DOI QR코드

DOI QR Code

The Effects of Calcium Nutrition on the Activities of Lactate Dehydrogenase, Alcohol Dehydrogenase and Other Enzymes in Melon (Cucumis melo L.) Seedlings Subjected to Flooding

  • Lee, Chang-Hee (School of Applied of Life Science, Kyungpook National University) ;
  • Park, Man (School of Applied of Life Science, Kyungpook National University) ;
  • Kang, Sang-Jae (School of Applied of Life Science, Kyungpook National University)
  • Received : 2015.11.24
  • Accepted : 2016.02.25
  • Published : 2016.02.29

Abstract

With transient flooding followed by poor or slow drainage plant roots may become reduction conditions because the root zone was fully filled with water. This study was examined the effects of calcium treatment in the early growth stage on biochemical changes in leaves and roots of melon (Cucumis melo L.) seedlings kept under flooding condition for 72 h. The activities of lactate dehydrogenase more gradually enhanced in the roots than those of leaves of melon seedlings treated with calcium. The activities of alcohol dehydrogenase associated with alcohol fermentation under low oxygen conditions continuously increased in the leaves and roots of seedlings untreated with calcium under flooding at least 72 h but those was constant within at least 12 h in treated with calcium. These results showed that calcium supplying in the early growth stage mitigated alcohol fermentation of melon seedlings kept under flooding condition for 72 h. Activities of nitrate reductase and acid phosphatase in the leaves and roots of seedlings in treated with calcium somewhat higher than those of non-treated with calcium. The activities of sucrose phosphate synthase and fructose-1,6-bisphosphatase of leaves of seedlings in treated with calcium more higher than those of non-treated with calcium. These results indicated that calcium nutrition mitigate the reduction of activities of some enzymes of melon seedling kept under flooding condition for 72 h.

