Study of sucrose and mannitol transport in plasma-membrane vesicles from phloem and non-phloem tissues of celery (Apium graveolens L.) petioles

Salmon, Sandrine; Lemoine, Rémi; Jamai, Aziz; Bouche-Pillon, Sabine; Fromont, J. C.

doi:10.1007/bf00239942

Cited by 33 publications

(24 citation statements)

References 21 publications

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“…4) revealed little effect of any of these compounds on 14 C-sorbitol transport by PmPLT2, whereas a significant inhibition was observed for mannitol and unlabeled sorbitol on PmPLT1-driven 14 C-sorbitol transport. On one hand, the observed lack of inhibition with PmPLT2 was in agreement with the high specificity described for the sorbitol transporters in cherry (Gao et al, 2003) and with earlier results from Salmon et al (1995). These latter authors analyzed mannitol transport in plasma membrane vesicles prepared from celery phloem tissue and showed that a 20-fold excess of sorbitol had no inhibitory effect on 3 H-mannitol transport.…”

Section: Transport Properties and Kinetic Parameterssupporting

confidence: 90%

“…So far, PCMBS was known to inhibit the activity of plant Suc transporters with high specificity (Riesmeier et al, 1992;Sauer and Stolz, 1994) but not the activity of plant monosaccharide transporters (Ludwig et al, 2000). For mannitol transport in celery, it has been reported that the transporter is not (Salmon et al, 1995) or is only slightly (Noiraud et al, 2001) inhibited by PCMBS; the sorbitol transporters from cherry were not sensitive to PCMBS (Gao et al, 2003). The observed PCMBS sensitivity of PmPLT1 can be explained by comparing the Cys residues in PmPLT1 (six Cys residues) and PmPLT2 (five Cys residues).…”

Section: Transport Properties and Kinetic Parametersmentioning

confidence: 99%

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Differential Expression of Sucrose Transporter and Polyol Transporter Genes during Maturation of Common Plantain Companion Cells

Ramsperger-Gleixner¹,

Geiger²,

Hedrich³

et al. 2004

Plant Physiology

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The cDNAs of two sorbitol transporters, common plantain (Plantago major) polyol transporter (PLT) 1 and 2 (PmPLT1 and PmPLT2), were isolated from a vascular bundle-specific cDNA library from common plantain, a dicot plant transporting Suc plus sorbitol in its phloem. Here, we describe the kinetic characterization of these sorbitol transporters by functional expression in Brewer's yeast (Saccharomyces cerevisiae) and in Xenopus sp. oocytes and for the first time the localization of plant PLTs in specific cell types of the vascular tissue. In the yeast system, both proteins were shown to be uncoupler sensitive and could be characterized as low-affinity and low-specificity polyol symporters. The K m value for the physiological substrate sorbitol is 12 mm for PmPLT1 and even higher for PmPLT2, which showed an almost linear increase in sorbitol transport rates up to 20 mm. These data were confirmed in the Xenopus sp. system, where PmPLT1 was analyzed in detail and characterized as a H ϩ symporter. Using peptide-specific polyclonal antisera against PmPLT1 or PmPLT2 and simultaneous labeling with the monoclonal antiserum 1A2 raised against the companion cell-specific PmSUC2 Suc transporter, both PLTs were localized to companion cells of the phloem in common plantain source leaves. These analyses revealed two different types of companion cells in the common plantain phloem: younger cells expressing PmSUC2 at higher levels and older cells expressing lower levels of PmSUC2 plus both PLT genes. The putative role of these low-affinity transporters in phloem loading is discussed.

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Section: Transport Properties and Kinetic Parameterssupporting

confidence: 90%

Section: Transport Properties and Kinetic Parametersmentioning

confidence: 99%

Differential Expression of Sucrose Transporter and Polyol Transporter Genes during Maturation of Common Plantain Companion Cells

Ramsperger-Gleixner¹,

Geiger²,

Hedrich³

et al. 2004

Plant Physiology

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“…Both the Plantago (Ramsperger-Gleixner et al, 2004) and apple (Watari et al, 2004) transporters are localized in the minor vein phloem. Furthermore, active uptake of mannitol has been demonstrated in isolated phloem strands of celery (Daie, 1987) and plasma membrane vesicles prepared from such strands (Salmon et al, 1995). As the respective authors have pointed out, these data are consistent with an energized, apoplastic loading mechanism.…”

supporting

confidence: 64%

Phloem Loading Strategies in Three Plant Species That Transport Sugar Alcohols

Reidel

Rennie²,

Amiard³

et al. 2009

Plant Physiol.

