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The Relationship between the Antioxidant System and Proline Metabolism in the Leaves of Cucumber Plants Acclimated to Salt Stress

dc.contributor.authorNaliwajski, Marcin
dc.contributor.authorSkłodowska, Maria
dc.date.accessioned2021-12-15T13:28:54Z
dc.date.available2021-12-15T13:28:54Z
dc.date.issued2021
dc.identifier.citationNaliwajski, M.; Skłodowska, M. The Relationship between the Antioxidant System and Proline Metabolism in the Leaves of Cucumber Plants Acclimated to Salt Stress. Cells 2021, 10, 609. https://doi.org/10.3390/ cells10030609pl_PL
dc.identifier.issn2073-4409
dc.identifier.urihttp://hdl.handle.net/11089/40052
dc.description.abstractThe study examines the effect of acclimation on the antioxidant system and proline metabolism in cucumber leaves subjected to 100 and 150 NaCl stress. The levels of protein carbonyl group, thiobarbituric acid reactive substances, α-tocopherol, and activity of ascorbate and glutathione peroxidases, catalase, glutathione S-transferase, pyrroline-5-carboxylate: synthetase and reductase as well as proline dehydrogenase were determined after 24 and 72 h periods of salt stress in the acclimated and non-acclimated plants. Although both groups of plants showed high α-tocopherol levels, in acclimated plants was observed higher constitutive concentration of these compounds as well as after salt treatment. Furthermore, the activity of enzymatic antioxidants grew in response to salt stress, mainly in the acclimated plants. In the acclimated plants, protein carbonyl group levels collapsed on a constitutive level and in response to salt stress. Although both groups of plants showed a decrease in proline dehydrogenase activity, they differed with regard to the range and time. Differences in response to salt stress between the acclimated and non-acclimated plants may suggest a relationship between increased tolerance in acclimated plants and raised activity of antioxidant enzymes, high-level of α-tocopherol as well, as decrease enzyme activity incorporates in proline catabolism.pl_PL
dc.description.sponsorshipThis research was funded by the Polish Ministry of Science and Higher Education. Grant number NN 302117735.pl_PL
dc.language.isoenpl_PL
dc.publisherMDPIpl_PL
dc.relation.ispartofseriesCells;10(3)
dc.rightsUznanie autorstwa 4.0 Międzynarodowe*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectCucumis sativuspl_PL
dc.subjectsalt stresspl_PL
dc.subjectacclimationpl_PL
dc.subjectantioxidant enzymespl_PL
dc.subjectproline metabolismpl_PL
dc.titleThe Relationship between the Antioxidant System and Proline Metabolism in the Leaves of Cucumber Plants Acclimated to Salt Stresspl_PL
dc.typeArticlepl_PL
dc.page.number15pl_PL
dc.contributor.authorAffiliationDepartment of Plant Physiology and Biochemistry, Faculty of Biology and Environmental Protection, University of Lodz, ul. Banacha 12/16, 90-237 Lodz, Polandpl_PL
dc.contributor.authorAffiliationDepartment of Plant Physiology and Biochemistry, Faculty of Biology and Environmental Protection, University of Lodz, ul. Banacha 12/16, 90-237 Lodz, Polandpl_PL
dc.referencesVan Zelm, E.; Zhang, Y.; Testerink, C. Salt tolerance mechanisms of plants. Annu. Rev. Plant Biol. 2020, 71, 403–433pl_PL
dc.referencesMunns, R.; Tester, M. Mechanisms of salinity tolerance. Annu. Rev. Plant Biol. 2008, 59, 651–681,pl_PL
