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Spatial and functional correlation between diamine-oxidase and peroxidase activities and their dependence upon de-etiolation and wounding in chick-pea stems

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Abstract

The activities of diamine oxidase (DAO, EC 1.4.3.6) and peroxidase (POD, EC 1.11.1.7) were determined along the stems of light-grown Cicer arietinum L. (chick-pea) seedlings. Enzyme activities were evaluated in the soluble, lightly bound (salt extraction) and tightly bound (Driselase digestion) wall fractions, and in residual fractions obtained from the different internodes. Apparent tissue distributions of both enzymes and lignin depositions were visualised by means of histochemical and immunohistochemical techniques. A close relationship was found between DAO and POD activities in the soluble and wall fractions along the stem. The biochemical activities of both enzymes decreased from the base to the apex of the stem in parallel with the distribution pattern of lignifying tissues in this organ. A similar activity gradient was found for each enzyme along the epidermis of the whole organ. Moreover, deetiolation elicited a rise in the activities of both enzymes in this tissue. Wounding chick-pea stems induced parallel increases in DAO and POD activities in the soluble and wall fractions. In-situ histochemical detection of both enzymes demonstrated the parallel occurrence of the DAO/POD system and lignosuberised depositions in the cell walls adjacent to the wound site. The patterns of POD isoforms resulting from the wound-healing process were determined by means of starch-gel electrophoresis. In addition to changes in relative intensity of enzyme bands in soluble and wall fractions, a new POD isoform, possibly related to the wounding response, appeared in the soluble fraction. This isoform was shown to be lightly bound to cell walls as it could be detected in the extracellular fluids obtained from wound-healed seedlings. On the basis of the above-mentioned results, a strict spatial and functional correlation can be inferred between DAO and POD in chick-pea, and probably in other Leguminosae species, in accordance with previous evidence indicating an integrated role for these enzymes in the apoplast.

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Abbreviations

DAO:

diamine oxidase

POD:

peroxidase

Syr:

syringaldazine

References

  • Angelini, R., Federico, R. (1986) Occurrence of diamine oxidase in the apoplast of Leguminosae seedlings. In: Biomedical studies of natural polyamines, pp. 183–189, Caldarera, C.M., Clò, C., Guarnieri, C., eds. CLUEB, Bologna

    Google Scholar 

  • Angelini, R., Federico, R. (1989) Histochemical evidence of polyamine oxidation and hydrogen peroxide production in the cell wall. J. Plant Physiol. 135, 212–217

    Google Scholar 

  • Angelini, R., Di Lisi, F., Federico, F. (1985) Immunoaffinity purification and characterization of diamine oxidase from Cicer. Phytochemistry 24, 2511–2513

    Google Scholar 

  • Angelini, R., Federico, R., Mancinelli, A. (1988) Phytochrome-mediated control of diamine oxidase level in lentil (Lens culinaris Medicus) seedlings. Plant Physiol. 88, 1207–1209

    Google Scholar 

  • Bagni, N., Serafini-Fracassini, D., Torrigiani, P. (1982) Polyamines and cellular growth processes in higher plants. In: Plant growth substances 1982, pp. 473–482, Wareing, P.F., ed. Academic Press, London

    Google Scholar 

  • Biggs, K.G., Fry, S.C. (1987) Phenolic cross-linking in the cell wall. In: Physiology of cell expansion during plant growth, pp. 46–57, Cosgrove, D.J., Knievel, D.P., eds. American Society of Plant Physiologists, Rockville, USA

    Google Scholar 

  • Borchert, R. (1978) Time course and spatial distribution of phenylalanine ammonia lyase and peroxidase activity in wounded potato tuber tissue. Plant Physiol. 62, 789–793

    Google Scholar 

  • Bradford, M.M. (1986) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248–254

    Google Scholar 

  • Espelie, K.E., Franceschi, V.R., Kolattukudy, P.E. (1986) Immunocytochemical localization and time course of appearance of an anionic peroxidase associated with suberization in wound-healing potato tuber tissue. Plant Physiol. 81, 487–492

    Google Scholar 

  • Federico, R., Angelini, R. (1986) Occurrence of diamine oxidase in the apoplast of pea epicotyls. Planta 167, 300–303

