Abstract
Studies on oxidative stress on organisms especially on invertebrates are widely used as biomarkers in relation to the redox regulatory system to assess the freshwater environment. Despite broad availability of Indian apple snail Pila globosa, no data on its antioxidant and oxidative stress status are available. Therefore, determination of tissue-specific redox regulatory systems in P. globosa was the aim of this study. Snails were sampled from a non-polluted site by determination of oxidative stress parameters in hepatopancreas and foot muscle tissues. The levels of lipid peroxidation and total antioxidant capacity were found to be ten- and two fold higher, respectively, in hepatopancreas than foot muscle. Activity of different antioxidant enzymes was 20 to 100% higher in hepatopancreas than foot muscle. The concentration of small redox regulatory antioxidant such as GSH and AA was found to be 25 and 128% higher, respectively, in hepatopancreas. Thus, above tissue-specific antioxidant data can be used as base line data in P. globosa that may be used as biomarker species.
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References
Chainy GBN, Paital B, Dandapat J (2016) An overview of seasonal changes in oxidative stress and antioxidant defence parameters in some invertebrate and vertebrate species. Scientifica. https://doi.org/10.1155/2016/6126570
Bal A, Pati SG, Panda F, Mohanty L, Paital B (2021) Low salinity induced challenges in the hardy fish Heteropneustes fossilis; future prospective of aquaculture in near coastal zones. Aquaculture 543:737007. https://doi.org/10.1016/j.aquaculture.2021.737007
Panda F, Pati SG, Bal A, Mathur S, Nirmaladevi R, Paital B (2021) Temporal morphometric analyses of Pila globosa in India for its use in aquaculture and food industry. J Basic Appl Zool 82:1–9. https://doi.org/10.1186/s41936-021-00216-z
Panda F, Pati SG, Bal A, Das K, Samanta L, Paital B (2021) Control of invasive apple snails and their use as pollutant ecotoxic indicators: a review. Environ Chem Lett. https://doi.org/10.1007/s10311-021-01305-9
Paital B, Chainy GBN (2010) Antioxidant defenses and oxidative stress parameters in tissues of mud crab (Scylla serrata) with reference to changing salinity. Comp Biochem Physiol C 151:142–151. https://doi.org/10.1016/j.cbpc.2009.09.007
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275
Ohkawa H, Ohishi N, Yagi K (1979) Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal Chem 95:351–358. https://doi.org/10.1016/0003-2697(79)90738-3
Das K, Samanta L, Chainy GBN (2000) A modified spectrophotometric assay of superoxide dismutase using nitrite formation by superoxide radicals. Indian J Biochem Biophys 37:201–204
Aebi Hugo (1974) Catalase. Methods of enzymatic analysis. Elsevier, pp 673–684. https://doi.org/10.1016/B978-0-12-091302-2.50032-3
Paglia DE, Valentine WN (1967) Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J Lab Clin Med 70:158–169. https://doi.org/10.1016/B978-0-12-091302-2.50032-3
Massey V, Williams JCH (1965) On the reaction mechanism of yeast glutathione reductase. J Biol Chem 240:4470–4480
Habig WH, Pubst MJ, Jokoby WB (1974) GST the first enzymatic step in mercapturic acid formation. J Biol Chem 249:7130–7139
Marxen K, Vanselow KH, Lippemeier S, Hintze R, Ruser A, Hansen UP (2007) Determination of DPPH radical oxidation caused by methanolic extracts of some microalgal species by linear regression analysis of spectrophotometric measurements. Sens 7:2080–2095. https://doi.org/10.3390/s7102080
Sedlak J, Lindsay RH (1968) Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman’s reagent. Anal Biochem 25:192–205
Mitsui A, Ohta T (1961) Photooxidative consumption and photoreductive formation of ascorbic acid in green leaves. Plant and Cell Physiol 2:31–44. https://doi.org/10.1093/oxfordjournals.pcp.a077661
Gassner B, Wuthrich A, Scholtysik G, Solioz M (1997) The pyrethroids permethrin and cyhalothrin are po tent inhibitors of the mitochondrial complex I. J Pharmacol Exp 281:855–860
Lambowitz AM (1979) Preparation and analysis of mitochondrial ribosomes. Methods Enzymol 59:421–433
