Environmental Analysis Health and Toxicology

The Korean Society of Environmental Health and Toxicology (환경독성보건학회)
권호 표지

Changes in Cellular Viability and Peroxidase Activities of Green Algae Selenastrum capricornutum (Chlorophyceae) to Cadmium

카드뮴에 대한 녹조류 Selenastrum capricornutum (Chlorophyceae)의 세포활력도 및 peroxidase 활성도 변화

  • Published : 2003.12.01
Download PDF
⟨ Previous Next ⟩

Abstract

Physiological cellular activities responses to cadmium (Cd) exposure in green algae with several reductases activities and viability of the cell were examined. The cell division of green algae, Selenastrum capricornutum treated with 5ppm was significantly decreased than that of normal algae. The mean cell number of normal algal culture was as twice much as than that of algae at 6 days after Cd treatment. The cellular viability of algae was analysed by flow-cytometry with fluorescent dye after esterase reaction on cell membrane. The 85.35% of cellular viability of normal culture was decreased to 34.35% when algae was treated with 5 ppm of Cd at 6 days after treatment. It was considered that those method of flow-cytometry is useful tool for toxicity test on micro-organisms in the respect of identifying cellular viability. Also, the activities of both glutathione peroxidase (GPX) and ascorbate peroxidase (APX), which are indirectly react against oxidative stress through reduction of glutathione by Cd were significantly increased with 25%. It is considered that both GPX and APX are involved in the metabolic pathway of Cd -detoxification with similar portion in Selenasturm capricornutum.

