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Effect of calcium, its inhibitors, and heavy metals on the growth cycle of peanut cell aggregates

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Abstract

During the normal growth cycle of peanut (Arachis hypogaea L.) cells, cultured in suspension medium, cell aggregates of <0.5 mm were formed during the log phase and grew to aggregates of >0.5 mm during late growth phase. Calmodulin rose to its original level during <0.5 mm aggregate formation following an initial 50% drop. Observations by UV microscopy showed that calmodulin. Ca2+ was centered in intense fluorescent sites. Calmodulin antagonists and a calcium chelator inhibited <0.5 mm aggregate formation as well as protein accumulation. The chelator suppressed cationic peroxidase isozyme release, while the antagonists had some partial effect on the anionic isozyme. Some heavy metals such as cadmium, mercury, lead and cobalt at low concentrations would allow continued growth of >0.5 but not of the <0.5 populations. At high (1 mM) concentrations these ions caused arrested growth. At low (10 μM) levels and in the presence of 3 mM calcium they had a synergistic effect.

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Abbreviations

AOA:

amino oxy acetic acid

BCA:

big cell aggregates

CPZ:

chlorpromazine

EGTA:

ethylene glycol bis (β-aminoethyl ether)

N, N, N′, N′:

tetra acetic acid

SCA:

small cell aggregates

TFP:

trifluoperazine

References

  • Allan E & Hepler PK (1989) Calmodulin and calcium binding proteins. In: Marcus A (Ed) The Biochemistry of Plants: A Comprehensive Treatise. Vol 15 (pp 455–484), Academic Press, San Diego

    Google Scholar 

  • Allan E & Trewavas AJ (1985) Quantitative changes in the calmodulin and NAD kinase during early cell development in the root apex of Pisum sativum L. Planta 165: 493–501

    Google Scholar 

  • Burns JK & Evensen KB (1986) Calcium effects on the ethylene, carbon dioxide and 1-aminocyclopropane-1-carboxylic synthase activity. Physiol. Plant. 66: 609–615

    Google Scholar 

  • Burns JK & Pressay R (1987) Ca2+ in cell walls of ripening tomato and peach. J. Amer. Soc. HortScience 112: 783–787

    Google Scholar 

  • Chao SH, Suzuki Y, Zysk JR & Cheung WY (1984) Activation of calmodulin by various metal ions as a function of ionic radii. Mol. Pharmacol. 26: 75–82

    Google Scholar 

  • Chafouleas JG, Bolton WE, Hidaka H, BoydIII AE & Means AR (1982) Calmodulin and the cell cycle: Involvement in regulation of cell-cycle progression. Cell 28: 41–50

    Google Scholar 

  • Chafouleas JG, Lagace L, Bolton WE, BoydIII AE & Means AR (1984) Changes in calmodulin and its mRNA accompany re-entry of quiescent cells into the cell cycle. Cell 36: 73–81

    Google Scholar 

  • Cheung WY (1980) Calmodulin plays a pivotal role in cellular regulation. Science 207: 19–27

    Google Scholar 

  • Cheung WY (1984) Calmodulin: Its potential role in cell proliferation and heavy metal toxicity. Feder. Proc. 43: 2995–2999

    Google Scholar 

  • Eklund & Eliasson L (1990) Effects of calcium ion concentration on cell wall synthesis. J. Exptl. Bot. 41: 863–867

    Google Scholar 

  • Ferguson IB (1984) Calcium in plant senesence and fruit ripening. Plant Cell Environ. 7: 477–489

    Google Scholar 

  • Gilroy S, Blower DP & Trewavas AJ (1987) Calcium a regulation system emerges in plant cells. Development 100: 181–184

    Google Scholar 

  • Goddard RH & LaClaireII JW (1991) Calmodulin and wound healing in the coenocytic green algae Ernodesmis verticulata. Planta 183: 281–293