dc.referencesFAO Soils Portal. Available online: http://www.fao.org/soils-portal/soil-management/management-of-some-problem-soils/en/pl_PL
dc.referencesSafdar, H.; Amin, A.; Shafiq, Y.; Ali, A.; Yasin, R. A review: Impact of salinity on plant growth. Nat. Sci. 2019, 17, 34–40.pl_PL
dc.referencesFlowers, T.J.; Munns, R.; Colmer, T.D. Sodium chloride toxicity and the cellular basis of salt tolerance in halophytes. Ann. Bot. 2015, 115, 419–431.pl_PL
dc.referencesParida, A.K.; Das, A.B. Salt tolerance and salinity effects on plants: A review. Ecotoxicol. Environ. Saf. 2005, 60, 324–349.pl_PL
dc.referencesAcosta-Motos, J.A.; Ortuño, M.F.; Bernal-Vicente, A.; Diaz-Vivancos, P.; Sanchez-Blanco, M.J.; Hernandez, J.A. Plant responses to salt stress: Adaptive mechanisms. Agronomy 2017, 7, 18.pl_PL
dc.referencesAshraf, M.; Harris, P.J.C. Potential biochemical indicators of salinity tolerance in plants. Plant Sci. 2004, 166, 3–16.pl_PL
dc.referencesParihar, P.; Singh, S.; Singh, R.; Singh, V.P.; Prasad, S.M. Effect of salinity stress on plants and its tolerance strategies: A review. Environ. Sci. Pollut. Res. Int. 2015, 22, 4056–4075.pl_PL
dc.referencesStrogonov, B.P. Practical Means for Increasing Salt Tolerance of Plants as Related to Type of Salinity in the Soil. In Physiological Basis of Salt Tolerance of Plants; Poljakoff-Mayber, A., Meyer, A.A., Eds.; Israel Program for Scientific Translations Ltd.: Jerusalem, Israel, 1964; pp. 218–244.pl_PL
dc.referencesHossain, Z.; Mandal, A.K.A.; Datta, S.K.; Biswas, A.K. Development of NaCl-tolerant line in Chrysanthemum morifolium Ramat. through shoot organogenesis of selected callus line. J. Biotechnol. 2007, 129, 658–667.pl_PL
dc.referencesQueirós, F.; Fidalgo, F.; Santos, I.; Salema, R. In vitro selection of salt tolerant cell lines in Solanum tuberosum L. Biol. Plant. 2007, 51, 728–734.pl_PL
dc.referencesDuhan, S.; Kumari, A.; Lal, M.; Sheokand, S. Oxidative Stress and Antioxidant Defense under Combined Waterlogging and Salinity Stresses. In Reactive Oxygen, Nitrogen and Sulfur Species in Plants: Production, Metabolism, Signaling and Defense Mechanisms; Hasanuzzaman, M., Fotopoulos, V., Nahar, K., Fujita, M., Eds.; John Wiley & Sons Ltd.: Hoboken, NJ, USA, 2019; pp. 113–142pl_PL
dc.referencesTalaat, N.B. Role of Reactive Oxygen Species Signaling in Plant Growth and Development. In Reactive Oxygen, Nitrogen and Sulfur Species in Plants: Production, Metabolism, Signaling and Defense Mechanisms; Hasanuzzaman, M., Fotopoulos, V., Nahar, K., Fujita, M., Eds.; John Wiley & Sons Ltd.: Hoboken, NJ, USA, 2019; pp. 225–256.pl_PL
dc.referencesMøller, I.M.; Jensen, P.E.; Hansson, A. Oxidative modification to cellular components in plants. Annu. Rev. Plant Biol. 2007, 58, 459–481.pl_PL
dc.referencesSweetlove, L.J.; Møller, I.M. Oxidation of Proteins in Plants-Mechanisms and Consequences. In Advances in Biological Research. Oxidative Stress and Redox Regulation in Plants; Jacquot, J.P., Ed.; Academic Press: Burlington, VT, USA, 2009; Volume 52, pp. 1–23.pl_PL
dc.referencesSoltabayeva, A.; Ongaltay, A.; Omondi, J.O.; Srivastava, S. Morphological, physiological and molecular markers for salt-stressed. Plants 2021, 10, 243.pl_PL
dc.referencesFrancoz, E.; Ranocha, P.; Nguyen-Kim, H.; Jamet, E.; Burlat, V.; Dunand, C.H. Roles of cell wall peroxidases in plant development. Phytochemistry 2015, 112, 15–21.pl_PL
dc.referencesLee, B.-R.; Kim, K.-Y.; Jung, W.-J.; Avice, J.-C.H.; Ourry, A.; Kim, T.-H. Peroxidases and lignification in relation to the intensity of water-deficit stress in white clover (Trifolium repens L.). J. Exp. Bot. 2007, 58, 1271–1279.pl_PL