Singh P, Mann KA, Mangat HK, Kaur G (2003) Prolonged glutamate excitotoxicity: effects on mitochondrial antioxidants and antioxidant enzymes. Mol Cell Biochem 243:139–145. https://doi.org/10.1023/A:1021668314070
Reddy MK, Labhasetwar V (2009) Nanoparticle-mediated delivery of superoxide dismutase to the brain: an effective strategy to reduce ischemia-reperfusion injury. FASEB 23:1384–1395. https://doi.org/10.1096/fj.08-116947
Sözmen EY, Sözmen B, Delen Y, Onat T (2001) Catalase/superoxide dismutase (SOD) and catalase/paraoxonase (PON) ratios may implicate poor glycemic control. Arch of med res 32:283–287. https://doi.org/10.1016/S0188-4409(01)00285-5
Lubrano V, Balzan S (2015) Enzymatic antioxidant system in vascular inflammation and coronary artery disease. World j of exp med 5:218. https://doi.org/10.5493/wjem.v5.i4.218
Fernandez J, Wilson RA (2014) Characterizing roles for the glutathione reductase, thioredoxin reductase and thioredoxin peroxidase-encoding genes of Magnaporthe oryzae during rice blast disease. PLoS ONE 9:87300. https://doi.org/10.1371/journal.pone.0087300
Yin Y, Jia H, Sun Y, Yu H, Wang X, Wu J, Xue Y (2007) Bioaccumulation and ROS generation in liver of Carassius auratus, exposed to phenanthrene. Comp Biochem Physiol C 145:288–293. https://doi.org/10.1016/j.cbpc.2007.01.002
Kankofer M (2001) Antioxidative defence mechanisms against reactive oxygen species in bovine retained and not-retained placenta: activity of glutathione peroxidase, glutathione transferase, catalase and superoxide dismutase. Placenta 22:466–472. https://doi.org/10.1053/plac.2001.0650
Akram NA, Shafiq F, Ashraf M (2017) Ascorbic acid-a potential oxidant scavenger and its role in plant development and abiotic stress tolerance. Front plant sci 8:613. https://doi.org/10.3389/fpls.2017.00613
Paital B, Chainy GB (2012) Effects of salinity on O2 consumption, ROS generation and oxidative stress status of gill mitochondria of the mud crab Scylla serrata. Comp Biochem Physiol C 155(2):228–37. https://doi.org/10.1016/j.cbpc.2011.08.009
Paital B (2013) Antioxidant and oxidative stress parameters in brain of Heteropneustes fossilis under air exposure condition; role of mitochondrial electron transport chain. Ecotoxicol Environ Saf 95:69–77. https://doi.org/10.1016/j.ecoenv.2013.05.016
Paital B, Chainy GB (2013) Seasonal variability of antioxidant biomarkers in mud crabs (Scylla serrata). Ecotoxicol Environ Saf 87:33–41. https://doi.org/10.1016/j.ecoenv.2012.10.006
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The authors declare no conflict of interest. Funding to BRP from the Science and Engineering Research Board, Department of Science and Technology, Govt. of India New Delhi, India (No. ECR/2016/001984) and Department of Science and Technology, Government of Odisha (Grant letter number 1188/ST, Bhubaneswar, dated 01.03.17, ST-(Bio)-02/2017) is acknowledged.
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BRP was involved in conceptualization; data curation; formal analysis; funding acquisition; investigation; methodology; project administration; resources; software; supervision; validation; visualization; roles/writing—original draft; and writing—review and editing. FP contributed to investigation; methodology, writing—original draft; and writing—review and editing. SGP, AB and LS were involved in writing original draft, review and editing.
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Significant statement: For the first time, tissue-specific redox regulatory markers in P. globosa, one of the largest freshwater, semi-sessile, ectothermic mollusks with amphibious life, are measured to use this snail as bio-indicator for the environmental monitoring.
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Panda, F., Pati, S.G., Bal, A. et al. Redox Regulatory System in Semi-Sessile Amphibious Indian Apple Snail Pila Globosa for Future Ecotoxic Studies. Proc. Natl. Acad. Sci., India, Sect. B Biol. Sci. 93, 443–450 (2023). https://doi.org/10.1007/s40011-022-01434-3
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DOI: https://doi.org/10.1007/s40011-022-01434-3