    Google Scholar 

  • Federico, R., Angelini, R. (1988) Distribution of polyamines and their related catabolic enzyme in epicotyls of etiolated and light-grown Leguminosae seedlings. Planta 173, 317–321

    Google Scholar 

  • Federico, R., Angelini, R., Argento-Cerù, M.P., Manes, F. (1985a) Immunohistochemical demonstration of lentil diamine oxidase Cell. Mol. Biol. 31, 171–174

    Google Scholar 

  • Federico, R., Angelini, R., Cesta, A., Pini, C. (1985b) Determination of diamine oxidase in lentil seedlings by enzyme activity and immunoreactivity. Plant Physiol. 79, 62–65

    Google Scholar 

  • Federico, R., Alisi, C., Angelini, R. (1988) On the occurrence of oxidoreductases in the apoplast of Leguminosae and Gramineae and their significance in the study of plasmamembrane-bound redox activities. In: Plasma membrane oxidoreductases in control of animal and plant growth, pp. 333–337, Crane F.L., Morré D.J., Low H., eds. Plenum Press, New York

    Google Scholar 

  • Fleuriet, A., Deloire, A. (1982) Aspects histochimique et biochimique de la cicatrisation des fruit de tomate blessés. Z. Pflanzenphysiol. 107, 259–268

    Google Scholar 

  • Friedman, R., Levin, N., Altman, A. (1986) Presence and identification of polyamines in xylem and phloem exudates of plants. Plant Physiol. 82, 1154–1157

    Google Scholar 

  • Fukuda, H., Komamine, A. (1982) Lignin synthesis and its related enzymes as marker of tracheary element differentiation in single cells isolated from Zinnia elegans. Planta 155, 423–430

    Google Scholar 

  • Gahan, P.B., Dawson, A.L., Auderset, G. (1986) Cytochemical assays of peroxidase activities in relation to growth and development. In: Molecular and physiological aspects of plant peroxidases, pp. 441–450, Greppin, H., Penel, C., Gaspar, T., eds. University of Geneva, Switzerland

    Google Scholar 

  • Gaspar, Th. (1986) Integrated relationship of biochemical and physiological peroxidase activities. In: Molecular and physiological aspects of plant peroxidases, pp. 455–468, Greppin, H., Penel, C., Gaspar, T., eds. University of Geneva, Switzerland

    Google Scholar 

  • Goldberg, R., Perdrizet, E. (1984) Ratio of free to bound polyamines during maturation of in mung-bean hypocotyl cells. Planta 161, 531–535

    Google Scholar 

  • Goldberg, R., Liberman, M., Mathieu, C., Pierron, A.M., Catesson, A.M. (1987) Development of epidermal cell wall peroxidases along the mung bean hypocotyl: possible involvement in the cell wall stiffening process. J. Exp. Bot. 38, 1378–1390

    Google Scholar 

  • Goldberg, R., Kevers, C., Gaspar, T. (1989) Guaiacol and ascorbate peroxidase compartmentation and gradient along the growing mung bean hypocotyl. Biochem. Physiol. Pflanzen 184, 155–161

    Google Scholar 

  • Haslam, S.C., Young, T.W. (1987) Partial purification of a diamine oxidase from Nicotiana rustica. Phytochemical Society of Europe Symposium on ‘Amines in plants’, University College, London, abstract

    Google Scholar 

  • Hatch, M.D., Glasziou, K.T. (1963) Sugar accumulation cycle in sugar cane. II. Relationship of invertase activity to sugar content and growth rate in storage tissue of plants grown in controlled environments. Plant Physiol. 38, 344–348

    Google Scholar 

  • Johansen, D.A.J. (1940) Plant microtechnique. McGraw-Hill, London

    Google Scholar 

  • Kaur-Sawhney, R, Flores, H.E., Galston, A.W. (1981) Polyamine oxidase in oat leaves: a cell wall localized enzyme. Plant Physiol. 68, 494–498

    Google Scholar 

  • Kutschera, U., Bergfeld, R., Schopfer, P. (1987) Cooperation of epidermis and inner tissues in auxin-mediated growth of maize coleoptiles. Planta 170, 168–180

    Google Scholar 

  • Lamport, D.T.A. (1986) Roles for peroxidases in cell wall genesis. In: Molecular and physiological aspects of plant peroxidases, pp. 199–207, Greppin, H., Penel, C., Gaspar, T., eds. University of Geneva, Switzerland