dc.referencesBolwell, G.P.; Wojtaszek, P. Mechanisms for the generation of reactive oxygen species in plant defense—A broad perspective. Physiol. Mol. Plant. Pathol. 1997, 51, 347–366.pl_PL
dc.referencesPandey, V.P.; Awasthi, M.; Singh, S.; Tiwari, S.; Dwivedi, U.N. A comprehensive review on function and application of plant peroxidases. Anal. Biochem. 2017, 6, 2161-1009.pl_PL
dc.referencesMhamdi, A.; Queval, G.; Chaouch, S.; Vanderauwera, S.; van Breusegem, F.; Noctor, G. Catalase function in plants: A focus on Arabidopsis mutants as stress-mimic models. J. Exp. Bot. 2010, 61, 4197–4220.pl_PL
dc.referencesMarrs, K.A. The functions and regulation of glutathione S-transferases in Plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 1996, 47, 127–158.pl_PL
dc.referencesRhodes, D.; Verslues, P.E.; Sharp, R.E. Role of Amino Acids in Abiotic Stress Resistance. In Plant Amino Acids. Biochemistry and Biotechnology; Singh, B.K., Ed.; Marcel Deker, Inc.: New York, NY, USA; Basel, Switzerland; Hong Kong, China, 1999; pp. 319–356.pl_PL
dc.referencesSignorelli, S.; Arellano, J.B.; Melø, T.B.; Borsani, O.; Monza, J. Proline does not quench singlet oxygen: Evidence to reconsider its protective role in plants. Plant Physiol. Biochem. 2013, 64, 80–83.pl_PL
dc.referencesSignorelli, S.; Coitiño, E.L.; Borsani, O.; Monza, J. Molecular mechanisms for the reaction between OH radicals and proline: Insights on the role as reactive oxygen species scavenger in plant stress. J. Phys. Chem. B 2014, 118, 37–47.pl_PL
dc.referencesNaliwajski, M.R.; Skłodowska, M. The relationship between carbon and nitrogen metabolism in cucumber leaves acclimated to salt stress. PeerJ 2018, 6, e6043.pl_PL
dc.referencesVerma, D.P.; Zhang, C.-S. Regulation of Proline and Arginine Biosynthesis in Plants. In Plant Amino Acids. Biochemistry and Biotechnology; Singh, B.K., Ed.; Marcel Deker, Inc.: New York, NY, USA; Basel, Switzerland; Hong Kong, China, 1999; pp. 249–265.pl_PL
dc.referencesSzabados, L.; Savoure, A. Proline: A multifunctional amino acid. Trends Plant Sci. 2010, 15, 89–97pl_PL
dc.referencesGarcia-Rios, M.; Fujita, T.; LaRosa, P.C.; Locy, R.D.; Clithero, J.M.; Bressan, R.A.; Csonka, L.N. Cloning of a polycistronic cDNA from tomato encoding γ-glutamyl kinase and γ-glutamyl phosphate reductase. Proc. Natl. Acad. Sci. USA 1997, 94, 8249–8254.pl_PL
dc.referencesSzoke, A.; Miao, G.; Hong, Z.; Verma, D.P.S. Subcellular location of Δ1-pyrroline-5-carboxylate reductase in root/nodule and leaf of soybean. Plant Physiol. 1992, 99, 1642–1649.pl_PL
dc.referencesRena, A.B.; Splittstoesser, W.E. Proline dehydrogenase and pyrroline-5-carboxylate reductase from pumpkin cotyledons. Phytochemistry 1975, 14, 657–661.pl_PL
dc.referencesNakano, Y.; Asada, K. Hydrogen peroxide is scavenged by ascorbate-specific peroxidase in spinach chloroplasts. Plant Cell Physiol. 1981, 22, 867–880.pl_PL
dc.referencesDhindsa, R.S.; Plumb-Dhindsa, P.; Thorpe, T.A. Leaf senescence: Correlated with increased levels of membrane permeability and lipid peroxidation, and decreased levels of superoxide dismutase and catalase. J. Exp. Bot. 1981, 32, 91–101.pl_PL
dc.referencesHabig, W.H.; Pabst, M.J.; Jakoby, W.B. Glutathione S-transferase. The first enzymatic step in mercaptane acid formation. J. Biol. Chem. 1974, 246, 7130–7139.pl_PL
