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1997 | 19 | 4 |

Tytuł artykułu

Plant cell responses to heavy metals: molecular and physiological aspects

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
The effect of lead, cadmium and cooper on protein pattern, free radicals and antioxidant enzymes in root of Lupinus luteus L. were investigated. Heavy metals inhibited growth of lupin roots, which was accompanied by increased synthesis and accumulation of a 16 kDa polypeptide (Przymusiński et al. 1991 Biochem. Physiol. Pflanzen., 187:51–57). This component has been earlier identified as immunologically related to Cu,Zn-superoxide dismutase (Przymusiński et al. 1995 Env.Exp.Bot., 35:485–495). However, more detailed study revealed that this stress-stimulated protein is composed of four to six polypeptides of different electrophoretic mobility. The most abundant polypeptides of the 16kDa region were found to be closely homologous to pathogen related proteins. The number and intensity of these polypeptides was highly variable in roots of individual seedlings, which suggests that they might represent separate allelic forms. Electron paramagnetic spectra revealed that at low lead concentrations the amplitude of the first derivative was similar to the control and distinctly increased at higher metal concentrations. On the other hand, at the lower lead concentrations the activity of antioxidant enzymes increased, whereas at higher metal doses the enzyme activities did not raise further (SOD) or even dropped (CAT, APOX). This implies that the responses of antioxidant system to lead is dose-dependent stimulated by low metal concentrations, whereas at the higher metal level the free radical emission is beyond the quenching capacity of antioxidant enzymes, which in turn might contribute to the reduced root growth. The effect of various heavy metals: Pb²⁺, Cd²⁺ and Cu²⁺ on phytochelatins and antioxidant enzymes depends on the kind of metal ion. Pb²⁺ and Cd²⁺ stimulated the PCs formation whereas Cu²⁺ was not effective. On the other hand, in root exposed to Cu the activity of catalase (CAT) was the highest as was the production of H₂O₂. The strong oxidative effect of Cu²⁺ ions which were not complexed by PCs suggests that these peptides might by involved in the cellular defense system by binding excessive heavy metal ions. On the basis of our results it can be concluded that in lupin roots exposed to heavy metals there is a complex defense system against metal phytotoxicity, which comprises of specific proteins, antioxidant enzymes and phytochelatins.

Wydawca

-

Rocznik

Tom

19

Numer

4

Opis fizyczny

p.459-465,fig.

Twórcy

autor
  • A.Mickiewicz University, Niepodleglosci 14, 61-713 Poznan, Poland
autor
autor

Bibliografia

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  • Becana M., Aparci-Tejo P., Irigoyen J. J., Sanchez-Diaz M. 1986. Some enzymes of hydrogen peroxide metabolism in leaves and root nodules of Medicago sativa. Plant Physiol. 82:1160–1171.
  • Breitender H., Pettenburger K., Bito A., Valenta R., Kraft D., Rumpold H., Scheiner O., Breitenbach M. 1989. The gene coding for the major birth pollen allergen BetvI, is highly homologous to a pea disease resistance response gene. EMBO J. 8: 1935–1938.
  • Davis B. J. 1964. Disc electrophoresis-II: method an application to human serum proteins. Ann. of New York Acad. Sci. 121: 404–427.
  • Grill E., Winnacker E.-L., Zenk M. H. 1987. Phytochelatins, a class of heavy-metal-binding peptides from plants, are functionally analogous to metallothoioneins. Proc. Nat. Acad. Sci. USA. 84: 517–524.
  • Harborne J.B. 1989. Introduction to Ecological Biochemistry, Academic Press Harcourt Brace Jovanovich, Publishers.
  • Mittler R., Zilinskas B. A. 1993. Detection of ascorbate peroxidase activity in native gels by inhibition of the ascorbate-dependent reduction of nitroblue tetrazolium. Anal. Bioch. 212, 540–546.
  • Moiseyev G.P., Fedoreyeva L.I., Zhuravlev Y.N., Yasnetskaya E., Jakel P.A., Beintema J.J. 1997. Primary structures of two ribonucleases from ginseng calluses. New members of the PR-10 family of intracellular pathogenesis-related plant proteins. FEBS Lett. 407: 207–210.
  • Pinto M.P., Ricardo C.P.P. 1995. Lupinus albus L. pathogenesis related proteins that show similarity to PR-10 proteins. Plant Physiol., 109: 1345–1352.
  • Przymusiński R., Spychała M., Gwóźdź E. A. 1991. Inorganic lead changes growth and polypeptide pattern of lupin roots. Biochem. Physiol. Pflanzen, 187: 51–57.
  • Przymusiński R., Gwóźdź E. A. 1994. Increased accumulation of the 16×103 Mr połypeptide in lupin roots exposed to lead, copper and nitrate ions. Environ. Exp. Bot., 34: 63–68.
  • Przymusiński R., Rucińska R., Gwóźdź E. A. 1995. The stress-stimulated 16kDa polypeptide from lupin roots has properties of cytosolic Cu:Zn-Superoxide dismutase. Environ. Exp. Bot., 35: 485–495.
  • Przymusiński R., Gwóźdź E. A., Ohlsson P.-I. 1996. Identification of PR proteins and SOD among polypeptides of lupin roots exposed to heavy metal ions. Plant Physiol.Biochem., Special issue. 10th FESPP Congress, pp.258.
  • Robinson N.J., Urwin P.E., Robinson P.J., Jackson P.J. 1994. Gene expression in relation to metal toxicity and tolerance. In Stress-Induced Gene Expression in Plants, ed. A.S. Basra, Harwood Academic Publisher: 209–248
  • Sikorski M.M., Szlagowska A.E., Legocki A.B. 1995. cDNA sequences encoding for two homologues of Lupinus luteus (L.) IPR-like proteins (Accession No. X79974 and X79975 for LIR18A and LIR18B mRNA=s respectively) Plant Physiol. 110: 335.
  • Tukendorf A., Rauser W. E. 1990. Changes in glutathione and phytochelatins in roots of maize seedlings exposed to cadmium. Plant Sci. 70: 155–166.
  • Vangronsveld J., Clijsters H. 1994. Toxic Effect of Metals. In Plants and the Chemical Elements, ed by M. G. Farago, VCH Weinheim New York Basel Cambridge Tokyo:149–177.
  • Woodbury W., Spencer A. K., Stahmann M. A. 1971. An improved procedure using ferricyanide for detecting catalase isozymes. Analytical Biochemistry, 44: 301–305.
  • Wilkins D.A. 1957. A technique for the measurement of lead tolerance in plants. Nature 180: 37–38.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-article-95704a9a-9e87-4b19-9808-244641873c9e
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