ArticleJournal of thrombosis and haemostasis : JTH2009
Rap1b is critical for glycoprotein VI-mediated but not ADP receptor-mediated alpha2beta1 activation.
Article in Journal of thrombosis and haemostasis : JTH, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- Review
- Circular RNA Expression Profiles in Plasma from Patients with Heart Failure Related to Platelet Activity.Biomolecules · 2020Article
- MiR-181a Reduces Platelet ActivationMicroRNA (Shariqah, United Arab Emirates) · 2020Article
- CLIC1 null mice demonstrate a role for CLIC1 in macrophage superoxide production and tissue injury.Physiological reports · 2017Article
- Article
- Chemoproteomic discovery of AADACL1 as a regulator of human platelet activation.Chemistry & biology · 2013Article
- The Small GTPase Rap1b: A Bidirectional Regulator of Platelet Adhesion Receptors.Journal of signal transduction · 2012Article
- Distinct roles for Rap1b protein in platelet secretion and integrin αIIbβ3 outside-in signaling.The Journal of biological chemistry · 2011Article
- The genetics of common variation affecting platelet development, function and pharmaceutical targeting.Journal of thrombosis and haemostasis : JTH · 2011Review
- Genome-wide meta-analyses identifies seven loci associated with platelet aggregation in response to agonists.Nature genetics · 2010Article
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
Abstract
backgroundThe platelet alpha2beta1 integrin functions as both an adhesion and signaling receptor upon exposure to collagen. Recent studies have indicated that alpha2beta1 function can be activated via inside-out signaling, similar to the prototypical platelet integrin alphaIIbbeta3. However, signaling molecules that regulate alpha2beta1 activation in platelets are not well defined. A strong candidate molecule is the small GTPase Rap1b, the dominant platelet isoform of Rap1, which regulates alphaIIbbeta3 activation.
objectivesWe hypothesized that Rap1b positively regulates alpha2beta1 during agonist-induced platelet activation.
methodsTo test whether Rap1b activates alpha2beta1 downstream of glycoprotein (GP)VI or other platelet receptors, we stimulated platelets purified from Rap1b-/- or wild-type mice with diverse agonists and measured alpha2beta1 activation using fluorescein isothiocyanate-labeled monomeric collagen. We also examined the role of Rap1b in outside-in signaling pathways by analyzing adhesion and spreading of Rap1b-/- or wild-type platelets on monomeric, immobilized collagen. Finally, we monitored the activation status of related Rap GTPases to detect changes in signaling pathways potentially associated with Rap1b-mediated events.
resultsRap1b-/- platelets displayed comparable ADP-induced or thrombin-induced alpha2beta1 activation as wild-type platelets, but reduced convulxin-dependent alpha2beta1 activation. Rap1b-/- platelets exhibited increased spreading on immobilized collagen but similar adhesion to immobilized collagen compared to wild-type platelets. Rap1b-/- platelets also showed Rap1a and Rap2 activation upon agonist stimulation, possibly revealing functional compensation among Rap family members.
conclusionsRap1b is required for maximal GPVI-induced but not ADP-induced activation of alpha2beta1 in murine platelets.
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