    Google Scholar 

  • Hazelton B, Mitchell B & Tupper T (1979) Calcium, magnesium and growth control in the WI-38 human fibroblast cell. Cell Biol. 83: 487–498

    Google Scholar 

  • Hernandez-Nistal J, Aldasaro JJ, Roderiquez D, Babiano J & Nicolas G (1986) Intracellular localization of calmodulin on embryonic axis of Cicer arietinum L. In: Trewavas AJ (Ed) Molecular and Cellular Aspects of Calcium in Plant Development (pp 313–315). Plenum Publ. Co. New York

    Google Scholar 

  • Hu C, Carbonera D & vanHuystee RB (1987a) Production and preliminary characterization of monoclonal antibodies against cationic peanut peroxidase. Plant Physiol. 85: 299–303

    Google Scholar 

  • Hu C, Lee D, Chibbar RN & vanHuystee RB (1987b) Ca2+ and peroxidase derived from cultured peanut cells. Physiol. Plant. 70: 99–102

    Google Scholar 

  • Kauss H (1987) Home aspects of calcium-dependent regulation in plant metabolism. Ann. Review Plant Physiol. 38: 47–72

    Google Scholar 

  • Kevers C, Sticher L, Penel C, Greppin H & Gaspar Th (1982) Calcium controlled peroxidase secretion by sugarbeet suspension in relation to habituation. Plant Growth Regul. 1: 61–66

    Google Scholar 

  • Lowry GH, Rosebrough HL, Farr L & Randall RJ (1951) Protein measurement with folin phenol reagent. J. Biol. Chem. 193: 265–275

    Google Scholar 

  • Lui Y, Wu Y, Xu Y & Zhou X (1990) The changes of ethylene production and calmodulin content in IAA-treated etiolated mungbean hypocotyl. Acta Botanica Sinica 32: 695–701

    Google Scholar 

  • Mackensie IA & Street HE (1970) Studies on the growth in culture of plant cells VIII. The production of ethylene by suspension cultures of Acer pseudoplatanus L. J. Exptl. Bot. 21: 824–834

    Google Scholar 

  • Mattoo AK, Adams DO, Patterson GW & Lieberman M (1982) Inhibition of 1-aminocyclopropane-1-carboxylic acid synthase by phenothiazine. Plant Science Lett. 28: 173–179

    Google Scholar 

  • Mazzei GJ, Girard PR & Kuo JF (1984) Environmental pollutant Cd2+ biphasically and differentially regulates myosin light chain kinase and phospholipid/Ca2+-dependent protein kinase. FEBS Lett. 173: 124–128

    Google Scholar 

  • Means AR, Tash JS & Chafousleas JG (1982) Physiological implications of the presence, distribution and regulation of calmodulin in eukaryotic cells. Physiol. Rev. 62: 1–39

    Google Scholar 

  • Morishima I, Kurono M & Shiro Y (1986) Presence of endogenous calcium ion in horseradish peroxidase. Elucidation of metal-binding site by substitution of divalent and lathanide ions for calcium and the use of metal-induced NMR (1h and 113Cd) resonances. J. Biol. Chem. 261: 9391

    Google Scholar 

  • Muto S, Miyachi S (1984) Production of antibody against spinach calmodulin and its application to radioimmunoassay for plant calmodulin. Z. Pflanzenphysiol. 114: 421–431

    Google Scholar 

  • Muto S & Takayasu H (1987) Inhibition of adventitious root growth in Tradescantia by calmodulin antagonists and calcium inhibitors. Plant Cell Physiol. 28: 1569–1574

    Google Scholar 

  • Perrino BA & Chou IN (1986) Role of calmodulin in cadmium-induced microtubule dissembly. Cell Biol. Intern. Rep. 10: 565–573

    Google Scholar 

  • Piazza GJ (1988) Calmodulin in plants. In: Thompson MP (Ed) Calcium Binding Proteins (1: 127–143). CRC Press