    Google Scholar 

  • Macheix, J.J., Fleuriet, A., Quessada, M.P. (1986) Involvement of phenols and peroxidase in wound-healing and grafting. In: Molecular and physiological aspects of plant peroxidases, pp. 267–286, Greppin, H., Penel, C., Gaspar, T., eds. University of Geneva, Switzerland

    Google Scholar 

  • Manes, F., Angelini, R., Federico, R. (1985) Diamine oxidase and peroxidase activity in pea seedlings. G. Bot. Ital. 119, (Suppl. 1), 115–116

    Google Scholar 

  • Palavan, N., Galston, A.W. (1982) Polyamine biosynthesis and their titer during various developmental stages of Phaseolus vulgaris. Physiol. Plant. 55, 438–444

    Google Scholar 

  • Penel, C., Greppin, H., Boisard, J. (1976) In vitro photomodulation of a peroxidase activity through membrane bound phytochrome. Plant Sci. Lett. 6, 117–121

    Google Scholar 

  • Percival, F.W., Purves, W.K. (1974) Multiple amine oxidase in cucumber seedlings. Plant Physiol. 54, 601–607

    Google Scholar 

  • Poulik, M.D. (1957) Starch gel electrophoresis in a discontinuous system of buffers. Nature 180, 1477

    CAS  PubMed  Google Scholar 

  • Rinaldi, A., Floris, G., Finazzi-Agrò, A. (1982) Purification and properties of diamine oxidase from Euphorbia latex. Eur. J. Biochem. 127, 417–420

    Google Scholar 

  • Rittinger, P.A., Biggs, A.R., Peirson, D.R. (1987) Histochemistry of lignin and suberin deposition in boundary layers formed after wounding in various plant species and organs. Can. J. Bot. 65, 1886–1892

    Google Scholar 

  • Roberts, L.W. (1987) Evidence from wound response and tissue culture. In: Vascular differentiation and growth regulators, pp. 63–88, Roberts, L.W., Gahan, P.B., Aloni, R., eds. Springer, Berlin Heidelberg New York

    Google Scholar 

  • Sharma, R., Sopory, S.K., Guha-Mukherjee, S. (1976) Phytochrome regulation of peroxidase activity in maize. Plant Sci. Lett. 6, 69–75

    Google Scholar 

  • Smith, T.A. (1985a) The di- and polyamine oxidases of higher plants. Biochem. Soc. Trans. 13, 319–322

    Google Scholar 

  • Smith, T.A. (1985b) Polyamines. Annu. Rev. Plant Physiol. 36, 117–143

    Google Scholar 

  • Smith, T.A., Barker, J.H.A. (1988) The di- and polyamine oxidases of plants. In: Progress in polyamine research: novel biochemical, pharmacological and clinical aspects, pp. 573–587, Zappia, V., Pegg, A.E., eds. Plenum Press, New York

    Google Scholar 

  • Torrigiani, P., Scoccianti, V., Bagni, N. (1988) Polyamine oxidase activity and polyamine content in maize during seed germination. Physiol. Plant. 74, 427–432

    Google Scholar 

  • Torrigiani, P., Serafini-Fracassini, D., Fara, A. (1989) Diamine oxidase activity in different physiological stages of Heliantus tuberosus tuber. Plant Physiol. 89, 69–73

    Google Scholar 

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Authors and Affiliations

  1. Dipartimento di Biologia Vegetale, Università “La Sapienza”, P. le Aldo Moro 5, I-00185, Rome, Italy

    R. Angelini, F. Manes & R. Federico

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  1. R. Angelini
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  2. F. Manes
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  3. R. Federico
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The authors wish to thank Professor M.M. Altamura (Università “La Sapienza”, Rome, Italy) for helpful discussion. We also thank C. Castellacci for technical assistance and M.I. Augeri for helping in figure preparation. This research was supported by the Ministero della Pubblica Istruzione, Italy.

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Angelini, R., Manes, F. & Federico, R. Spatial and functional correlation between diamine-oxidase and peroxidase activities and their dependence upon de-etiolation and wounding in chick-pea stems. Planta 182, 89–96 (1990). https://doi.org/10.1007/BF00239989

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  • DOI: https://doi.org/10.1007/BF00239989

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