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Cited by 107Platelet Disorders and TreatmentsProtein Kinase Regulation and GTPase SignalingBlood Coagulation and Thrombosis Mechanisms

The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.

Potent inhibition of human platelets by cGMP analogs independent of cGMP-dependent protein kinase

Gambaryan, Stepan, Geiger, Jörg, Schwarz, Ulrike R., Butt, Elke, Begonja, Antonija, Obergfell, Achim, Walter, Ulrich·2004·Blood
DOI 10.1182/blood-2003-09-3349
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Abstract

Platelets play a key role in hemostasis through their ability to rapidly adhere to activated or injured endothelium, subendothelial matrix proteins, and other activated platelets. A strong equilibrium between activating and inhibiting processes is essential for normal platelet and vascular function, impairment of this equilibrium being associated with either thrombophilic or bleeding disorders. Both cyclic guanosine monophosphate (cGMP) and cyclic adenosine monophosphate (cAMP) have been established as crucial and synergistic intracellular messengers that mediate the effects of platelet inhibitors such as nitric oxide (NO) and prostacyclin (PG-I2). However, it was recently suggested that a rapid cGMP/cGMP-dependent protein kinase (cGK)–mediated extracellular signal-related kinase (ERK) phosphorylation promotes platelet activation. This hypothesis was examined here by evaluating established and proposed cGK activators/inhibitors with respect to their capacity to promote either platelet activation or inhibition. In particular, the regulatory role of cGK for ERK phosphorylation and thrombin-, thromboxane-, and VWF-induced platelet activation was investigated. The data obtained do not support the concept that cGK-mediated ERK phosphorylation promotes platelet activation but confirm the inhibitory role of cGK in platelet function. One explanation for these discrepancies is the novel finding that extracellular cGMP analogs potently and rapidly inhibit thrombin-, thromboxane-, and VWF-induced human platelet signaling and activation by a cGK-independent mechanism.

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Crossref · 10.1182/blood-2003-09-3349

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Metadata

Authors
Gambaryan, S., Geiger, J., Schwarz, U. R., Butt, E., Begonja, A., Obergfell, A., & Walter, U.
Affiliations
  • University of Würzburg (DE)
  • From the Institute of Clinical Biochemistry and Pathobiochemistry, University of Wuerzburg, Germany.
ORCID
Venue
Blood
Publisher
American Society of Hematology
Published
2004-04-01
Volume
103
Issue
7
Pages
2593-2600
ISSN
  • 0006-4971 (ISSN-L)
  • 1528-0020
DOI
10.1182/blood-2003-09-3349
OpenAlex
W2095417890
Cited by
107
References
27
Citations by year
2025: 2 · 2024: 3 · 2023: 1 · 2022: 3 · 2021: 3 · 2020: 2 · 2019: 2 · 2018: 8 · 2017: 5 · 2016: 3 · 2015: 2 · 2014: 3 · 2013: 6 · 2012: 5
FWCI
4.95
Type
journal article
Language
en
Open access
closed
Locations
  • Blood (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Hematology › Platelet Disorders and Treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
Keywords
platelet activation, cGMP-dependent protein kinase, ERK1/2 phosphorylation, thrombin, thromboxane, von Willebrand factor, platelet aggregation inhibition, intracellular signaling, hemostasis, thrombosis
MeSH terms
Blood Platelets, Calcium, Cyclic GMP, Humans, Kinetics, Platelet Aggregation, Platelet Aggregation Inhibitors, von Willebrand Factor, 8-Bromo Cyclic Adenosine Monophosphate, Cyclic GMP-Dependent Protein Kinases, Nitric Oxide Donors, S-Nitroso-N-Acetylpenicillamine

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