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COVID-19 and erythrocrine function: The roller coaster and danger
Erythrocrine function refers to erythrocytes’ ability to synthesize and release active signaling molecules such as ATP and nitric oxide (NO). Erythrocyte NO regulates its deformability and increases its perfusion and circulation that prevent tissue hypoxia. Recently, there is a connotation between S...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
SAGE Publications
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9124636/ https://www.ncbi.nlm.nih.gov/pubmed/35590466 http://dx.doi.org/10.1177/03946320221103151 |
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author | Al-kuraishy, Hayder M Al-Gareeb, Ali I Onohuean, Hope El-Saber Batiha, Gaber |
author_facet | Al-kuraishy, Hayder M Al-Gareeb, Ali I Onohuean, Hope El-Saber Batiha, Gaber |
author_sort | Al-kuraishy, Hayder M |
collection | PubMed |
description | Erythrocrine function refers to erythrocytes’ ability to synthesize and release active signaling molecules such as ATP and nitric oxide (NO). Erythrocyte NO regulates its deformability and increases its perfusion and circulation that prevent tissue hypoxia. Recently, there is a connotation between SARS-CoV-2 infection and erythrocrine function due to alteration in the release of NO and ATP from erythrocytes. SARS-CoV-2 binds erythrocyte band3 protein, which has a similar characteristic of ACE2, leading to alteration of erythrocyte physiology like oxygen transport with development of hypoxia. Similarly, SARS-CoV-2 infection activates erythrocyte protein kinase C alpha (PKC-α), causing significant changes in the erythrocyte functions. The erythrocytes can bind SARS-CoV-2 and its active particles with subsequent virus delivery to the liver and spleen macrophages. Thus, the erythrocytes act as elimination for SARS-CoV-2 in COVID-19. Moreover, the erythrocyte stored, release sphingosine-1 phosphate (S1P) improves endothelial and regulates lymphocyte functions. SARS-CoV-2 ORF8 protein binds the porphyrin part of hemoglobin heme at the β1 chain, causing hemolysis and dysfunctional hemoglobin to reduce oxygen-carrying capacity. In conclusion, SARS-CoV-2 infection and associated pro-inflammatory disorders lead to abnormal erythrocrine function with subsequent inflammatory complications and endothelial dysfunction due to deficiency of protective released molecules (NO, G1P, and ATP) from functional erythrocytes. In vitro, preclinical, and clinical studies are mandatory in this regard. |
format | Online Article Text |
id | pubmed-9124636 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | SAGE Publications |
record_format | MEDLINE/PubMed |
spelling | pubmed-91246362022-05-24 COVID-19 and erythrocrine function: The roller coaster and danger Al-kuraishy, Hayder M Al-Gareeb, Ali I Onohuean, Hope El-Saber Batiha, Gaber Int J Immunopathol Pharmacol Inflammatory Mediators in COVID-19 and Other Diseases-Original Research Article Erythrocrine function refers to erythrocytes’ ability to synthesize and release active signaling molecules such as ATP and nitric oxide (NO). Erythrocyte NO regulates its deformability and increases its perfusion and circulation that prevent tissue hypoxia. Recently, there is a connotation between SARS-CoV-2 infection and erythrocrine function due to alteration in the release of NO and ATP from erythrocytes. SARS-CoV-2 binds erythrocyte band3 protein, which has a similar characteristic of ACE2, leading to alteration of erythrocyte physiology like oxygen transport with development of hypoxia. Similarly, SARS-CoV-2 infection activates erythrocyte protein kinase C alpha (PKC-α), causing significant changes in the erythrocyte functions. The erythrocytes can bind SARS-CoV-2 and its active particles with subsequent virus delivery to the liver and spleen macrophages. Thus, the erythrocytes act as elimination for SARS-CoV-2 in COVID-19. Moreover, the erythrocyte stored, release sphingosine-1 phosphate (S1P) improves endothelial and regulates lymphocyte functions. SARS-CoV-2 ORF8 protein binds the porphyrin part of hemoglobin heme at the β1 chain, causing hemolysis and dysfunctional hemoglobin to reduce oxygen-carrying capacity. In conclusion, SARS-CoV-2 infection and associated pro-inflammatory disorders lead to abnormal erythrocrine function with subsequent inflammatory complications and endothelial dysfunction due to deficiency of protective released molecules (NO, G1P, and ATP) from functional erythrocytes. In vitro, preclinical, and clinical studies are mandatory in this regard. SAGE Publications 2022-05-19 /pmc/articles/PMC9124636/ /pubmed/35590466 http://dx.doi.org/10.1177/03946320221103151 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by-nc/4.0/This article is distributed under the terms of the Creative Commons Attribution-NonCommercial 4.0 License (https://creativecommons.org/licenses/by-nc/4.0/) which permits non-commercial use, reproduction and distribution of the work without further permission provided the original work is attributed as specified on the SAGE and Open Access pages (https://us.sagepub.com/en-us/nam/open-access-at-sage). |
spellingShingle | Inflammatory Mediators in COVID-19 and Other Diseases-Original Research Article Al-kuraishy, Hayder M Al-Gareeb, Ali I Onohuean, Hope El-Saber Batiha, Gaber COVID-19 and erythrocrine function: The roller coaster and danger |
title | COVID-19 and erythrocrine function: The roller coaster and
danger |
title_full | COVID-19 and erythrocrine function: The roller coaster and
danger |
title_fullStr | COVID-19 and erythrocrine function: The roller coaster and
danger |
title_full_unstemmed | COVID-19 and erythrocrine function: The roller coaster and
danger |
title_short | COVID-19 and erythrocrine function: The roller coaster and
danger |
title_sort | covid-19 and erythrocrine function: the roller coaster and
danger |
topic | Inflammatory Mediators in COVID-19 and Other Diseases-Original Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9124636/ https://www.ncbi.nlm.nih.gov/pubmed/35590466 http://dx.doi.org/10.1177/03946320221103151 |
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