dc.referencesHopkins, J.; Tudhope, G.R. Glutathione peroxidase in human red cells in health and disease. Br. J. Haematol. 1973, 25, 563–575.pl_PL
dc.referencesYagi, K. Assay for Serum Lipid Peroxide Level Its Clinical Significance. In Lipid Peroxides in Biology and Medicine; Yagi, K., Ed.; Academic Press, Inc.: London, UK; New York, NY, USA, 1982; pp. 223–241.pl_PL
dc.referencesLevine, R.L.; Garland, D.; Oliver, C.N.; Amici, A.; Climent, I.; Lenz, A.G.; Ahn, B.W.; Shaltiel, S.; Stadtman, E.R. Determination of carbonyl content in oxidatively modified proteins. Methods Enzymol. 1990, 186, 464–478.pl_PL
dc.referencesTaylor, S.L.; Lamden, M.P.; Tappel, A.L. Sensitive fluorometric method for tissue tocopherol analysis. Lipids 1976, 11, 530–538.pl_PL
dc.referencesBradford, M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248–254.pl_PL
dc.referencesFoyer, C.H.; Noctor, G. Oxidant and antioxidant signaling in plants: A re-evaluation of the concept of oxidative stress in a physiological context. Plant Cell Environ. 2005, 28, 1056–1071.pl_PL
dc.referencesSakhno, L.O.; Yemets, A.I.; Blume, B.Y. The Role of Ascorbate-Glutathione Pathway in Reactive Oxygen Species Balance under Abiotic Stresses. In Reactive Oxygen, Nitrogen and Sulfur Species in Plants: Production, Metabolism, Signaling and Defense Mechanisms; Hasanuzzaman, M., Fotopoulos, V., Nahar, K., Fujita, M., Eds.; John Wiley & Sons Ltd.: Hoboken, NJ, USA, 2019; pp. 89–111.pl_PL
dc.referencesAkram, N.A.; Shafiq, F.; Ashraf, M. Ascorbic acid—A potential oxidant scavenger and its role in plant development and abiotic stress tolerance. Front. Plant Sci. 2017, 8, 613.pl_PL
dc.referencesMittova, V.; Tal, M.; Volkovita, M.; Guy, M. Up-regulation of the mitochondrial and peroxisomal antioxidative systems in response to salt-induced oxidative stress in the wild salt-tolerant tomato species. Plant Cell Environ. 2002, 26, 845–856.pl_PL
dc.referencesMittova, V.; Guy, M.; Tal, M.; Volkovita, M. Response of the cultivated tomato and its wild salt-tolerant Lycopersicon pennellii to salt-dependent oxidative stress: Increased activities of antioxidant enzymes in root plastids. Free Radic. Res. 2002, 36, 195–202.pl_PL
dc.referencesMunné-Bosch, S. The role of α–tocopherol in plant stress tolerance. J. Plant Physiol. 2005, 162, 743–748.pl_PL
dc.referencesHernandez, J.A.; Jimenez, A.; Mullineaux, P.; Sevilla, F. Tolerance of pea (Pisum sativum L.) to long-term salt stress is associated with induction of antioxidant defences. Plant Cell Environ. 2000, 23, 853–862.pl_PL
dc.referencesSudhakar, C.; Lakshmi, A.; Giridarakumar, S. Changes in antioxidant enzyme efficacy in two high yielding genotypes of mulberry (Morus alba L.) under NaCl salinity. Plant Sci. 2001, 161, 613–619.pl_PL
dc.referencesSivritepe, N.; Sivritepe, H.Ö.; Türkan, I.; Bor, M.; Özdemir, F. NaCl pre-treatment mediate salt adaptation in melon plants through antioxidative system. Seed Sci. Technol. 2008, 36, 360–370.pl_PL
dc.referencesHoque, M.A.; Banu, M.N.A.; Nakamura, Y.; Shimoishi, Y.; Murata, Y. Proline and glycinebetaine enhanced antioxidant defense and mathylglyoxal detoxification systems and reduced NaCl-induced damage in cultured tobacco cells. J. Plant Physiol. 2008, 165, 813–824.pl_PL
dc.referencesPena, L.B.; Pausini, L.A.; Tomaro, M.L.; Gallego, S.M. Proteolytic system in sunflower (Helianthus annuus L.) leaves under cadmium stress. Plant Sci. 2006, 171, 53–537.pl_PL
