Does Oxidative Stress Promote The Effect of The Paraoxonase Enzyme Family (PON) On Cancer? A Review Study to Clarify This Relationship by PONs

Year 2022, Volume: 12 Issue: 4, 756 - 765, 28.12.2022

Tugba Kevser Uysal , Muhammet Örnek , Özen Özensoy Güler

https://doi.org/10.31832/smj.1199508

Abstract

Cancer development and progression are associated with oxidative stress. Oxidative stress can favor high concentrations of reactive oxygen species (ROS), and free radicals are associated with antioxidant metabolism. The human enzyme paraoxonase (PON) contributes to antioxidant metabolism and decreased antioxidant levels. This leads to a high-risk factor for coronary heart disease. This review focuses on specific changes that affect the DNA molecule, and signaling pathways, and regulate the various cancers through the attraction of PON, an enzyme for degrading lipid peroxides within the cell as well as lipoproteins in the bloodstream.

Keywords

PON, cancer, antioxidant, oxidative stress, hypoxia

Oksidatif Stres Paraoksonaz Enzim Ailesinin (PON) Kanser Üzerindeki Etkisini Arttırır mı? PON Ailesinin Oksidatif Stres ve Kanser İlişkisinin İncelenmesini Amaçlayan Bir Derleme

Abstract

Kanser gelişimi ve ilerlemesi oksidatif stres ile ilişkilidir. Yüksek seviyelerde reaktif oksijen türleri (ROS) ve serbest radikaller, fizyolojik bir durum olan oksidatif strese neden olmaktadır. Oksidatif strese karşı geliştirilen antioksidan metabolizması çok önemlidir. Antioksidan seviyelerindeki azalma, koroner kalp hastalıklarının risk faktörleri arasında sayılabilir. Paraoksonaz enzimi (PON), kan dolaşımındaki lipoproteinlerin yanı sıra hücre içindeki lipid peroksitlerini de parçalayarak antioksidan metabolizmanın devreye girmesine sebep olmakta ve düşük seviylerdeki antioksidanlar koroner kalp hastalığinda etkili bir risk faktörü haline gelebilmektedir. Bu derleme, önemli bir antioksidan enzim olan PON’un; DNA hasarı, çeşitli kanser türlerinin progresyonu ve sinyal yolaklarındaki değişiklikler ve lipoproteinler ile ilişkisi üzerindeki rollerine odaklanmaktadır.

