Platelet HIF-2α promotes thrombogenicity through PAI-1 synthesis and extracellular vesicle release
Identifieur interne : 000585 ( Pmc/Curation ); précédent : 000584; suivant : 000586Platelet HIF-2α promotes thrombogenicity through PAI-1 synthesis and extracellular vesicle release
Auteurs : Susheel N. Chaurasia [Inde] ; Geeta Kushwaha [Inde] ; Paresh P. Kulkarni [Inde] ; Ram L. Mallick [Népal] ; Nazmy A. Latheef [Inde] ; Jai K. Mishra [Inde] ; Debabrata Dash [Inde]Source :
- Haematologica [ 0390-6078 ] ; 2019.
Abstract
Oxygen-compromised environments, such as high altitude, are associated with platelet hyperactivity. Platelets confined within the relatively impervious core of an aggregate/thrombus have restricted access to oxygen, yet they continue to perform energy-intensive procoagulant activities that sustain the thrombus. Studying platelet signaling under hypoxia is, therefore, critical to our understanding of the mechanistic basis of thrombus stability. We report here that hypoxia-inducible factor (HIF)-2α is translated from pre-existing mRNA and stabilized against proteolytic degradation in enucleate platelets exposed to hypoxia. Hypoxic stress, too, stimulates platelets to synthesize plasminogen-activator inhibitor-1 (PAI-1) and shed extracellular vesicles, both of which potentially contribute to the prothrombotic phenotype associated with hypoxia. Stabilization of HIF-α by administering hypoxia-mimetics to mice accelerates thrombus formation in mesenteric arterioles. In agreement, platelets from patients with chronic obstructive pulmonary disease and high altitude residents exhibiting thrombogenic attributes have abundant expression of HIF-2α and PAI- 1. Thus, targeting platelet hypoxia signaling could be an effective anti-thrombotic strategy.
Url:
DOI: 10.3324/haematol.2019.217463
PubMed: 31004026
PubMed Central: 6959171
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<front><div type="abstract" xml:lang="en"><p>Oxygen-compromised environments, such as high altitude, are associated with platelet hyperactivity. Platelets confined within the relatively impervious core of an aggregate/thrombus have restricted access to oxygen, yet they continue to perform energy-intensive procoagulant activities that sustain the thrombus. Studying platelet signaling under hypoxia is, therefore, critical to our understanding of the mechanistic basis of thrombus stability. We report here that hypoxia-inducible factor (HIF)-2α is translated from pre-existing mRNA and stabilized against proteolytic degradation in enucleate platelets exposed to hypoxia. Hypoxic stress, too, stimulates platelets to synthesize plasminogen-activator inhibitor-1 (PAI-1) and shed extracellular vesicles, both of which potentially contribute to the prothrombotic phenotype associated with hypoxia. Stabilization of HIF-α by administering hypoxia-mimetics to mice accelerates thrombus formation in mesenteric arterioles. In agreement, platelets from patients with chronic obstructive pulmonary disease and high altitude residents exhibiting thrombogenic attributes have abundant expression of HIF-2α and PAI- 1. Thus, targeting platelet hypoxia signaling could be an effective anti-thrombotic strategy.</p>
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<pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Haematologica</journal-id>
<journal-id journal-id-type="iso-abbrev">Haematologica</journal-id>
<journal-id journal-id-type="hwp">haematol</journal-id>
<journal-id journal-id-type="publisher-id">Haematologica</journal-id>
<journal-title-group><journal-title>Haematologica</journal-title>
</journal-title-group>
<issn pub-type="ppub">0390-6078</issn>
<issn pub-type="epub">1592-8721</issn>
<publisher><publisher-name>Ferrata Storti Foundation</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">31004026</article-id>
<article-id pub-id-type="pmc">6959171</article-id>
<article-id pub-id-type="doi">10.3324/haematol.2019.217463</article-id>
<article-id pub-id-type="publisher-id">1042482</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Article</subject>
<subj-group subj-group-type="heading"><subject>Platelet Biology & its Disorders</subject>
</subj-group>
</subj-group>
</article-categories>
<title-group><article-title>Platelet HIF-2α promotes thrombogenicity through PAI-1 synthesis and extracellular vesicle release</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Chaurasia</surname>
<given-names>Susheel N.</given-names>
</name>
<xref ref-type="aff" rid="af1-1042482">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kushwaha</surname>
