Skip to main content
PMC home page
Plant Physiology logoLink to Plant Physiology
. 1997 Feb;113(2):411–418. doi: 10.1104/pp.113.2.411

Natural Senescence of Pea Leaves (An Activated Oxygen-Mediated Function for Peroxisomes).

G M Pastori 1, L A Del Rio 1
PMCID: PMC158155  PMID: 12223615

Abstract

We studied the activated oxygen metabolism of peroxisomes in naturally and dark-induced senescent leaves of pea (Pisum sativum L.). Peroxisomes were purified from three different types of senescent leaves and the activities of different peroxisomal and glyoxysomal enzymes were measured. The activities of the O2-- and H2O2-producing enzymes were enhanced by natural senescence. Senescence also produced an increase in the generation of active oxygen species (O2- and H2O2) in leaf peroxisomes and in the activities of two glyoxylate-cycle marker enzymes. A new fraction of peroxisomes was detected at an advanced stage of dark-induced senescence. Electron microscopy revealed that this new peroxisomal fraction varied in size and electron density. During senescence, the constitutive Mn-superoxide dismutase (SOD) activity of peroxisomes increased and two new CuZn-SODs were induced, one of which cross-reacted with an antibody against glyoxysomal CuZn- SOD. This fact and the presence of glyoxylate-cycle enzymes support the idea that foliar senescence is associated with the transition of peroxisomes into glyoxysomes. Our results indicate that natural senescence causes the same changes in peroxisome-activated oxygen metabolism as dark-induced senescence, and reinforce the hypothesis of an effective role of peroxisomes and their activated oxygen metabolism in this stage of the life cycle.

Full Text

The Full Text of this article is available as a PDF (1.1 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Aebi H. Catalase in vitro. Methods Enzymol. 1984;105:121–126. doi: 10.1016/s0076-6879(84)05016-3. [DOI] [PubMed] [Google Scholar]
  2. Beauchamp C., Fridovich I. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal Biochem. 1971 Nov;44(1):276–287. doi: 10.1016/0003-2697(71)90370-8. [DOI] [PubMed] [Google Scholar]
  3. Boveris A., Oshino N., Chance B. The cellular production of hydrogen peroxide. Biochem J. 1972 Jul;128(3):617–630. doi: 10.1042/bj1280617. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bradford 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 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  5. Del Río L. A., Fernández V. M., Rupérez F. L., Sandalio L. M., Palma J. M. NADH Induces the Generation of Superoxide Radicals in Leaf Peroxisomes. Plant Physiol. 1989 Mar;89(3):728–731. doi: 10.1104/pp.89.3.728. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Flatmark T., Christiansen E. N., Kryvi H. Polydispersity of rat liver peroxisomes induced by the hypolipidemic and carcinogenic agent clofibrate. Eur J Cell Biol. 1981 Apr;24(1):62–69. [PubMed] [Google Scholar]
  7. Goglia F., Liverini G., Lanni A., Iossa S., Barletta A. Morphological and functional modifications of rat liver peroxisomal subpopulations during cold exposure. Exp Biol. 1989;48(3):127–133. [PubMed] [Google Scholar]
  8. Graham I. A., Leaver C. J., Smith S. M. Induction of Malate Synthase Gene Expression in Senescent and Detached Organs of Cucumber. Plant Cell. 1992 Mar;4(3):349–357. doi: 10.1105/tpc.4.3.349. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Just W. W., Hartl F. U., Schimassek H. Rat liver peroxisomes. I. New peroxisome population induced by thyroid hormones in the liver of male rats. Eur J Cell Biol. 1982 Feb;26(2):249–254. [PubMed] [Google Scholar]
  10. King G. A., Davies K. M., Stewart R. J., Borst W. M. Similarities in Gene Expression during the Postharvest-Induced Senescence of Spears and Natural Foliar Senescence of Asparagus. Plant Physiol. 1995 May;108(1):125–128. doi: 10.1104/pp.108.1.125. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Levine A., Tenhaken R., Dixon R., Lamb C. H2O2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response. Cell. 1994 Nov 18;79(4):583–593. doi: 10.1016/0092-8674(94)90544-4. [DOI] [PubMed] [Google Scholar]
  12. López-Huertas E., Sandalió L. M., Del Rio L. A. Superoxide generation in plant peroxisomal membranes: characterization of redox proteins involved. Biochem Soc Trans. 1996 May;24(2):195S–195S. doi: 10.1042/bst024195s. [DOI] [PubMed] [Google Scholar]
  13. Prasad T. K., Anderson M. D., Martin B. A., Stewart C. R. Evidence for Chilling-Induced Oxidative Stress in Maize Seedlings and a Regulatory Role for Hydrogen Peroxide. Plant Cell. 1994 Jan;6(1):65–74. doi: 10.1105/tpc.6.1.65. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Sautter C., Bartscherer H. C., Hock B. Separation of plant cell organelles by zonal centrifugation in reorienting density gradients. Anal Biochem. 1981 May 1;113(1):179–184. doi: 10.1016/0003-2697(81)90062-2. [DOI] [PubMed] [Google Scholar]
  15. Schwitzguebel J. P., Siegenthaler P. A. Purification of peroxisomes and mitochondria from spinach leaf by percoll gradient centrifugation. Plant Physiol. 1984 Jul;75(3):670–674. doi: 10.1104/pp.75.3.670. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. del Río L. A., Palma J. M., Sandalio L. M., Corpas F. J., Pastori G. M., Bueno P., López-Huertas E. Peroxisomes as a source of superoxide and hydrogen peroxide in stressed plants. Biochem Soc Trans. 1996 May;24(2):434–438. doi: 10.1042/bst0240434. [DOI] [PubMed] [Google Scholar]
  17. del Río L. A., Sandalio L. M., Palma J. M., Bueno P., Corpas F. J. Metabolism of oxygen radicals in peroxisomes and cellular implications. Free Radic Biol Med. 1992 Nov;13(5):557–580. doi: 10.1016/0891-5849(92)90150-f. [DOI] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES