Theoretical and Natural Science
- The Open Access Proceedings Series for Conferences
Theoretical and Natural Science
Vol. 33, 08 March 2024
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Biochemical characterization of the NTPDases family and thrombosis
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Abstract
This paper provides insight into the key role of the Nucleoside Triphosphate Diphosphohydrolase (NTPDase) family in thrombosis and its therapeutic potential. Thrombosis is an important mechanism to prevent bleeding, but its abnormal formation can lead to serious health problems such as myocardial infarction and stroke. This paper employs the method of literature analysis, obtaining materials through the investigation of previous literature, thereby conducting a literature review on the biochemical characteristics of some members of the NTPDase family. This paper begins with a description of the basic mechanisms of thrombosis and the biochemical characterization of the NTPDase family, including the structure, function, and specific substrate specificity of its members. The NTPDase enzymes regulate platelet activation by hydrolyzing extracellular Adenosine Triphosphate (ATP) and Adenosine Diphosphate (ADP), thereby preventing excessive thrombosis. The article describes in detail the catalytic roles of the NTPDase family members, their relationship to platelets and thrombosis, and discusses their role in regulating platelet function and blood coagulation. Finally, the article identifies NTPDase family members as promising targets for the treatment of thrombosis and explores the possibility of utilizing these enzymes in the clinical prevention and treatment of thrombosis-related diseases, highlighting their therapeutic potential in the control of inflammatory vascular diseases.
Keywords
NTPDases, thrombosis, P2 receptors
References
1. Atkinson, B., et al. (2006). “Ecto-nucleotidases of the CD39/NTPDase family modulate platelet activation and thrombus formation: potential as therapeutic targets.” Blood Cells Mol Dis 36(2): 217-222.
2. Sévigny, J., et al. (2002). “Differential catalytic properties and vascular topography of murine nucleoside triphosphate diphosphohydrolase 1 (NTPDase1) and NTPDase2 have implications for thromboregulation.” Blood 99(8): 2801-2809.
3. Kuku lski, F., et al. (2005). “Comparative hydrolysis of P2 receptor agonists by NTPDases 1, 2, 3 and 8.” Purinergic Signal 1(2): 193-204.
4. Robson, S. C., et al. (2006). “The E-NTPDase family of ectonucleotidases: Structure function relationships and pathophysiological significance.” Purinergic Signal 2(2): 409- 430.
5. Zimmermann, H., et al. (2012). “Cellular function and molecular structure of ecto-nucleotidases.” Purinergic Signal 8(3): 437-502.
6. Weisman GA, Erb L, Garrad RC et al (1998) P2Y nucleotide receptors in the immune system: signaling by a P2Y2 receptor in U937 monocytes. Drug Dev Res 45:222 -228.
7. North RA. Molecular physiology of P2X receptors. Phy siol Rev 2002; 82: 1013-7.
Data Availability
The datasets used and/or analyzed during the current study will be available from the authors upon reasonable request.
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- Volume Title
- Proceedings of the 2nd International Conference on Modern Medicine and Global Health
- ISBN (Print)
- 978-1-83558-323-4
- ISBN (Online)
- 978-1-83558-324-1
- Published Date
- 08 March 2024
- Series
- Theoretical and Natural Science
- ISSN (Print)
- 2753-8818
- ISSN (Online)
- 2753-8826
- DOI
- 10.54254/2753-8818/33/20240957
- Copyright
- © 2023 The Author(s)
- Open Access
- This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited