedly lead to the identification of novel strategies for the effective inhibition of platelet integrin function.
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Cite this article as:
Robinson Aisling, O'Neill Sarah and Moran Niamh, Novel Integrin-Specific Targets for Anti-Platelet Therapies, Current Pharmaceutical Design 2004; 10 (14) . https://dx.doi.org/10.2174/1381612043384628
DOI https://dx.doi.org/10.2174/1381612043384628 |
Print ISSN 1381-6128 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4286 |
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