Journal of Plant Biotechnology

The Korean Society of Plant Biotechnology (한국식물생명공학회)
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Stress-induced Activity of Matrix Metalloproteinase in Tobacco Plants

담배식물체에서 스트레스에 따른 Matrix Metalloproteinase의 활성

  • Published : 2004.12.01
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Abstract

Matrix metalloproteinases (MMPs) are zinc-dependent endopeptidases produced by a variety of cell type, and have a fundamental role in the degradation and remodeling of extracellular matrix. In this study, we screened the secretion of MMPs in leaves of different developmental stages and in response to environmental stress using tobacco. Compare with fully maturing leaves and older leaves, the rate of MMPs activity was high in expanding and younger leaves. It is tempting to speculate that MMPs may be involved in tissue modeling, which must occur during leaf expansion. The MMPs activity in tobacco leaves grown in the presence of stressors showed a significantly increase at salinity treatment and pathogen infection. The MMPs activity in salinity and pathogen treatment increased respectively, by 1.2- and 1.5-fold with respect to the control. These results suggest that MMPs may be involved in plant defence against adverse environment and pathogenic infection.

MMPs는 $Zn^{2+}$-의존성 endopeptidase로서 세포외 기질을 분해하는 능력을 갖고 있다. 본 연구에서는 담배식물체에서 잎의 발생단계별로 분비되는 MMPs의 활성과 환경 스트레스에 의한 MMPs의 활성을 조사하였다. 그 결과 MMPs의 활성은 기부 부위의 완전히 성숙한 잎보다 엽신의 확장이 일어나고 있는 어린잎에서 높았다. 이는 식물체에서 잎 신장을 위한 세포내 공간 형성 및 조직재구성에 MMPs가 중요한 단백질분해효소로 작용함을 시사하였다. 또한 환경 스트레스에 대한 반응으로서 MMPs의 활성을 조사한 결과 염처리와 병원균 감염에 의해 각각 1.2배와 1.5배의 증가를 보였다. 이러한 결과는 식물체가 발생단계 외에도 불리한 환경에 대한 방어 수단으로 MMPs가 생성 분비함을 알 수 있었다.

