Purification and properties of native cell wall acid phosphatase from cultured tobacco cells

Kaneko, Takako; Kikuti, Rie; Kubota, K

doi:10.1016/0031-9422(90)87097-e

Cited by 14 publications

(6 citation statements)

References 29 publications

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“…At the end of the incubation period, the medium was separated from the protoplasts by centrifugation. APase activity in the medium was determined using p ‐nitrophenol as described previously (Kaneko et al 1990). The medium was brought to 80% saturation with (NH 4 ) 2 SO 4.…”

Section: Methodsmentioning

confidence: 99%

“…Evidence for the existence of acid phosphatase (EC3.1.3.2; APase) in the cell wall of higher plants has been reported repeatedly (Lamport and Northcote 1960, Kivilann et al 1961, Chang and Bandurski 1964, Lamport 1965, Hall and Butt 1968, Suzuki and Sato 1973, Suzuki and Sato 1976, Crasnier and Giordani 1985, Nagahasi and Seibles 1986, Kaneko et al 1990). The native cell wall acid phosphatase (cell wall APase) is an intrinsic component of plant cell walls; however, the precise function of the enzyme has yet to be determined, a situation that also applies to other wall enzymes, such as invertase and peroxidase, which are without doubt also involved in numerous processes, from wall modification to metabolite transport and cell signalling (Cosgrove 1997).…”

Section: Introductionmentioning

confidence: 93%

“…The native cell wall acid phosphatase (cell wall APase) is an intrinsic component of plant cell walls; however, the precise function of the enzyme has yet to be determined, a situation that also applies to other wall enzymes, such as invertase and peroxidase, which are without doubt also involved in numerous processes, from wall modification to metabolite transport and cell signalling (Cosgrove 1997). In a previous paper, we demonstrated the purification and some properties of the cell wall APase of tobacco cells (Kaneko et al 1990). The cell wall APase second fraction (WP‐II) was eluted by column chromatography of isolated cell walls of tobacco cells.…”

Section: Introductionmentioning

confidence: 99%

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Involvement of an acid phosphatase on cell wall regeneration of tobacco protoplasts

Sano

Kaida

Maki

et al. 2003

Physiologia Plantarum

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Tobacco protoplasts begin to regenerate their own cell walls, the major components of which are b-glucans, soon after they are transferred into an adequate medium. During the cell wall regeneration the protoplasts secrete two isoforms of acid phosphatase (APase) in time-dependent manner. We determined that one of the isoforms, the Brefeldin A (BFA) sensitive one, is the cell wall resident APase (WP-II) by immunoblotting of the isoform with anti-WP-II antibody. We hypothesized that the WP-II may participate in the deposition of b-glucan microfibrils on the protoplast surface during cell wall regeneration. In order to examine this hypothesis, the protoplasts were cultivated in the cell wall regeneration medium containing the same amount of the BFA-sensitive APase (230 mg protein) as is secreted by the observed number of protoplasts (1.4 · 10 5 protoplasts) per plate (30-mmdiameter) during a 3-h cultivation after transfer to the cell wall regeneration medium. The addition of WP-II to the cell wall regeneration medium stimulated the deposition of b-glucan microfibrils on the surface of the protoplasts during cell wall regeneration. To determine the stimulative effect of the 60 kDa polypeptide of WP-II, protoplasts were cultivated in the medium containing the amount of anti-WP-II IgG (230 mg protein) equivalent to the BFA-sensitive APase. These results suggested that the 60 kDa polypeptide of WP-II is the BFAsensitive APase which is responsible for the enhanced deposition of b-glucan microfibrils on the surface of the protoplasts.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

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Involvement of an acid phosphatase on cell wall regeneration of tobacco protoplasts

Sano

Kaida

Maki

et al. 2003

Physiologia Plantarum

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“…Acid phosphatases are a group of enzymes that nonspecifically catalyze the hydrolysis of a variety of phosphate esters and are widely distributed in nature. They have been extensively studied in a number of plant systems (Kaneko et al 1990, Thaker et al 1996) and have considerable diversity with regard to their physical properties.…”

mentioning

confidence: 99%

“…They are widely distributed; their function has been studied in microorganisms but little data exist about their role in higher plants, and despite having broad specificity (Kaneko et al 1990), relatively little is known about their physiologic roles. In some cases it has not been possible to quantify or even detect them in plants (Hota and Israelstam 1978).…”

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confidence: 99%

Biochemical Changes Associated With Brassica juncea Seed Development. IV. Acid and Alkaline Phosphatases

Saroop

Chanda

Singh

1999

J Plant Growth Regul

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Changes in acid and alkaline phosphatase activities in cytoplasmic and wall-bound fractions of developing mustard (Brassica juncea) seed were studied. Growth was measured by seed dry weight and water content. Seed dry weight data were fitted to a cubic polynomial equation. Seed water content and dry matter accumulation was significantly correlated. Cytoplasmic acid and alkaline phosphatase activities were substantially less in the cytoplasmic fraction than the wall-bound fraction. Wall-bound acid phosphatase activity was low initially, but high levels were maintained after day 25, indicating a relationship with dry matter accumulation. The results suggest that acid phosphatase plays an important role during mustard seed development.

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Two isoforms of acid phosphatase secreted by tobacco protoplasts: differential effect of brefeldin A on their secretion

et al. 1996

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The effects of brefeldin A (BFA) on the secretion of acid phosphatase (APase) by tobacco protoplasts were investigated. Secretion of APase was inhibited by BFA in a dose-dependent manner, with a concomitant intracellular accumulation of the enzyme. The secreted APase was composed of two isoforms. BFA (10/ μg/ml) inhibited the secretion of one of the isoforms without inhibiting that of the other, and this phenomenon explains the partial inhibition of APase secretion as a whole. The inhibition of APase secretion was accompanied by changes in the morphology of the Golgi apparatus and also by an increment in massdensity of cells.

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Purification and properties of native cell wall acid phosphatase from cultured tobacco cells

Cited by 14 publications

References 29 publications

Involvement of an acid phosphatase on cell wall regeneration of tobacco protoplasts

Involvement of an acid phosphatase on cell wall regeneration of tobacco protoplasts

Biochemical Changes Associated With Brassica juncea Seed Development. IV. Acid and Alkaline Phosphatases

Two isoforms of acid phosphatase secreted by tobacco protoplasts: differential effect of brefeldin A on their secretion

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