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Research Article

Influence of chitotriosidase gene polymorphisms on oxidative stress and susceptibility to Aspergillus infection among exposed workers

ORCID Icon, , , &
Pages 1195-1204 | Received 25 Mar 2022, Accepted 17 May 2022, Published online: 26 May 2022

References

  • Boot RG, Renkema GH, Verhoek M, Strijland A, Bliek J, De Meulemeester TM, Mannens MM, Aerts JM. 1998. The human chitotriosidase gene - nature of inherited enzyme deficiency. J Biol Chem. 273(40):25680–25685. doi:10.1074/jbc.273.40.25680.
  • Boot RG, Blommaart EFC, Swart E, Ghauharali-van der Vlugt K, Bijl N, Moe C, Place A, Aerts JM. 2001. Identification of a novel acidic mammalian chitinase distinct from chitotriosidase. J Biol Chem. 276(9):6770–6778. doi:10.1074/jbc.M009886200.
  • Boot RG, Bussink AP, Verhoek M, De Boer PAJ, Moorman AFM, Aerts JM. 2005. Marked differences in tissue-specific expression of chitinases in mouse and man. J Histochem Cytochem. 53(10):1283–1292. doi:10.1369/jhc.4A6547.2005.
  • Caramori G, Papi A. 2004. Oxidants and asthma. Thorax. 59(2):170–173. doi:10.1136/thorax.2002.002477.
  • Cemek M, Çaksen H, Bayiroğlu F, Cemek F, Dede S. 2006. Oxidative stress and enzymic–non‐enzymic antioxidant responses in children with acute pneumonia. Cell Biochem Funct. 24:269–273.
  • Chang D, Sharma L, Dela Cruz CS. 2020. Chitotriosidase: a marker and modulator of lung disease. Eur Respir Rev. 29(156):1–12. doi:10.1183/16000617.0143-2019.
  • Elias JA, Homer RJ, Hamid Q, Chun GL. 2005. Chitinases and chitinase-like proteins in TH2 inflammation and asthma. J Allergy Clin Immunol. 116(3):497–500. doi:10.1016/j.jaci.2005.06.028.
  • Ergueder IB, Ucar A, Aritürk I, Ergueder T, Avci A, Hasipek S, Sunguroğlu K. 2009. The effects of cigarette smoking on serum oxidant status, and cholesterol, homocysteine, folic acid, copper, and zinc levels in university students. Turkish J Med Sci. 39:513–517.
  • Fadel F, Zhao Y, Cousido-Siah A, Ruiz FX, Mitschler A, Podjarny A. 2016. X-Ray crystal structure of the full length human chitotriosidase (CHIT1) reveals features of its chitin binding domain. PLoS One. 11(4):1–15. doi:10.1371/journal.pone.0154190.
  • Fusetti F, Von Moeller H, Houston D, Rozeboom HJ, Dijkstra BW, Boot RG, Aerts JM, Van Aalten DM. 2002. Structure of human chitotriosidase: Implications for specific inhibitor design and function of mammalian chitinase-like lectins. J Biol Chem. 277(28):25537–25544. doi:10.1074/jbc.M201636200.
  • Ghiselli A, Serafini M, Natella F, Scaccini C. 2000. Total antioxidant capacity as a tool to assess redox status: Critical view and experimental data. Free Radic Biol Med. 29(11):1106–1114. doi:10.1016/S0891-5849(00)00394-4.
  • Han Y, Li L, Wang Y, Ma J, Li P, Han C, Liu J. 2020. Composition, dispersion, and health risks of bioaerosols in wastewater treatment plants: a review. Front Environ Sci Eng. 15(3):1–16. doi:10.1007/s11783-020-1330-1.
  • Hector A, Chotirmall SH, Lavelle GM, Mirković B, Horan D, Eichler L, Mezger M, Singh A, Ralhan A, Berenbrinker S et al. 2016. Chitinase activation in patients with fungus-associated cystic fibrosis lung disease. J Allergy Clin Immunol. 138(4):1183–1189.e4. doi:10.1016/j.jaci.2016.01.031.
  • Jackson LW, Schisterman EF, Dey-Rao R, Browne R, Armstrong D. 2005. Oxidative stress and endometriosis. Hum Reprod. 20(7):2014–2020. doi:10.1093/humrep/dei001.
  • Koracevic D, Koracevic G, Djordjevic V, Andrejevic S, Cosic V. 2001. Method for the measurement of antioxidant activity in human fluids. J Clin Pathol. 54(5):356–361. doi:10.1136/jcp.54.5.356.
  • Lee P, Waalen J, Crain K, Smargon A, Beutler E. 2007. Human chitotriosidase polymorphisms G354R and A442V associated with reduced enzyme activity. Blood Cells Mol Dis. 39(3):353–360. doi:10.1016/j.bcmd.2007.06.013.
  • Lee CG, Da Silva CA, Lee JY, Hartl D, Elias JA. 2008. Chitin regulation of immune responses: an old molecule with new roles. Curr Opin Immunol. 20(6):684–689. doi:10.1016/j.coi.2008.10.002.
  • Lee CG, Da Silva CA, Dela Cruz CS, Ahangari F, Ma B, Kang MJ, He CH, Takyar S, Elias JA. 2011. Role of chitin and chitinase/chitinase-like proteins in inflammation, tissue remodeling, and injury. Annu Rev Physiol. 73(1):479–501. doi:10.1146/annurev-physiol-012110-142250.
