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The Human Carbonic Anhydrase II in Platelets: An Underestimated Field of Its Activity
Carbonic anhydrases constitute a group of enzymes that catalyse reversible hydration of carbon dioxide leading to the formation of bicarbonate and proton. The platelet carbonic anhydrase II (CAII) was described for the first time in the '80s of the last century. Nevertheless, its direct role in...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6046183/ https://www.ncbi.nlm.nih.gov/pubmed/30050931 http://dx.doi.org/10.1155/2018/4548353 |
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author | Jakubowski, Maciej Szahidewicz-Krupska, Ewa Doroszko, Adrian |
author_facet | Jakubowski, Maciej Szahidewicz-Krupska, Ewa Doroszko, Adrian |
author_sort | Jakubowski, Maciej |
collection | PubMed |
description | Carbonic anhydrases constitute a group of enzymes that catalyse reversible hydration of carbon dioxide leading to the formation of bicarbonate and proton. The platelet carbonic anhydrase II (CAII) was described for the first time in the '80s of the last century. Nevertheless, its direct role in platelet physiology and pathology still remains poorly understood. The modulation of platelet CAII action as a therapeutic approach holds promise as a novel strategy to reduce the impact of cardiovascular diseases. This short review paper summarises the current knowledge regarding the role of human CAII in regulating platelet function. The potential future directions considering this enzyme as a potential drug target and important pathophysiological chain in platelet-related disorders are described. |
format | Online Article Text |
id | pubmed-6046183 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Hindawi |
record_format | MEDLINE/PubMed |
spelling | pubmed-60461832018-07-26 The Human Carbonic Anhydrase II in Platelets: An Underestimated Field of Its Activity Jakubowski, Maciej Szahidewicz-Krupska, Ewa Doroszko, Adrian Biomed Res Int Review Article Carbonic anhydrases constitute a group of enzymes that catalyse reversible hydration of carbon dioxide leading to the formation of bicarbonate and proton. The platelet carbonic anhydrase II (CAII) was described for the first time in the '80s of the last century. Nevertheless, its direct role in platelet physiology and pathology still remains poorly understood. The modulation of platelet CAII action as a therapeutic approach holds promise as a novel strategy to reduce the impact of cardiovascular diseases. This short review paper summarises the current knowledge regarding the role of human CAII in regulating platelet function. The potential future directions considering this enzyme as a potential drug target and important pathophysiological chain in platelet-related disorders are described. Hindawi 2018-06-28 /pmc/articles/PMC6046183/ /pubmed/30050931 http://dx.doi.org/10.1155/2018/4548353 Text en Copyright © 2018 Maciej Jakubowski et al. https://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Jakubowski, Maciej Szahidewicz-Krupska, Ewa Doroszko, Adrian The Human Carbonic Anhydrase II in Platelets: An Underestimated Field of Its Activity |
title | The Human Carbonic Anhydrase II in Platelets: An Underestimated Field of Its Activity |
title_full | The Human Carbonic Anhydrase II in Platelets: An Underestimated Field of Its Activity |
title_fullStr | The Human Carbonic Anhydrase II in Platelets: An Underestimated Field of Its Activity |
title_full_unstemmed | The Human Carbonic Anhydrase II in Platelets: An Underestimated Field of Its Activity |
title_short | The Human Carbonic Anhydrase II in Platelets: An Underestimated Field of Its Activity |
title_sort | human carbonic anhydrase ii in platelets: an underestimated field of its activity |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6046183/ https://www.ncbi.nlm.nih.gov/pubmed/30050931 http://dx.doi.org/10.1155/2018/4548353 |
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