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Many plants translocate sugar alcohols in the phloem. However, the mechanism(s) of sugar alcohol loading in the minor veins of leaves are debated. We characterized the loading strategies of two species that transport sorbitol (Plantago major and apple [Malus domestica]), and one that transports mannitol (Asarina scandens). Plasmodesmata are abundant at all interfaces in the minor vein phloem of apple, and in one of two types of phloem in the minor veins of A. scandens. Few plasmodesmata are present in the minor veins of P. major. Apple differs from the other two species in that sugar alcohol and sucrose (Suc) are present in much higher concentrations in leaves. Apple leaf tissue exposed to exogenous [ 14

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“…Phloem-localized MTD in celery may serve an analogous function to that of Suc synthase in phloem by providing access to translocated mannitol for generating energy. Although little is known about phloem loading and unloading of mannitol, recent evidence suggests that a proton motive force is involved in its transport across plasma membrane vesicles that are isolated from celery phloem (Salmon et al, 1995).…”

Section: Discussionmentioning

confidence: 99%

Immunolocalization of Mannitol Dehydrogenase in Celery Plants and Cells

et al. 1996

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MTD, an enzyme that catalyzes the oxidation of mannitol to Man (Stoop and Pharr, 1992), constitutes the initial reaction in the pathway by which mannitol enters the central metabolism in vascular plants (Pharr et al., 1995a(Pharr et al., , 1995b. MTD is distinctly different from M6PR, an enzyme that is localized almost exclusively in the cytosol of mature photosynthetic leaves (Everard et al., 1993), that catalyzes the central reaction of mannitol biosynthesis (Rumpho et al., 1983). Mannitol is an early photosynthetic product in celery (Apium gruveolens L.; Davis et al., 1988; Keller and Matile, 1989; Davis and Loescher, 1990) and other species (Loescher and Everard, 1996) and makes up to 50% of the phloem-translocated carbohydrate in celery plants (Loescher et al., 1995).Previous studies have focused on the role of mannitol as an important source of carbon for growth as well as its role in salt-and water-stress tolerance (Pharr et al., 1995a, 199513). The regulation of MTD expression has been shown to be an important control point in determining whether mannitol is to be used in metabolism for the production of carbon skeletons for assimilation and energy or whether it will accumulate for use as an osmoprotectant (Pharr et al., 1995a). In celery carbohydrate-utilizing sinks such as growing root tips and young leaves contain relatively high MTD activity (Stoop and Pharr, 1994), whereas mature photosynthetic leaves, mature roots, and storage sinks, such as fleshy petioles and the storage organ (knob) of celeriac (Stoop and Pharr, 1992), contain little or no MTD activity. Under conditions of h g h salinity and/or osmostress, MTD is strongly down-regulated in celery sink tissues, and this results in decreased mannitol utilization by these tissues and a corresponding increase in mannitol accumulation throughout the plant. In contrast, Mtd is induced in cell cultures in response to salicyclic acid and has strong sequence homology to EL13 pathogenesis-related proteins (Williamson et al., 1995). Thus, MTD may function in the resistance to an attack by plant pathogens (Stoop et al., 1996). MTD has been purified to homogeneity (Stoop et al., 1995), and this antigen was used for the production of polyclonal antiserum. This MTD-specific antiserum was used here to examine the tissue-and cell-type localization in celery of this important enzyme of mannitol catabolism. It is anticipated that such studies will help to elucidate the metabolic role of MTD in whole plants and assist in identifying the physiological and metabolic mechanisms that modulate Mtd gene expression. MATERIALS A N D METHODSCelery (Apium gruveolens L. var dulce [Mill] Pers. cv Tal1Golden Self-Blanching) seeds were grown in a greenhouse with a minimum day/night temperature of 24/18"C. Mature leaves were collected from plants 14 months after planting. Three-week to 3-month-old plants, cv Florida 638, were used as the source for the different developmental stages of leaves and roots. Celery suspension cultures were grown in Murashige-Skoog medium (Murashig...

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Study of sucrose and mannitol transport in plasma-membrane vesicles from phloem and non-phloem tissues of celery (Apium graveolens L.) petioles

Cited by 33 publications

References 21 publications

Differential Expression of Sucrose Transporter and Polyol Transporter Genes during Maturation of Common Plantain Companion Cells

Differential Expression of Sucrose Transporter and Polyol Transporter Genes during Maturation of Common Plantain Companion Cells

Phloem Loading Strategies in Three Plant Species That Transport Sugar Alcohols

Immunolocalization of Mannitol Dehydrogenase in Celery Plants and Cells

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