Keywords

References

  1. Andrew, D.L., M.C. Drew, J.R. Johnson, and B.G. Cobb. 1994. The response of maize seedlings of different ages to hypoxic and anoxic stress. Plant Physiol. 105:53-60. https://doi.org/10.1104/pp.105.1.53
  2. Beck, E. and P. Ziegler. 1989. Biosynthesis and degradation of starch in higher plants. Annu. Rev. Plant Physio. Plant Mol. Biol. 40:95-118. https://doi.org/10.1146/annurev.pp.40.060189.000523
  3. Biemelt, S., U. Keetman, and G. Albrecht. 1998. Reaeration following hypoxia of anoxia lead to activation of the antioxidative defense system in roots of wheat seedlings. Plant Physiol. 116:651-658. https://doi.org/10.1104/pp.116.2.651
  4. Bozzo, G.G., K.G. Raghothama, and W.C. Plaxton. 2004. Structural ad kinetic properties of a novel purple acid phosphatase from phosphate-starved tomato (Lycopersicon esculentum) cell culture. Biochem. J. 377:419-428. https://doi.org/10.1042/bj20030947
  5. Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microquantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72:248-254. https://doi.org/10.1016/0003-2697(76)90527-3
  6. Bush, D.S. 1996. Effects of gibberellic acid and environmental factors on cytosolic calcium in wheat aleurone cells. Planta 199:89-99.
  7. Chang, W.P., L. Hunag, M. Shen, C. Webster, A. Burlingame, and J.K.M. Roberts. 2000. Patterns of protein synthesis and tolerance of anoxia in root tips of maize seedlings acclimated to a low oxygen environment, and identification of proteins by mass spectrometry. Plant Physiol. 122:295-318. https://doi.org/10.1104/pp.122.2.295
  8. Chung, H.-J., and R.J. Ferl. 1999. Arabidopsis alcohol dehydrogenase expression in both shoots and roots is conditioned by root growth environment. Plant Physiol. 121:429-436. https://doi.org/10.1104/pp.121.2.429
  9. Drueckes, P., R. Schinzel, and D. Palm. 1995. Photometric microtiter assay of inorganic phosphate in the presence of acid-labile organic phosphate. Anal. Biochem. 230:173-177. https://doi.org/10.1006/abio.1995.1453
  10. Drew, M.C. 1997. Oxygen deficiency and root metabolism: Injury and acclimation under hypoxia and anoxia. Annu. Rev. Plant Physiol. and Plant Mol. Biol. 48:223-250. https://doi.org/10.1146/annurev.arplant.48.1.223
  11. Epstein, E., and A.J. Bloom. 2005. Ecology and Environmental Stress. p. 328-330, Mineral Nutrition of Plants: Principles and Perspective, 2 nd edition, Sinauer Associate, MA. USA.
  12. Ferl, R., and B. Laughner. 1989. In vivo detection of the regulatory factor binding sites of Arabidopsis thaliana Adh. Plant Mol. Biol. 12:357-366.
  13. Fukuda, T., F. Yokoyama, T. Nakamura, I-J. Song, T. Ito, T. Ochiai, A. Kanno, T. Kameya, and M. Maki. 2005. Molecular phylogeny and evolution of alcohol dehydrogenase (Adh) genes in legumes. BMC Plant Biol. 5:6-15. https://doi.org/10.1186/1471-2229-5-6
  14. Grierson, W. 1999. Beneficial aspects of stress on plants. In: Handbook of Plant and crop stress, 2 nd edition, Pessarakli, M., ed. Dekker, New York. pp 1185-1198.
  15. Hoffman, N.E., A.F. Bent, and A.D. Hanson. 1986. Induction of lactate dehydrogenase isozymes by oxygen deficit in barley root tissue. Plant Physiol. 82:658-663. https://doi.org/10.1104/pp.82.3.658
  16. Ismail, A.M., E.S. Ella, G.V. Vergara, and D.J. Mackill. 2009. Mechanisms associated with tolerance to flooding during germination and early seedling growth in rice (Oryza sativa). Annal. Bot. 103:197-209. https://doi.org/10.1093/aob/mcn211
  17. Jeschke, W.D., E.A. Kirkby, A.D. Peuke, J.S. Pate, and W. Hartung. 1997. Effects of P deficiency on assimilation and transport of nitrate and phosphate in intact plants of caster bean (Ricinus communis L.). J. Exp. Bot. 48:75-91. https://doi.org/10.1093/jxb/48.1.75
  18. Johnson, J.R., B.G. Cobb, and M.C. Drew. 1994. Hypoxic induction of anoxia tolerance in roots of Adh null Zea mays L. Plant Physiol. 105:61-67. https://doi.org/10.1104/pp.105.1.61
  19. Kato-Noguchi, H., K-N., and M. Morokuma. 2007. Ethanolic fermentation and anoxia tolerance in four rice cultivar. J Plant Physiol. 164:168-173. https://doi.org/10.1016/j.jplph.2005.09.017
  20. Kerr, P.S., S.C. Huber, and D.W. Israel. 1984. Effect of N-source on soybean leaf sucrose phosphate synthase, starch formation and whole plant growth. Plant Physiol. 75:483-488. https://doi.org/10.1104/pp.75.2.483
  21. Kyozuka, J. M. Olive, W. Peacock, E. Dennis, and K. Shimamoto. 1994. Promotor elements required for developmental expression of the maize Adh1 gene in transgenic rice. Plant Cell 6:799-810. https://doi.org/10.1105/tpc.6.6.799
  22. Lefebvre, D.D., S.M.G. Duff, C.A. Fife, C. Julien-Inalsingh, and W.C. Plaxton. 1990. response to phosphate deprivation in Brassica nigra suspension cells. Plant Physiol. 93:504-511. https://doi.org/10.1104/pp.93.2.504
  23. Mann, A.F., D.P. Hucklesby, and E.J. Hewitt. 1979. Effect of aerobic and anaerobic conditions on the in vivo nitrate reductase assay in spinach leaves. Planta 146:83-89. https://doi.org/10.1007/BF00381259
  24. Matton, D.P., P. Constabel, and N. Brission. 1990. Alcohol dehydrogenase gene expression in potato following elicitor and stress treatment. Plant Mol. Biol. 14:775-783. https://doi.org/10.1007/BF00016510
  25. Mayne, R.G. and P.J. Lea. 1984. Alcohol dehydrogenase in Hordeum vulgare: Changes in isoenzyme levels under hypoxia. Plant Sci. Lett. 37:73-78. https://doi.org/10.1016/0304-4211(84)90206-2
  26. Peng, H-P., C-S. Chan, M-C. Shih, and S.F. Yang. 2001. Signaling events in the hypoxic induction of alcohol dehydrogenase gene in Arabidopsis. Plant Physiol. 126:742-749. https://doi.org/10.1104/pp.126.2.742
  27. Robinson, W.D., J.Park, H.T. Tran, H.A. Del Vecchio, S. Ying, J.L. Zins, K. Patel, T.D. McKnight, and W.C. Plaxton. 2012. The secreted purple acid phosphatase isozymes AtPAP12 and AtPAP26 play a pivotal role in extracellular phosphate scavenging by Arabidopsis thaliana. J. Exp. Bot 63:6531-6542. https://doi.org/10.1093/jxb/ers309
  28. Rudd, J.J., and V.E. Fraklin-Tong. 2001. Unravelling response-specificity in $Ca^{+2}$ signalling pathways in plant cells. New Phytologist. 151:7-33. https://doi.org/10.1046/j.1469-8137.2001.00173.x
  29. Rufty, T.W., P.S. Kerr, and S.C. Huber. 1983. Characterization of diurnal changes in activities of enzymes involved in sucrose biosynthesis. Plant Physiol. 73:428-433. https://doi.org/10.1104/pp.73.2.428
  30. Sach, M.M., M. Freeling, and R. Okimoto. 1980. The anaerobic proteins of maize. Cell 20:761-767. https://doi.org/10.1016/0092-8674(80)90322-0
  31. Sander, D., C. Brownlee, J.F. Harper. 1999. Communicating with calcium. The Plant Cell 11:691-706. https://doi.org/10.1105/tpc.11.4.691
  32. Sedbrook, J.C., P.J. Kronebusch, G.G. Borisy, A.J. Trewavas, and P.H. Masson. 1996. Transgenic aequorin reveals organspecific cytosolic $Ca^{+2}$ responses to anoxia in Arabidopsis thaliana seedlings. Plant Physiol. 111:243-257. https://doi.org/10.1104/pp.111.1.243
  33. Solomon, L.P. and M.J. Barber. 1990. Assimilatory nitrate reductase: functional properties and regulation. Annu. Rev. Plant Biol. 41:224-253.
  34. Subbaiah, C.C., J. Zhang, and M.M. Sach. 1994. Involvement of interacellular calcium in anaerobic gene expression an survival of maize seedlings. Plant Physiol. 105:369-376. https://doi.org/10.1104/pp.105.1.369
  35. Subbaiah, C.C., D.S. Bush, and M.M. Sachs. 1998. Mitochondrial contribution to the anoxic $Ca^{+2}$ signal in maize suspension-cultured cells. Plant Physiol. 118:759-771. https://doi.org/10.1104/pp.118.3.759
  36. Taiz, L., and E. Zeiger. 2002. Photosynthesis: carbon reaction p. 145-170. Plant Physiology, 3rd edition, Sinauer Associates, Massachusettes, USA.

Cited by

  1. vol.58, pp.12, 2017, https://doi.org/10.3341/jkos.2017.58.12.1333