  • Lionakis MS, Levitz SM. 2018. Host control of fungal infections: lessons from basic studies and human cohorts. Annu Rev Immunol. 36(1):157–191. doi:10.1146/annurev-immunol-042617-053318.
  • Livnat G, Bar-Yoseph R, Mory A, Dagan E, Elias N, Gershoni R, Bentur L. 2014. Duplication in CHIT1 gene and the risk for aspergillus lung disease in CF patients. Pediatr Pulmonol. 49(1):21–27. doi:10.1002/ppul.22749.
  • Malaguarnera L. 2006. Chitotriosidase: the yin and yang. Cell Mol Life Sci. 63(24):3018–3029. doi:10.1007/s00018-006-6269-2.
  • Manafa PO, Okafor CC, Okeke CO, Chukwuma GO, Ibeh NC, Ogenyi SI, Nwene EK, Aneke JC. 2017. Assessment of superoxide dismutase activity and total antioxidant capacity in adult male cigarette smokers in Nnewi metropolis, Nigeria. J Med Res. 3(1):23–26. doi:10.31254/jmr.2017.3109.
  • Naik B, Ahmed SM, Laha S, Dos SP. 2021. Genetic susceptibility to fungal infections and links to human ancestry. Front Genet. 1417. doi:10.3389/fgene.2021.709315.
  • Odebode A, Adekunle A. 2019. Biomarkers of oxidative stress as indicators of fungi environmental pollution in Balb/c albino mice monitored from South West, Nigeria. J Pathog. 2019:1–9. doi:10.1155/2019/6561520.
  • Rahman I, Adcock IM. 2006. Oxidative stress and redox regulation of lung inflammation in COPD. Eur Respir J. 28(1):219–242. doi:10.1183/09031936.06.00053805.
  • Reese TA, Liang HE, Tager AM, Luster AD, Van Rooijen N, Voehringer D, Locksley RM. 2007. Chitin induces accumulation in tissue of innate immune cells associated with allergy. Nature. 447(7140):92–96. doi:10.1038/nature05746.
  • Renkema GH, Boot RG, Au FL, Donker-Koopman WE, Strijland A, Muijsers AO, Hrebicek M, Aerts JM. 1998. Chitotriosidase a chitinase, and the 39-kDa human cartilage glycoprotein, a chitin-binding lectin, are homologues of family 18 glycosyl hydrolases secreted by human macrophages. Eur J Biochem. 251(1–2):504–509. doi:10.1046/j.1432-1327.1998.2510504.x.
  • Rodrigues MR, Sá Miranda MC, Amaral O. 2004. Allelic frequency determination of the 24-bp chitotriosidase duplication in the Portuguese population by real-time PCR. Blood Cells Mol Dis. 33(3):362–364. doi:10.1016/j.bcmd.2004.07.005.
  • Saad-Hussein A, Soliman MK, Moubarz G. 2022. 18S rRNA gene sequencing for environmental aflatoxigenic fungi and risk of hepatic carcinoma among exposed workers. J Environ Sci Heal a. 1–9. doi:10.1080/10934529.2022.2046428.
  • Shawky MM, Moubarz G, Saad-Hussien A, Shousha WG, Shawki S. 2022. Assessment of workers exposure to Aspergillus in waste water treatment plant. Egypt J of Chem. doi:10.21608/ejchem.2022.101284.4715.
  • Shukla SD, Vanka KS, Chevalier A, Chong WC, Pabreja K, Shastri MD, O’-Toole RF. 2020. Infection-Induced oxidative stress in chronic respiratory diseases. Role Oxidative Stress Pathophysiol Dis. 125–147. doi:10.1007/978-981-15-1568-2_8.
  • Tachu B, Pillai S, Lucius R, Pogonka T. 2008. Essential role of chitinase in the development of the filarial nematode acanthocheilonema viteae. Infect Immun. 76(1):221–228. doi:10.1128/IAI.00701-07.
  • Van Dyken SJ, Liang HE, Naikawadi RP, Woodruff PG, Wolters PJ, Erle DJ, Locksley RM. 2017. Spontaneous chitin accumulation in airways and age-related fibrotic lung disease. Cell. 169(3):497–509.e13. doi:10.1016/j.cell.2017.03.044.
  • Vega K, Kalkum M. 2012. Chitin, chitinase responses, and invasive fungal infections. Int J Microbiol. 2012:1–10. doi:10.1155/2012/920459.
  • Wiesner DL, Specht CA, Lee CK, Smith KD, Mukaremera L, Lee ST, Lee CG, Elias JA, Nielsen JN, Boulware DR et al. 2015. Chitin recognition via chitotriosidase promotes pathologic type-2 helper T cell responses to cryptococcal infection. PLoS Pathog. 11(3):1–28. doi:10.1371/journal.ppat.1004701.
  • Yagi K. 1982. Assay for serum lipid peroxide level and its clinical significance. Lipid Peroxides Biol Med. 223:242–249.
  • Yu BP. 1994. Cellular defenses against damage from reactive oxygen species. Physiol Rev. 74(1):139–162. doi:10.1152/physrev.1994.74.1.139.

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