Keywords

PON, kanser, antioksidan, oksidatif stres, hipoksi

References

• 1. Shakunthala N. New cytochrome P450 mechanisms: implications of understanding the molecular basis for drug toxicity at the level of the cytochrome. Expert opinion on drug metabolism & toxicology 2010; 6(1): 1-15.
• 2. Bacchetti T, Ferretti G, Sahebkar A. The role of paraoxonase in cancer. Seminars in Cancer Biology; 2019: Elsevier; 2019. p. 72-86.
• 3. Reichert CO, Levy D, Bydlowski SP. Paraoxonase Role in Human Neurodegenerative Diseases. Antioxidants 2021; 10(1): 11.
• 4. Reddy ST, Wadleigh DJ, Grijalva V, Ng C, Hama S, Gangopadhyay A, et al. Human paraoxonase-3 is an HDL-associated enzyme with biological activity similar to paraoxonase-1 protein but is not regulated by oxidized lipids. Arteriosclerosis, thrombosis, and vascular biology 2001; 21(4): 542-7.
• 5. Ng CJ, Shih DM, Hama SY, Villa N, Navab M, Reddy ST. The paraoxonase gene family and atherosclerosis. Free Radical Biology and Medicine 2005; 38(2): 153-63.
• 6. Demirel T, Yaylim I, Ergen HA, Gunay MK, Tekant Y, Isbir T. Association of paraoxonase (PON1) polymorphisms and activity with colorectal cancer predisposition. Biotechnology Biotechnological Equipment 2021; 35(1): 232-8.
• 7. Mackness B, Mackness M. Anti-inflammatory properties of paraoxonase-1 in atherosclerosis. Paraoxonases in Inflammation, Infection, and Toxicology: Springer; 2010: 143-51.
• 8. Rosenblat M, Gaidukov L, Khersonsky O, Vaya J, Oren R, Tawfik DS, et al. The catalytic histidine dyad of high-density lipoprotein-associated serum paraoxonase-1 (PON1) is essential for PON1-mediated inhibition of low-density lipoprotein oxidation and stimulation of macrophage cholesterol efflux. Journal of Biological Chemistry 2006; 281(11): 7657-65.
• 9. Manco G, Porzio E, Carusone TM. Human Paraoxonase-2 (PON2): Protein Functions and Modulation. Antioxidants (Basel) 2021; 10(2).
• 10. Grdic Rajkovic M, Rumora L, Barisic K. The paraoxonase 1, 2 and 3 in humans. Biochemia medica: Biochemia medica 2011; 21(2): 122-30.
• 11. Furlong CE, Marsillach J, Jarvik GP, Costa LG. Paraoxonases-1,-2 and-3: what are their functions? Chemical-biological interactions 2016; 259: 51-62.
• 12. Milani P, Ambrosi G, Gammoh O, Blandini F, Cereda C. SOD1 and DJ-1 converge at Nrf2 pathway: a clue for antioxidant therapeutic potential in neurodegeneration. Oxidative medicine and cellular longevity 2013; 2013.
• 13. Saeidnia S, Abdollahi M. Toxicological and pharmacological concerns on oxidative stress and related diseases. Toxicology and applied pharmacology 2013; 273(3): 442-55.
• 14. Bozan N, Demir H, Gürsoy T, Özkan H, Düzenli U, Sarıkaya E, et al. Alterations in oxidative stress markers in laryngeal carcinoma patients. Journal of the Chinese Medical Association 2018; 81(9): 811-5.
• 15. Shokri Y, Variji A, Nosrati M, Khonakdar-Tarsi A, Kianmehr A, Kashi Z, et al. Importance of paraoxonase 1 (PON1) as an antioxidant and antiatherogenic enzyme in the cardiovascular complications of type 2 diabetes: Genotypic and phenotypic evaluation. Diabetes research clinical practice 2020; 161: 108067.
• 16. Camps J, Marsillach J, Joven J. The paraoxonases: role in human diseases and methodological difficulties in measurement. Critical reviews in clinical laboratory sciences 2009; 46(2): 83-106.
• 17. Khersonsky O, Tawfik DS. Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase. Biochemistry 2005; 44(16): 6371-82.
• 18. Ponce-Ruiz N, Murillo-González F, Rojas-García A, Mackness M, Bernal-Hernández Y, Barrón-Vivanco B, et al. Transcriptional regulation of human paraoxonase 1 by nuclear receptors. Chemical-biological interactions 2017; 268: 77-84.
• 19. Mackness M, Mackness B. Human paraoxonase-1 (PON1): Gene structure and expression, promiscuous activities and multiple physiological roles. Gene 2015; 567(1): 12-21.
• 20. Arenas M, Rodríguez E, Sahebkar A, Sabater S, Rizo D, Pallisé O, et al. Paraoxonase-1 activity in patients with cancer: A systematic review and meta-analysis. Critical reviews in oncology/hematology 2018; 127: 6-14.
• 21. Medina-Díaz IM, Ponce-Ruíz N, Rojas-García AE, Zambrano-Zargoza JF, Bernal-Hernández YY, González-Arias CA, et al. The Relationship between Cancer and Paraoxonase 1. Antioxidants 2022; 11(4): 697.
• 22. Huang C, Wang Y, Liu S, Ding G, Liu W, Zhou J, et al. Quantitative proteomic analysis identified paraoxonase 1 as a novel serum biomarker for microvascular invasion in hepatocellular carcinoma. Journal of proteome research 2013; 12(4): 1838-46.
• 23. Kowalska K, Socha E, Milnerowicz H. The role of paraoxonase in cardiovascular diseases. Annals of Clinical & Laboratory Science 2015; 45(2): 226-33.
• 24. Zhu L, Shen Y, Sun W. Paraoxonase 3 promotes cell proliferation and metastasis by PI3K/Akt in oral squamous cell carcinoma. Biomedicine & Pharmacotherapy 2017; 85: 712-7.
• 25. Mackness M, Sozmen EY. A critical review on human serum Paraoxonase-1 in the literature: truths and misconceptions. Turkish Journal of Biochemistry 2021; 46(1): 3-8.
• 26. Gilad D, Atiya S, Mozes-Autmazgin Z, Ben-Shushan RS, Ben-David R, Amram E, et al. Paraoxonase 1 in endothelial cells impairs vasodilation induced by arachidonic acid lactone metabolite. Biochimica et Biophysica Acta (BBA)-Molecular and Cell Biology of Lipids 2019; 1864(3): 386-93.
• 27. Kaya MO, Sinan S, Güler ÖÖ, Arslan O. Is there a relationship between genetic susceptibility with cancer? A study about paraoxonase (PON1) enzyme activity in breast cancer cases. Journal of Enzyme Inhibition and Medicinal Chemistry 2016; 31(6): 1349-55.
• 28. Mutlu M, Korkmaz MH, Simsek E, Terzi E, Oz Bedir BE, Uysal TK, et al. Do CO2 and oxidative stress induce cancer?: a brief study about the evaluation of PON 1, CAT, CA and XO enzyme levels on head and neck cancer patients. Journal of Enzyme Inhibition and Medicinal Chemistry 2019; 34(1): 459-64.
• 29. Mittal M, Siddiqui MR, Tran K, Reddy SP, Malik AB. Reactive oxygen species in inflammation and tissue injury. Antioxidants & redox signaling 2014; 20(7): 1126-67.
• 30. Franco R, Panayiotidis MI, Cidlowski JA. Glutathione depletion is necessary for apoptosis in lymphoid cells independent of reactive oxygen species formation. Journal of biological chemistry 2007; 282(42): 30452-65.
• 31. Aronis A, Melendez JAs, Golan O, Shilo S, Dicter N, Tirosh O. Potentiation of Fas-mediated apoptosis by attenuated production of mitochondria-derived reactive oxygen species. Cell Death & Differentiation 2003; 10(3): 335-44.
• 32. Reuter S, Gupta SC, Chaturvedi MM, Aggarwal BB. Oxidative stress, inflammation, and cancer: how are they linked? Free radical biology medicine 2010; 49(11): 1603-16.
• 33. Ozensoy O, Kockar F, Arslan O, Isik S, Supuran CT, Lyon M. An evaluation of cytosolic erythrocyte carbonic anhydrase and catalase in carcinoma patients: An elevation of carbonic anhydrase activity. Clinical biochemistry 2006; 39(8): 804-9.
• 34. Litvinov D, Mahini H, Garelnabi M. Antioxidant and anti-inflammatory role of paraoxonase 1: implication in arteriosclerosis diseases. North American journal of medical sciences 2012; 4(11): 523.