dc.referencesCai-Hong, P.; Su-Jun, Z.; Zhi-Zhong, G.; Bao-Shan, W. NaCl treatment markedly enhances H2O2-scavenging system in leaves of halophyte Suaeda salsa. Physiol. Plant. 2005, 125, 490–499.pl_PL
dc.referencesKeleş, Y.; Öncel, I. Response of antioxidative defence system to temperature and water stress combinations in wheat seedlings. Plant Sci. 2002, 163, 783–790pl_PL
dc.referencesSkłodowska, M.; Gapińska, M.; Gajewska, E.; Gabara, B. Tocopherol content and enzymatic antioxidant activities in chloroplasts from NaCl-stressed tomato plants. Acta Physiol. Plant. 2009, 31, 393–400.pl_PL
dc.referencesBanerjee, A.; Roychoudhury, A. Role of Glutathione in Plant Abiotic Stress Tolerance. In Reactive Oxygen, Nitrogen and Sulfur Species in Plants: Production, Metabolism, Signaling and Defense Mechanisms; Hasanuzzaman, M., Fotopoulos, V., Nahar, K., Fujita, M., Eds.; John Wiley & Sons Ltd.: Hoboken, NJ, USA, 2019; pp. 159–172.pl_PL
dc.referencesRoxas, V.P.; Smith, R.K.; Allen, E.R.; Allen, R.D. Overexpression of glutathione S-transferase/glutathione peroxidase enhances the growth of transgenic tobacco seedlings during stress. Nat. Biotech. 1997, 15, 988–991.pl_PL
dc.referencesRoxas, V.P.; Lodhi, S.A.; Garrett, D.K.; Mahan, J.R.; Allen, R.D. Stress tolerance in transgenic tobacco seedlings that overexpress glutathione S-transferase/glutathione peroxidase. Plant Cell Physiol. 2000, 41, 1229–1234.pl_PL
dc.referencesHasanuzzaman, M.; Nahar, K.; Fujita, M. Plant Response to Salt Stress and Role of Exogenous Protectants to Mitigate Salt-Induced Damages. In Ecophysiology and Responses of Plants under Salt Stress; Ahmad, P., Azooz, M.M., Prasad, M.N.V., Eds.; Springer: New York, NY, USA, 2013; pp. 25–87.pl_PL
dc.referencesHoque, M.A.O.E.; Banu, M.N.A.; Nakamura, Y.; Shimoishi, Y.; Murata, Y. Exogenous proline mitigates the detrimental effects of salt stress more than the betaine by increasing antioxidant enzyme activities. J. Plant Physiol. 2007, 164, 553–561.pl_PL
dc.referencesBanu, N.A.; Hoque, A.; Watanabe-Sugimoto, M.; Matsuoka, K.; Nakamura, Y.; Shimoishi, Y.; Murata, Y. Proline and glicinebetaine induce antioxidant defense gene expression and suppress cell death in cultured tobacco cells under salt stress. J. Plant Physiol. 2009, 166, 146–156.pl_PL
dc.referencesNaliwajski, M.R.; Skłodowska, M. Proline and its metabolism enzymes in cucumber cell cultures during acclimation to salinity. Protoplasma 2014, 251, 201–209.pl_PL
dc.referencesWang, Z.Q.; Yuan, Y.Z.; Ou, J.Q.; Lin, Q.H.; Zhang, C.F. Glutamine synthetase and glutamate dehydrogenase contribute differentially to proline accumulation in leaves of wheat (Triticum aestivum) seedlings exposed to different salinity. J. Plant Physiol. 2007, 164, 695–701.pl_PL
dc.referencesMattioni, C.; Lacerenza, N.G.; Troccoli, A.; de Leonardis, A.M.; Di Fonzo, N. Water and salt stress-induced alterations in proline metabolism of Triticum durum seedlings. Physiol. Plant. 1997, 101, 787–792.pl_PL
dc.referencesPeng, Z.; Lu, Q.; Verma, D.P.S. Reciprocal regulation of Δ1-pyrroline-5-carboxylate synthetase and proline dehydrogenase genes controls proline levels during and after osmotic stress in plants. Mol. Gen. Genet. 1996, 235, 334–341.pl_PL
dc.contributor.authorEmailmarcin.naliwajski@biol.uni.lodz.plpl_PL
dc.identifier.doi10.3390/cells10030609
dc.relation.volume609pl_PL
dc.disciplinenauki biologicznepl_PL


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Uznanie autorstwa 4.0 Międzynarodowe
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