  • Pietrobon D, Virgilio FO & Pozzea T (1990) Structural and functional aspects of calcium homeostasis in eukaryotic cells. Eur. J. Biochem. 193: 599–622

    Google Scholar 

  • Reddy GN & Prasad MNV (1989) Cadmium inducible proteins in Scenedesmus guadricauda. Current Science 58: 1380–1382

    Google Scholar 

  • Small JGC, Botha FC, Pretorius JC & Hoffman E (1991) Evidence for ethylene requirement to reduce soaking injury in bean seeds and the beneficial effect of heavy metals. J. Exptl. Bot. 42: 277–280

    Google Scholar 

  • Saunders MJ & Hepler PK (1981) Localization of membrane associated calcium following cytokinin treatment in Funeria using chlorotetracycline. Planta 152: 272–281

    Google Scholar 

  • Saunders MJ & Hepler PK (1982) Ca2+ ionophore A-23187 stimulates cytokinin-like mitosis in Funeria. Science 217: 943–945

    Google Scholar 

  • Saunders MJ & Hepler PK (1983) Calcium antagonists and calmodulin inhibitors block cytokinin-induced bud formation in Funeria. Developmental Biol. 99: 41–49

    Google Scholar 

  • Sotiroudis TG (1986) Lanthanide ions and Cd2+ are able to substitute for Ca2+ in regulating phosphorylase kinase. Biochem. Intern. 13: 59–64

    Google Scholar 

  • Suzuki Y, Chao SH, Zysk JR & Cheung WY (1985) Stimulation of calmodulin by cadmium. Arch. Toxicol. 57205–57211

  • Tupper JT, Kaufman L & Bodine PV (1980) Related effects of calcium and serum on the C1 phase of the human WI-38 fibroblast. J. Cell Physiol. 104: 97–103

    Google Scholar 

  • Sesto PA & vanHuystee RB (1989) Purification and yield of a cationic peroxidase from a peanut suspension cell culture. Plant Sci. 61: 163–168

    Google Scholar 

  • vanHuystee RB, Xu Y & O'donnell JP (1992) Variation in soret band absorption of peroxidase due to calcium. Plant Physiol. Biochem. 30(3) 293–297

    Google Scholar 

  • Vantard M, Lambert AM, DeMey J, Picquot P & VanEldik LJ (1985) Characterization and immunocytological distribution of calmodulin in higher plant endosperm cells: Localization in the mitotic apparatus. J. Cell Biol. 101: 488–499

    Google Scholar 

  • Weast RC & Astle MJ (1981) Handbook of Chemistry and Physics. 62nd edition (F-285). CRC Press, Boca Raton, FL

    Google Scholar 

  • Wick SM, Muto S & Duniec J (1985) Double immunofluorescence labelling of calmodulin and tubulin in dividing plant cells. Protoplasma 126: 198–206

    Google Scholar 

  • Xu Y, Lu L, Zhou X, Chao S, Yu H & Zhang M (1988) Preparation of the enzyme-linked-immuno-sorbent-assay kit for calmodulin. J. Nanjing Agricultural University 11: 32–42

    Google Scholar 

  • Xu Y, Hu C & vanHuystee RB (1990) Quantitative determination of a peanut anionic peroxidase by specific monoclonal antibodies. J. Exptl. Bot. 41: 1479–1488

    Google Scholar 

  • Xu Y & van Huystee RB (1992) Association of calcium and calmodulin to peroxidase secretion. J. Plant Physiol. (in press)

  • Yang SF (1980) Regulation of ethylene synthesis. Hortscience 15: 238–243

    Google Scholar 

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Xu, Y., van Huystee, R.B. Effect of calcium, its inhibitors, and heavy metals on the growth cycle of peanut cell aggregates. Plant Cell Tiss Organ Cult 32, 319–328 (1993). https://doi.org/10.1007/BF00042295

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