<given-names>Geeta</given-names>
</name>
<xref ref-type="aff" rid="af1-1042482">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kulkarni</surname>
<given-names>Paresh P.</given-names>
</name>
<xref ref-type="aff" rid="af1-1042482">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Mallick</surname>
<given-names>Ram L.</given-names>
</name>
<xref ref-type="aff" rid="af2-1042482">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Latheef</surname>
<given-names>Nazmy A.</given-names>
</name>
<xref ref-type="aff" rid="af3-1042482">3</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Mishra</surname>
<given-names>Jai K.</given-names>
</name>
<xref ref-type="aff" rid="af3-1042482">3</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Dash</surname>
<given-names>Debabrata</given-names>
</name>
<xref ref-type="aff" rid="af1-1042482">1</xref>
<xref ref-type="corresp" rid="c1-1042482"></xref>
</contrib>
</contrib-group>
<aff id="af1-1042482"><label>1</label>
Department of Biochemistry, Institute of Medical Sciences, Banaras Hindu University, Varanasi, India</aff>
<aff id="af2-1042482"><label>2</label>
Department of Biochemistry, Birat Medical College & Teaching Hospital, Biratnagar, Nepal</aff>
<aff id="af3-1042482"><label>3</label>
Department of Tuberculosis & Respiratory Diseases, Institute of Medical Sciences, Banaras Hindu University, Varanasi, India</aff>
<author-notes><corresp id="c1-1042482"><bold>Correspondence:</bold>
<italic>DEBABRATA DASH</italic>
<email>ddash.biochem@gmail.com</email>
</corresp>
</author-notes>
<pub-date pub-type="ppub"><month>12</month>
<year>2019</year>
</pub-date>
<pub-date pub-type="epreprint"><day>19</day>
<month>4</month>
<year>2019</year>
</pub-date>
<volume>104</volume>
<issue>12</issue>
<fpage>2482</fpage>
<lpage>2492</lpage>
<history><date date-type="received"><day>24</day>
<month>1</month>
<year>2019</year>
</date>
<date date-type="accepted"><day>17</day>
<month>4</month>
<year>2019</year>
</date>
</history>
<permissions><copyright-statement>Copyright© 2019 Ferrata Storti Foundation</copyright-statement>
<copyright-year>2019</copyright-year>
<license license-type="open-access"><license-p>Material published in Haematologica is covered by copyright. All rights are reserved to the Ferrata Storti Foundation. Use of published material is allowed under the following terms and conditions:</license-p>
<license-p><ext-link ext-link-type="uri" xlink:href="https://creativecommons.org/licenses/by-nc/4.0/legalcode">https://creativecommons.org/licenses/by-nc/4.0/legalcode</ext-link>
. Copies of published material are allowed for personal or internal use. Sharing published material for non-commercial purposes is subject to the following conditions:</license-p>
<license-p><ext-link ext-link-type="uri" xlink:href="https://creativecommons.org/licenses/by-nc/4.0/legalcode">https://creativecommons.org/licenses/by-nc/4.0/legalcode</ext-link>
, sect. 3. Reproducing and sharing published material for commercial purposes is not allowed without permission in writing from the publisher.</license-p>
</license>
</permissions>
<self-uri content-type="pdf" xlink:type="simple" xlink:href="1042482.pdf"></self-uri>
<abstract><p>Oxygen-compromised environments, such as high altitude, are associated with platelet hyperactivity. Platelets confined within the relatively impervious core of an aggregate/thrombus have restricted access to oxygen, yet they continue to perform energy-intensive procoagulant activities that sustain the thrombus. Studying platelet signaling under hypoxia is, therefore, critical to our understanding of the mechanistic basis of thrombus stability. We report here that hypoxia-inducible factor (HIF)-2α is translated from pre-existing mRNA and stabilized against proteolytic degradation in enucleate platelets exposed to hypoxia. Hypoxic stress, too, stimulates platelets to synthesize plasminogen-activator inhibitor-1 (PAI-1) and shed extracellular vesicles, both of which potentially contribute to the prothrombotic phenotype associated with hypoxia. Stabilization of HIF-α by administering hypoxia-mimetics to mice accelerates thrombus formation in mesenteric arterioles. In agreement, platelets from patients with chronic obstructive pulmonary disease and high altitude residents exhibiting thrombogenic attributes have abundant expression of HIF-2α and PAI- 1. Thus, targeting platelet hypoxia signaling could be an effective anti-thrombotic strategy.</p>
</abstract>
</article-meta>
</front>
</pmc>
</record>
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