Tulsi Patil¹*, Chirag Patel², Arun Soni³ and Sanjeev Acharya³

¹Research Scholar, SSR College of Pharmacy, UT of Dadra and Nagar Haveli, India
²L. M. College of Pharmacy, Ahmedabad, India
³SSR College of Pharmacy, UT of Dadra and Nagar Haveli, India

*Corresponding Author: Tulsi Patil, Research Scholar, SSR College of Pharmacy, UT of Dadra and Nagar Haveli, India.

Received: April 28, 2021; Published: May 24, 2021

Abstract

This review article aims to point out the many roles of HIF-1α in COVID-19 diseases. World health organization named the newly emerged virus SARS-CoV-2 or 2019-nCoV or covid-19. At beginning of coronavirus symptoms of pneumonia were appeared in December 2019 near Wuhan city of China. The Coronavirus Disease 2019 outbreak spread rapidly worldwide and is associated with the high death rate in humans. However, there are currently fewer safe and effective drugs available for targeting SARS-CoV-2. So, there is an emergency for the invention of effective prevention and treatment options for the SARS-CoV-2 outbreak. SARS-CoV-2 recognizes the human ACE2 more strongly than SARS-CoV. SARS-CoV-2 spike supermolecule having a very high robust binding affinity to human ACE2. Relatively limited information is understood about the transcriptional regulation of ACE2. Hypoxic condition reduces the synthesis of ACE2, Further experimentation has shown that hypoxic condition induced HIF-1α protein leads to increases ACE synthesis which, prompts to rise the amount of Ang II and overall this process modulates the reduction in ACE2 synthesis with the help of Ang II. Activation of HIF-1 is related to numerous physiological and pathological processes. HIF-1 will manage ACE2 regulation and several natural components exhibit the role in activation and stabilization of the HIF-1α protein. The level of HIF-1α in cells gives us future opportunities for new, safe, and effective treatment options for the novel coronavirus.

Keywords:COVID-19; SARS-COV; HIF-1α Pathway; Influenza A Virus; Natural HIF-1α Activators

References

1. Petersen E., et al. “Comparing SARS-CoV-2 with SARS-CoV and influenza pandemics”. Lancet Infectious Disease9 (2020): 238-244.
2. Semenza GL. “Expression of hypoxia-inducible factor 1: mechanisms and consequences”. Biochemical Pharmacology 1 (2000): 47-53.
3. Rezaei M., et al. “ACE2: Its potential role and regulation in severe acute respiratory syndrome and COVID-19”. Journal of Cell Physiology4 (2020): 2430-2442.
4. Zhang R., et al. “Role of HIF-1α in the regulation ACE and ACE2 expression in hypoxic human pulmonary artery smooth muscle cells”. American Journal of Physiology - Lung Cellular and Molecular Physiology4 (2009): L631-640.
5. Reyes A., et al. “Contribution of hypoxia inducible factor-1 during viral infections”. Virulence 1 (2020): 1482-1500.
6. Lee JW., et al. “Hypoxia signaling in human diseases and therapeutic targets”. Experimental and Molecular Medicine 6 (2019): 1-13.
7. Zhou Y., et al. “Network-based drug repurposing for novel coronavirus 2019-nCoV/SARS-CoV-2”. Cell Discovery 1 (2020): 1-18.
8. Nagle DG and Zhou Y-D. “Natural product-derived small molecule activators of hypoxia-inducible factor-1 (HIF-1)”. Current Pharmaceutical Design 21 (2006): 2673-2688.
9. Wang GL and Semenza GL. “Desferrioxamine induces erythropoietin gene expression and hypoxia-inducible factor 1 DNA-binding activity: implications for models of hypoxia signal transduction”. Blood 12 (1993): 3610-3615.
10. Linden T., et al. “The antimycotic ciclopirox olamine induces HIF-1α stability, VEGF expression, and angiogenesis”. FASEB Journal6 (2003): 761-763.
11. Cunliffe CJ., et al. “Novel inhibitors of prolyl 4-hydroxylase. 3. Inhibition by the substrate analog N-oxaloglycine and its derivatives”. Journal of Medicinal Chemistry 14 (1992): 2652-2658.
12. HIGASHIDE E., et al. “Isolation of dealanylalahopcin, a new amino acid, and its biological activity”. Journal of Antibiotics (Tokyo). 38.3 (1985): 296-301.
13. Schlemminger I., et al. “Analogues of dealanylalahopcin are inhibitors of human HIF prolyl hydroxylases”. Bioorganic and Medicinal Chemistry Letters 8 (2003): 1451-1454.
14. Leclerc S., et al. “Indirubins inhibit glycogen synthase kinase-3β and CDK5/P25, two protein kinases involved in abnormal tau phosphorylation in Alzheimer’s disease: a property common to most cyclin-dependent kinase inhibitors?”. Journal of Biological Chemistry1 (2001): 251-260.
15. Sogawa K., et al. “Inhibition of hypoxia-inducible factor 1 activity by nitric oxide donors in hypoxia”. Proceedings of the National Academy of Sciences of the United States of America 13 (1998): 7368-7373.
16. Jung Y-J., et al. “Microtubule disruption utilizes an NFκB-dependent pathway to stabilize HIF-1α protein”. Journal of Biological Chemistry9 (2003): 7445-7452.
17. Mabjeesh NJ., et al. “Dibenzoylmethane, a natural dietary compound, induces HIF-1α and increases expression of VEGF”. Biochemical and Biophysical Research Communications1 (2003): 279-286.
18. Wilson WJ and Poellinger L. “The dietary flavonoid quercetin modulates HIF-1α activity in endothelial cells”. Biochemical and Biophysical Research Communications1 (2002): 446-450.
19. Mandel S., et al. “Cell signaling pathways in the neuroprotective actions of the green tea polyphenol (-)-epigallocatechin-3-gallate: implications for neurodegenerative diseases”. Journal of Neurochemistry6 (2004): 1555-1569.
20. Aneja R., et al. “Epigallocatechin, a green tea polyphenol, attenuates myocardial ischemia reperfusion injury in rats”. Molecular Medicine1 (2004): 55-62.

Citation

Citation: Tulsi Patil.,et al. “Role of HIF 1 α in Covid-19 Disease".Acta Scientific Nutritional Health 5.6 (2021): 60-64.

Copyright

Copyright: © 2021 Tulsi Patil., et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.