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http://dx.doi.org/10.5762/KAIS.2015.16.9.6425

Immunolocalization of Wound-Inducible Insoluble Acid Invertases in Pea (Pisum sativum L)  

Kim, Donggiun (Department of Life Science, Silla University)
Lee, Taek-Kyun (South Sea Institute, Korea Institute of Ocean Science and Technology)
Publication Information
Journal of the Korea Academia-Industrial cooperation Society / v.16, no.9, 2015 , pp. 6425-6431 More about this Journal
Abstract
Invertase, that hydrolyzes sucrose into glucose and fructose, plays a great role in carbohydrate reallocation between the photosynthetic source tissue and various sink tissues. Invertase also occurs in a variety of isoforms for various functions in plants. Insoluble invertases were extracted only in buffer solutions containing high concentrations of salt. Within these classes, acid invertase has an optimum activity at acidic pH (pH 4-5). Induction of insoluble acid invertase (INAC-INV) in leaf, stem, and root tissues in response to physical wounding has been investigated. To detect the localization of INAC-INV within the plant, immunolocalization has been performed. In this study, the accumulation of INAC-INV was noticeable to reach maximum levels on 72 hr after mechanical injuries. INAC-INV was induced in wounded leaves 3 times more than control leaves. Immunolocalization results showed that INAC-INV accumulated in wall appositions and intercellular spaces. INAC-INV was also localized at sieve cell walls in phloem tissues close to the site of wounding. Taken together, this study suggested that INAC-INV induction upon wounding injuries can play a role on responses to the high energy demand for wound healing process.
Keywords
Immunocytochemistry; Insoluble acid invertase; Localization; Pisum sativum L.; Wounding;
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1 K. Koch. "Sucrose metabolism: regulatory mechanisms and pivotal roles in sugar sensing and plant development". Curr. Opin. Plant Biol. 7, 235-246, 2004. DOI: http://dx.doi.org/10.1016/j.pbi.2004.03.014   DOI
2 F. Rolland, E. Baena-Gonzalez, J. Sheen. "Sugar sensing and signaling in plants: conserved and novel mechanisms". Annu. Rev. Plant Biol. 57, 675-709, 2006. DOI: http://dx.doi.org/10.1146/annurev.arplant.57. 032905.105441   DOI
3 J. Wind, S. Smeekens, J. Hanson. "Sucrose: metabolite and signaling molecule". Phytochemistry 71, 1610-1614, 2010. DOI: http://dx.doi.org/10.1016/j.phytochem.2010. 07.007   DOI
4 T. Roitsch, M. C. Gonzalez. "Function and regulation of plant invertases: sweet sensations". Trends Plant Sci. 9, 606-613, 2004. DOI: http://dx.doi.org/10.1016/j.tplants.2004.10.009   DOI
5 A. Sturm. "Invertases: Primary structures, functions, and roles in plant development and sucrose partitioning". Plant Physiol. 121, 1-7. 1999 DOI: http://dx.doi.org/10. 1104/ pp. 121. 1. 1   DOI
6 J. A. Tognetti, H. G. Pontis, G. M. Martinez-Noel. "Sucrose signaling in plants: A world yet to be explored". Plant Signal Behav. 8, e23316. 2013. DOI: http://dx.doi.org/10.4161/psb.23316   DOI
7 H. B. Krishnan, S. G. Pueppke. "Invertases from rust-infected wheat leaves". J Plant Physiol 133, 336-339, 1988. DOI: http://dx.doi.org/10.1016/S0176-1617(88)80211-6   DOI
8 A. Sturm, M. J. Chrispeels. "cDNA cloning of carrot extracellular beta-fructosidase and its expression in response to wounding and bacterial infection". Plant Cell 2, 1107-1119, 1990. DOI: http://dx.doi.org/10.1105/tpc.2.11.1107
9 L. Zhang, N. Cohn, J. Mitchell. "Induction of a pea cell-wall invertase gene by wounding and its localized expression in phloem". Plant Physiol. 112, 1111-1117, 1996. DOI: http://dx.doi.org/10.1104/ pp.112.3.1111   DOI
10 D. Kim, S. Park, Y. Chung, J. Park, S. Lee, T-K. Lee. "Biochemical Characterization of Soluble Acid and Alkaline Invertases from Shoots of Etiolated Pea Seedlings". J. Integr. Plant. Biol. 52, 536-548, 2010. DOI: http://dx.doi.org/10.1111/j.1744-7909.2010.00937.x.   DOI
11 D. Kim, G. Lee, M. Chang, J. Park, Y. Chung, S. Lee, T-K. Lee. "Purification and Biochemical Characterization of Insoluble Acid Invertase (INAC-INV) from Pea Seedlings". J. Agric. Food Chem. 59, 11228-11233, 2011. DOI: http://dx.doi.org/10.1021/jf201057c   DOI
12 K. Matsushita, I. Uritani. "Change in invertase activity of sweet potato in response to wounding and purification and properties of its invertases". Plant Physiol 54, 60-66, 1974.   DOI
13 N. S. Cohn, J. P. Mitchell. "Immunocytochemical localization of proteins in differentiating tissues of Pisum sativum. Histochemistry 84, 432-438, 1986. DOI: http://dx.doi.org/10.1007/BF00482975   DOI
14 J. W. Stirling, P. S. Graff. "Antigen unmasking for immunoelectron microscopy: labeling is improved by treating with sodium ethoxide or sodium metaperiodate, then heating on retrieval medium". J Histochem Cytochem 43, 115-123, 1995. DOI: http://dx.doi.org/10.1177/43.2.7529784   DOI
15 M. C. Jamur, C. D. Faraco, L. O. Lunardi, R. P. Siraganian, C. Oliver. "Microwave fixation improves the antigenicity of glutaraldehyde-sensitive antigens while preserving ultrastructural detail". J Histochem Cytochem 43, 307-311, 1995. DOI: http://dx.doi.org/10.1177/43.3.7868860   DOI
16 N. Benhamou, J. Grenier, M.J. Chrispeels. "Accumulation of beta-fructosidase in the cell walls of tomato roots following infection by a fungal wilt pathogen". Plant Physiol. 97, 739-750. 1991. DOI: http://dx.doi.org/10.1104/pp.97.2.739   DOI
17 T. Roitsch, W. Tanner. "Cell wall invertases: Bridging the gap". Botanica Acta 109, 90-93. 1996. DOI: http://dx.doi.org/10.1111/j.1438-8677.1996.tb00547.x   DOI
18 J. W. Patrick. "Sieve element unloading, cellular pathway, mechanism and control". Physiol Plant 78: 298-308. 1990. DOI: http://dx.doi.org/10.1111/j.1399-3054.1990.tb02095.x   DOI
19 A. S. Tauzin, T. Giardina. "Sucrose and invertases, a part of the plant defense response to the biotic stresses". Frontiers in plant science 293(5), 1-8, 2014. DOI: http://dx.doi.org/10.3389/fpls.2014.00293
20 Z. Tymowska-Lalanne, M. Kreis. "The plant invertases: physiology, biochemistry and molecular biology". Adv. Bot. Resear. 28, 71-117, 1998. DOI: http://dx.doi.org/10.1016/S0065-2296(08)60294-3   DOI