Keywords

References

  1. Birkedal-Hansen H (1995) Proteolytic remodeling of extracellular matrix. Curr Opin Cell Biol 7: 728-735 https://doi.org/10.1016/0955-0674(95)80116-2
  2. Borkakoti N (2000) Structural studies of matrix metalloproteinases. J Mol Med 78: 261-268 https://doi.org/10.1007/s001090000113
  3. Bradford MM (1976) 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 https://doi.org/10.1016/0003-2697(76)90527-3
  4. Delorme VG, McCabe PF, Kim DJ, Leaver CJ (2000) A matrix metalloproteinase gene is expressed at the boundary of senescence and programmed cell death in cucumber. Plant Physiol 123: 917-27 https://doi.org/10.1104/pp.123.3.917
  5. Flowers TJ, Troke PE, Yeo AR (1985) The mechanism of salt tolerance in halophytes. Ann Rev Plant Physiol 28: 89-121
  6. Frederic J and Woessner JF Jr (1998) The matrix metalloproteinase family. In: Parks WC, RP Mecham RP, (eds), Matrix metalloproteinase, Academic Press, London, pp 1-14
  7. Glazebrook J (1999) Genes controlling expression of defense responses in Arabidopsis. Curr Opin Plant Biol 2: 280-286 https://doi.org/10.1016/S1369-5266(99)80050-8
  8. Golldack D, Popova OV, Dietz KJ (2002) Mutation of the matrix metalloproteinase At2-MMP inhibits growth and causes late flowering and early senescence in Arabidopsis. J Biol Chem 277: 5541-5547 https://doi.org/10.1074/jbc.M106197200
  9. Graham JS, Xiong J, Gillikin JW (1991) Purification and developmental analysis of a metalloproteinase from leaves of Glycine max. Plant Physiol 97: 786-792 https://doi.org/10.1104/pp.97.2.786
  10. Greenway H, Munns R (1980) Mechanism of salt tolerance in nonhalopytes. Ann Rev Plant Physiol 31: 149-190 https://doi.org/10.1146/annurev.pp.31.060180.001053
  11. Gussarson M, H Asp, Adalsteinsson S, Jensen P(1996) Enhancement of cadmium effects on growth and nutrient composition of birch (Betula pendula) by buthionine sulphoximine (BSO). J Exp Bot 47: 211-215 https://doi.org/10.1093/jxb/47.2.211
  12. Lease K, Ingham E, Walker JC (1998) Challenges in understanding RLK function. Curr Opin Plant Biol 1: 388-392 https://doi.org/10.1016/S1369-5266(98)80261-6
  13. Liu Y, Dammann C, Bhattacharyya MK (2001) The matrix metalloproteinase gene GmMMP2 is activated in response to pathogenic infections in soybean. Plant Physiol 127: 1788-1797 https://doi.org/10.1104/pp.010593
  14. Maidment JM, Moore D, Murphy GP, Murphy G, Clark IM (1999) Matrix metalloproteinase homologues from Arabidopsis thaliana. Expression and Activity. J Biol Chem 274: 34706-134710 https://doi.org/10.1074/jbc.274.49.34706
  15. Matrisian LM (1992) The matrix-degrading metalloproteinases. BioAssays 14: 455-463 https://doi.org/10.1002/bies.950140705
  16. Murashige T, Skoog F (1962) A revised medium for rapid growth and bioassays with tobacco tissue culture. Physiol Plant 15: 473-497 https://doi.org/10.1111/j.1399-3054.1962.tb08052.x
  17. Ouchi S. (1983) Induction of resistance or susceptibility. Annu Rev Phytopathol 21: 289-315 https://doi.org/10.1146/annurev.py.21.090183.001445
  18. Pak JH, Liu CY, Huangpu J, Graham JS (1997) Construction and characterization of the soybean leaf metalloproteinase cDNA. FEBS Lett 404: 283-288 https://doi.org/10.1016/S0014-5793(97)00141-5
  19. Satterlee JS, Sussman MR (1998) Unusual membrane-associated protein kinases in higher plants. J Membr Biol 164: 205-213 https://doi.org/10.1007/s002329900406
  20. Sequeira L (1983) Mechanisms of induced resistance in plants. Annu Rev Microbiol 37: 51-79 https://doi.org/10.1146/annurev.mi.37.100183.000411
  21. Shah J, Kachroo P, Klessig DF (1999) The Arabidopsis ssi1 mutation restores pathogenesis-related gene expression in npr1 plants and renders defensin gene expression salicylic acid dependent. Plant Cell 11: 191-206 https://doi.org/10.1105/tpc.11.2.191
  22. Somashekaraiah BV, Padmaja K, Prasad ARK (1992) Phytotoxicity of cadmium ions on germinating seedlings of mung bean (Phaseolus vulgaris): involvement of lipides in chlorophyll degradation. Physiol Plant 85: 85-89 https://doi.org/10.1111/j.1399-3054.1992.tb05267.x
  23. Wagner GJ (1993) Accumulation of cadmium in crop plants and its consequences to human health. Adv Agron 51: 173-212 https://doi.org/10.1016/S0065-2113(08)60593-3
  24. Wang Y, Johnson AR, Ye QZ, Dyer RD (1999) Catalytic activities and substrate specificity of the human membrane type 4 matrix metalloproteinase catalytic domain. J Biol Chem 274: 33043-33049 https://doi.org/10.1074/jbc.274.46.33043
  25. Woessner JF Jr (1998) Role of matrix proteases in processing enamel proteins. Connect Tissue Res 39: 69-73 https://doi.org/10.3109/03008209809023913
  26. Zhou HE, Zhang X, Nothnick WB (2004) Disruption of the TIMP-1 gene product is associated with accelerated endometrial gland formation during early postnatal uterine development. Biol Reprod 71: 534-539 https://doi.org/10.1095/biolreprod.104.029181