Effect of Na+ on Ca2+-Binding on the Plasma Membrane of Barley Mesophyll Cells: an Electrophoretic Study

Murata, Yoshiyuki; Fujita, Masashi; Nakatani, Takuya; Obi, Ichiro; Kakutani, Tadaaki

doi:10.1093/oxfordjournals.pcp.a029390

Cited by 8 publications

(16 citation statements)

References 14 publications

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“…In our previous paper (Murata et al 1998a), we found that Na + ions reduced approximately the same amount of Ca 2+ bound to PM of salt-tolerant barley mesophyll protoplasts as K + ions did, that is, Na + did not specifically decrease the amount of Ca 2+ bound to PM of salt-tolerant plants. These results seem to imply that the susceptibility of PM to Na + -specifically inducing desorption of membrane-bound Ca 2+ may be related to the degree of salt tolerance of plant species.…”

Section: Introductionmentioning

confidence: 62%

“…In this study, we measured the amounts of Ca 2+ bound to the outer surface of PM for NaCladapted and NaCl-unadapted tobacco cells using electrophoresis and compared effects of salinity (Na + ions) on Ca 2+ binding in NaCl-adapted cells with those in NaCl-unadapted cells. NaCl-adapted cells used here had acquired a higher degree of salt tolerance compared with NaCl-unadapted cells (Murata et al 1998a, Murata et al 1994b).…”

Section: Introductionmentioning

confidence: 84%

“…The surface concentrations of ions were calculated from the corresponding bulk concentrations using Boltzmann equation. Other details of the electrophoretic measurements and data analysis were described in our previous papers (Obi et al 1989, Murata et al 1998a.…”

Section: Electrophoresismentioning

confidence: 99%

“…These results seem to imply that the susceptibility of PM to Na + -specifically inducing desorption of membrane-bound Ca 2+ may be related to the degree of salt tolerance of plant species. Therefore, comparative studies using salt-tolerant and salt-sensitive plant cells would allow us to elucidate more clearly the significance of our results (Murata et al 1998a) in salt tolerance. However, there are no comparative studies on Ca 2+ binding to PM using salt-adapted (tolerant) and salt-unadapted (sensitive) plant cells.…”

Section: Introductionmentioning

confidence: 99%

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Alterations in Ca2+-Binding on Plasma Membrane after Adaptation to Salt Stress of Tobacco Cells in Suspension

Murata¹,

Katsura²,

Obi³

et al. 2000

Plant and Cell Physiology

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Electrophoresis was used to study effects of salinity on the characteristics of Ca2+ binding to the outer surface of plasma membrane (PM) of protoplasts isolated from two types of tobacco (Nicotiana tabacum L., cv. Bright Yellow) cultured cells that were adapted (tolerant) and unadapted (sensitive) to 50 mM NaCl stress. Electrophoretic analysis of salt-sensitive NaCl-unadapted cells shows that Na+ induced an appreciably higher degree of reduction in the amount of Ca2+ bound to PM compared with K+ with increasing concentration from 0.1 to 30 mM. In salt-tolerant NaCl-adapted cells, however, both Na+ and K+ ions induced almost the same degree of reduction in the amount of Ca2+ bound to PM in the physiological concentration range of Ca2+ in the medium between 2 and 4 mM. These results suggest that, under the physiological conditions, PM of salt-sensitive NaCl-unadapted cells has an appreciable amount of PM-bound Ca2+ that is desorbed much easier by Na+ than K+, whereas PM of salt-tolerant NaCl-adapted cells has the PM-bound Ca2+ that can be equally desorbed by Na+ and K+.

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Section: Introductionmentioning

confidence: 62%

Section: Introductionmentioning

confidence: 84%

Section: Electrophoresismentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Alterations in Ca2+-Binding on Plasma Membrane after Adaptation to Salt Stress of Tobacco Cells in Suspension

Murata¹,

Katsura²,

Obi³

et al. 2000

Plant and Cell Physiology

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show abstract

“…Displacement of Ca 2+ by Na + , as a primary response to salt stress has already been suggested many years ago, based on measurements of Ca 2+ -CTC Xuorescence (Cramer et al 1985;Lynch and Läuchli 1988). In the following years this notion was supported by computational analysis of surface electrical potentials based on competition experiments between Na + and Ca 2+ (Yermiyahu et al 1994(Yermiyahu et al , 1997aKinraide 1998Kinraide , 1999, as well as by employing electrophoretic studies on barley mesophyll protoplasts (Murata et al 1998a(Murata et al , 2000. It has been suggested that the speciWc amelioration of Na + toxicity by Ca 2+ is in a minor part due to restoration of Ca 2+ at the plasma membrane surface, and in the major part may entail the blockage of a Na + uptake level (Kinraide 2004).…”

Section: Introductionmentioning

confidence: 96%

The involvement of calcium in the regulation of GPX1 expression

Gueta-Dahan

Avsian-Kretchmer

Ben–Hayyim

2008

Planta

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Detrimental effects of salinity on plants are known to be partially alleviated by external Ca(2+). Previously we demonstrated that in citrus cells, phospholipid hydroperoxide glutathione peroxidase (GPX1) is induced by salt and its activation can be monitored by pGPX1::GUS fusion in transformed tobacco cells. In this paper we further characterized the induction of GPX1 by additional treatments, which are known to affect Ca(2+) transport. Omission of Ca(2+) changed the pattern of the transient salt-induced expression of GPX1 and chelation of Ca(2+) by EGTA, or treatment with caffeine, abolished the salt-induced GPX1 transcript. On the other hand, La(3+) was found to be as potent as NaCl in inducing GPX1 transcription and the combined effect of La(3+) and NaCl seemed to be additive. Pharmacological perturbation of either external or internal Ca(2+) pools by La(3+), EGTA, caffeine, Ca(2+) channel blockers, or a Ca(2+)-ATPase inhibitor rendered the imposed salt stress more severe. Except for La(3+), all these Ca(2+) effectors had no effect on their own. In addition, the fluidizer benzyl alcohol dramatically increased the NaCl-induced GPX1 transcription. Taken together, our results show that: 1) the mode of action of La(3+) on GPX1 expression differs from its established role as a Ca(2+) channel blocker, 2) membrane integrity has an important role in the perception of salt stress, and 3) internal stores of Ca(2+) are involved in activating GPX1 expression in response to salt stress. We propose that the common basis for these effects lies in the membrane bound Ca(2+).

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