Keywords

References

  1. Berglund DL and Eversman S. Flow Cytometric measure-ments of pollutant stresses on algal cells, Cytometry 1988; 9: 150-155 https://doi.org/10.1002/cyto.990090209
  2. Breeuwer P, Drocourt JL, Bunschoten N, Zwietering MH, Romouts FM and Abee T. Characterisation of uptake and hydrolysis of fluorescein diacetate and carboxy-fluorescein diacetate by intracellular esterases in Sac-charomyces cerevisiae, which result in accumulation of fluorescent product, Appl. Environ. Microbiol. 1995; 61: 1614-1619
  3. Dorsey J, Yentsch C, Mayo S and McKenna C. Rapid analytical technique for the assessment of cell metabolic activity in marine microalgae, Cytometry 1989; 10: 622-628 https://doi.org/10.1002/cyto.990100518
  4. Franklin NM, Adams MS and Stauber RP. Development of an improved rapid enzyme inhibition bioassy with marine and freshwater microalgae using flow cytometry, Archives of Environmental Contamination and Toxicology 2000; 40: 469-480
  5. Gala WR and Giesy JP. Flow cytometric techniques to assess toxicity to algae, In: Landis WG, van der Schalie WH(eds). Aquatic toxicology and risk assessment, American Society for Testing and Materials, Philadelphia, PA, 1990; 13: 237-246
  6. Grill E, Loffler S, Winnacker EL and Zenk MH. Phytoche-latins, the heavy-metal-binding peptides of plant, are synthesised from glutathione by a specific $\gamma$-glutamylcysteine dipeptidyl transpepticlase (phytochelatin syn-thase), Proc. Natl. Acad. Sci. USA. 1986; 86: 6838-42 https://doi.org/10.1073/pnas.86.18.6838
  7. Hamer DH, Thiele DJ and Lemontt. Function and autoregu-lation of yeast copperthionein, Science 1985; 228: 685-690 https://doi.org/10.1126/science.3887570
  8. Howden R and Cobbett CS. Cadmium-sensitive mutants of Arabidopsis thaliana, Plant Physiol. 1992; 99: 100-107
  9. Humphreys MJ, Allman R and Lloyd D. Determination of the viability of Trichomonas vaginalis using flow cytom-etry, Cytometry 1994; 15: 343-348 https://doi.org/10.1002/cyto.990150410
  10. Jin CD. Effect of Benzyladenine on Development of En-zymes Related to Ascorbate-Glutathione Pathway in Senescing Wheat Leaves, J. Plant Biol. 1995; 38(1): 47-54
  11. Kaprelyants AS and Kell DB. Rapid toxicity assessment of bacterial viability and vitality by rhodamine 123 and flow cytometry, JM Appl. Bacteriol. 1992; 72: 410-422 https://doi.org/10.1111/j.1365-2672.1992.tb01854.x
  12. Mannervik B. The isozymes of glutathione S-transferases, Adv. Enzymol. Relat. Ares. Mol. Biol. 1985; 57: 357-417
  13. Michalska AE and Choo KHA. Targeting and germ-line transmission of a null mutation at the metallothionein I and II loci in mouse, Proc. Natl. Acad. Sci. USA. 1993; 90: 8088-8092 https://doi.org/10.1073/pnas.90.17.8088
  14. Mittler R and Zilinskas BA. Detection of Ascorbate Perox-idase Activity in Native Gels by Inhibition of the Ascor-bate-Dependent Reduction of Nitroblue Tetrazolium, Anal. Biochem. 1993; 212: 540-546 https://doi.org/10.1006/abio.1993.1366
  15. Murasugi A, Wada C and Hayashi Y. Occurrence of acidlabile sulfide in cadmium-binding peptide I from fis-sion yeast, J. Biochem. JP. 1983; 93: 661-664 https://doi.org/10.1093/oxfordjournals.jbchem.a134222
  16. Ortiz DF, Ruscitti T, McCue KF and Ow DW. Transport of metal-binding peptides by HMTl, a fission yeast ABC-type vacuolar membrane protein, J. Biol. Chem. 1995; 270: 4721-4728 https://doi.org/10.1074/jbc.270.9.4721
  17. Pickett CB and Lu AY. Glutathione S-transferases: gene structure, regulation, and biological function, Ann. Rev. Biochem. 1989; 59: 61-86 https://doi.org/10.1146/annurev.bi.59.070190.000425
  18. Piscator M. Dietary exposure to cadmium and health effects: Impact of environmental changes, Environ. Health. Per-spect. 1985; 63: 127-131 https://doi.org/10.2307/3430038
  19. Rauser WE. Phytochelatins and related peptides: structure, biosynthesis and function, Plant Physiol. 1995; 109: 1141-1149 https://doi.org/10.1104/pp.109.4.1141
  20. Rauser WE. Structure and function of metal chelators pro-duced by plant; the case for organic acids, amino acids, phytin and metallothioneins, Cell Biochem. Biophys. 1999; 31: 19-48 https://doi.org/10.1007/BF02738153
  21. Surasak S, Samuel T, Desh PS, Richard V and Sayre T. Molecular mechanisms of proline-mediated tolerance to toxic heavy metals in transgenic microalgae, Plant Cell 2002; 14: 2837-2847 https://doi.org/10.1105/tpc.004853
  22. Tomsett AB and Thurman DA. Molecular biology of metal tolerances of plants, Plant Cell Environ. 1988; 11: 383-394 https://doi.org/10.1111/j.1365-3040.1988.tb01362.x
  23. Vilem Z, Oliver S and Arminio B. Growth controled oscilla-tion in activity of histone HI kinase during the cell cycle of Chlamydomonas reinhardtii (Chlorophyta), J. Phycol. 1997; 33: 673-681 https://doi.org/10.1111/j.0022-3646.1997.00673.x
  24. Vogeli-Lange R and Wagner GJ. Subcellular localisation of cadmium and cadmium-binding peptides in tobacco leaves: implication of a transport function for cadmium-binding peptides, Plant Physiol. 1990; 92: 1086-1093 https://doi.org/10.1104/pp.92.4.1086
  25. Waalkes MP, Hjelle JJ and Klaassen CD. Transient induc-tion of hepatic metallothionein following oral ethanol administration, Toxicol. Appl. Pharmacol. 1984; 74(2): 230-236 https://doi.org/10.1016/0041-008X(84)90147-9
  26. Zenk MH. Heavy metal detoxification in higher plants: a review, Gene 1996; 179: 21-30 https://doi.org/10.1016/S0378-1119(96)00422-2