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. 1996 Jun;111(2):569–576. doi: 10.1104/pp.111.2.569

Differential Expression of Lipoxygenase Isoenzymes in Embryos of Germinating Barley.

W L Holtman 1, G Van Duijn 1, NJA Sedee 1, A C Douma 1
PMCID: PMC157868  PMID: 12226311

Abstract

Expression of lipoxygenase was studied in barley (Hordeum distichum L.) embryos during germination. Total lipoxygenase activity was high in quiescent grains, dropped during the 1st d of germination, and subsequently increased to a level similar to that in quiescent grains. The contribution of two isoenzymes, lipoxygenases 1 (LOX-1) and 2 (LOX-2), was studied at the activity, protein, and mRNA levels. Activity ratios of the two isoforms were determined via the ratio of 9- and 13-hydroperoxides, which are formed from linoleic acid. Isoenzyme protein levels were determined using specific monoclonal antibodies. mRNA levels were studied using the specific cDNA probes LoxA and LoxC, which correspond to LOX-1 and LOX-2, respectively. The major difference in temporal expression of LOX-1 and LOX-2 was observed in quiescent grains. At this stage, LOX-1 contributed almost exclusively to total lipoxygenase activity. LOX-2 activity rapidly increased until d 2 of germination. From this time point onward, LOX-1 and LOX-2 showed similar patterns at both activity and protein levels. The tissue distribution of the two isoenzymes in the germinating embryo was closely similar, with the highest expression levels in leaves and roots. The levels of LOX-1 and LOX-2 may be regulated mainly pretranslationally, as suggested by the similarity of the protein and mRNA patterns corresponding to the two isoforms.

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Selected References

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  1. Creelman R. A., Tierney M. L., Mullet J. E. Jasmonic acid/methyl jasmonate accumulate in wounded soybean hypocotyls and modulate wound gene expression. Proc Natl Acad Sci U S A. 1992 Jun 1;89(11):4938–4941. doi: 10.1073/pnas.89.11.4938. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Doderer A., Kokkelink I., van der Veen S., Valk B. E., Schram A. W., Douma A. C. Purification and characterization of two lipoxygenase isoenzymes from germinating barley. Biochim Biophys Acta. 1992 Mar 27;1120(1):97–104. doi: 10.1016/0167-4838(92)90429-h. [DOI] [PubMed] [Google Scholar]
  3. Feussner I., Kindl H. A lipoxygenase is the main lipid body protein in cucumber and soybean cotyledons during the stage of triglyceride mobilization. FEBS Lett. 1992 Feb 24;298(2-3):223–225. doi: 10.1016/0014-5793(92)80062-l. [DOI] [PubMed] [Google Scholar]
  4. Gardner H. W. Recent investigations into the lipoxygenase pathway of plants. Biochim Biophys Acta. 1991 Jul 30;1084(3):221–239. doi: 10.1016/0005-2760(91)90063-n. [DOI] [PubMed] [Google Scholar]
  5. Inman R. D., Gallegos K. V., Brause B. D., Redecha P. B., Christian C. L. Clinical and microbial features of prosthetic joint infection. Am J Med. 1984 Jul;77(1):47–53. doi: 10.1016/0002-9343(84)90434-0. [DOI] [PubMed] [Google Scholar]
  6. Kato T., Ohta H., Tanaka K., Shibata D. Appearance of new lipoxygenases in soybean cotyledons after germination and evidence for expression of a major new lipoxygenase gene. Plant Physiol. 1992 Jan;98(1):324–330. doi: 10.1104/pp.98.1.324. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Maccarrone M., Veldink G. A., Vliegenthart J. F. Phytochrome control and anoxia effect on the activity and expression of soybean seedling lipoxygenases 1 and 2. FEBS Lett. 1991 Oct 7;291(1):117–121. doi: 10.1016/0014-5793(91)81117-q. [DOI] [PubMed] [Google Scholar]
  8. Schewe T., Rapoport S. M., Kühn H. Enzymology and physiology of reticulocyte lipoxygenase: comparison with other lipoxygenases. Adv Enzymol Relat Areas Mol Biol. 1986;58:191–272. doi: 10.1002/9780470123041.ch6. [DOI] [PubMed] [Google Scholar]
  9. Smith P. K., Krohn R. I., Hermanson G. T., Mallia A. K., Gartner F. H., Provenzano M. D., Fujimoto E. K., Goeke N. M., Olson B. J., Klenk D. C. Measurement of protein using bicinchoninic acid. Anal Biochem. 1985 Oct;150(1):76–85. doi: 10.1016/0003-2697(85)90442-7. [DOI] [PubMed] [Google Scholar]
  10. Tranbarger T. J., Franceschi V. R., Hildebrand D. F., Grimes H. D. The soybean 94-kilodalton vegetative storage protein is a lipoxygenase that is localized in paraveinal mesophyll cell vacuoles. Plant Cell. 1991 Sep;3(9):973–987. doi: 10.1105/tpc.3.9.973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Yamamoto S. "Enzymatic" lipid peroxidation: reactions of mammalian lipoxygenases. Free Radic Biol Med. 1991;10(2):149–159. doi: 10.1016/0891-5849(91)90008-q. [DOI] [PubMed] [Google Scholar]

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