Polyamine membrane transport regulation

Khan, Naim Akhtar; Quemener, V.; Moulinoux, Jacques-Philippe

doi:10.1016/0309-1651(91)90078-w

Cited by 71 publications

(32 citation statements)

References 41 publications

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“…A direct proof of sharing the common transporter by spermidine and MGBG comes from the observations on CHOMG mutant cells (like 3T3MG cells used in this study) which are deficient in the transport properties for both of these molecules (Byers et al, 1989). Polyamines are taken up by the cells via an active and Na+ dependent transport system (for recent reviews, see Khan et al, 1991;Seiler and Dezeure, 1990). It seems tempting that metformin might utilize polyamine transport pathways to enter the cells.…”

Section: Metformin {(Ch)-nc( =Nh)nhc( -Nh)-nh} Is Amentioning

confidence: 78%

Characterization of metformin transport system in NIH 3T3 cells

Khan

Wiernsperger²,

Quemener

et al. 1992

Journal Cellular Physiology

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The biochemical properties of the metformin transport system were studied in NIH 3T3 cells. 14C-metformin uptake appeared to be a sodium dependent process. Iso-osmotical replacement of Na+ by choline chloride in the assay medium resulted in a decrease of metformin uptake. Amiloride (200 microM) inhibited the metformin transport by 35% in these cells. Gramicidin, a channel ionophore, was the most effective in inhibiting the metformin transport as compared to valinomycin, a mobile ion carrier, and Ca2+ ionophore (A 23187). Loading of cells with asparagine, ornithine, or polylysine did not influence the uptake process. However, the addition of lysine or arginine significantly stimulated the metformin uptake by NIH 3T3 cells. Similarly, the addition of metformin stimulated the arginine uptake by these cells, suggesting that metformin shares the y+ transport system. Metformin inhibited competitively the uptake of 14C-spermidine, a molecule of the polyamine family, by NIH 3T3 cells, whereas the latter failed to influence the uptake of the former significantly by these cells. Incubation of NIH 3T3 cells in the presence of difluoromethyl-ornithine (a suicidal inhibitor of polyamine biosynthesis) stimulated the spermidine, but not the metformin, uptake by these cells. Interestingly, a prolonged incubation of these cells in the presence of metformin failed to down-regulate the spermidine transport process. The spermidine- and methylglyoxal-bis(guanylhydrazone), MGBG-transport deficient (3T3MG) cells which do not accumulate exogeneous spermidine or MGBG, took up 14C-metformin. However, 14C-metformin uptake by 3T3MG cells was lower than that by normal NIH 3T3 cells.

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Section: Metformin {(Ch)-nc( =Nh)nhc( -Nh)-nh} Is Amentioning

confidence: 78%

Characterization of metformin transport system in NIH 3T3 cells

Khan

Wiernsperger²,

Quemener

et al. 1992

Journal Cellular Physiology

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“…8B) The noncompetitive nature of spermine inhibition of paraquat and putrescine uptake suggests that the system that transports paraquat, putrescine, and cadaverine is not involved in spermine absorption. Studies with animal tissues have previously shown the existence of more than one transport system for polyamines (12). Multiple carrier systems for various polyamines may also exist in the plasmalemma of maize root cells.…”

Section: Specificity Of Paraquat/putrescine Transportmentioning

confidence: 99%

Transport Interactions between Paraquat and Polyamines in Roots of Intact Maize Seedlings

Hart¹,

DiTomaso²,

Linscott³

et al. 1992

Plant Physiol.

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Interactions between absorption of paraquat and the polyamines putrescine, cadaverine, and spermine in roots of intact maize (Zea mays L. cv 3377 Pioneer) seedlings were examined. Concentrationdependent kinetics for paraquat and putrescine influx were similar and both kinetic curves could be resolved into a linear and a saturable component. The linear component was previously shown to represent cell wall/membrane binding. The saturable components for paraquat and putrescine uptake, which represent influx across the plasmalemma, had Km values of 98 and 120 micromolar, respectively, and Vmax values of 445 and 456 nanomoles per gram fresh weight per hour, respectively. Lineweaver-Burk transformation of the saturable component of paraquat influx in the presence of varying concentrations of putrescine indicated that the diamine competitively inhibited the saturable component of paraquat uptake. Reciprocal experiments similarly demonstrated that paraquat competitively inhibited the saturable component of putrescine uptake. Competitive inhibition of both paraquat and putrescine influx could also be demonstrated with the diamine cadaverine, which has a charge distribution similar to that of paraquat and putrescine. In contrast, the larger, tetravalent polyamine spermine appeared to noncompetitively inhibit the influx of paraquat and putrescine. These results strongly suggest that paraquat enters maize root cells via a carrier system that normally functions in the transport of diamines with a charge distribution similar to that of paraquat.Paraquat is a widely used postmergence contact herbicide that acts by accepting electrons from PSI of chloroplast membranes (3). To reach its site of action following foliar application, paraquat must be capable of crossing the plasmalemma (as well as the chloroplast envelope). In aqueous solution, however, paraquat exists as a divalent cation and is therefore unlikely to passively diffuse across the lipid bilayer of plant cell membranes. Until recently (11), however, little evidence has been reported for a paraquat transport mechanism in plant cell membranes.With the exception of 2,4-D (6, 18), herbicides have seldom been reported to require a carrier-mediated transport system for uptake across the plasmalemma. Recent evidence from our laboratories suggested that paraquat is taken up by maize (Zea mays L. cv 3377 Pioneer) root epidermal and cortical cells via a protein-mediated system. This is based primarily on concentration-dependent kinetic studies of paraquat absorption. In these studies, we demonstrated that paraquat influx across the plasmalemma is via a saturable system with a Km of 90 tiM and a Vmax of 458 nmol g-1 fresh weight h-1 (11).Paraquat uptake in animal tissues has also been reported to be mediated by a saturable system with a Km of 40 to 80 AM (17,21) and Vmax of 300 to 600 nmol g-' fresh weight h-1 (15,17). In contrast with our data from maize roots, influx into animal cells was reported to be sensitive to respiratory inhibitors such as cyanide and rotenone ...

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“…Although we have provided evidence that this phenomenon is not mediated by classical histamine receptors, Ha receptor antagonists, such as thioperamide and MR16155, are potent inhibitors. Conversely to the polyamine transport system, which exists in numerous cell types and has been extensively studied [14,15], histamine transport seems to be restricted to astrocytes, endothelial and glial cells, and is still poorly understood [16][17][18]. It has been suggested that astrocytes could use the same means of transport for histamine uptake and release [18].…”

mentioning

confidence: 99%

Evidence for bidirectional histamine transport by murine hematopoietic progenitor cells

Corbel

1996

FEBS Letters

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Murine hematopoietic progenitor cells synthesize substantial amounts of histamine in response to IL-3 or calcium ionophore. They also take up extracellular histamine by an active transport system. In the present study we demonstrate that this system mediates both influx and efflux of histamine. Indeed, MR16155 and thioperamide, the two 1-13 antagonists which are most effective in inhibiting histamine uptake, likewise diminish the release of preloaded histamine from bone marrow cells. These compounds also inhibit the release of histamine which has been newly synthesized by hematopoietic progenitors in response to IL-3 or calcium ionophore, as assessed by the accumulation of the mediator inside the cells in the presence of the antagonists. The potency of different histamine receptor antagonists as inhihitors of histamine release increases with their capacity to block histamine uptake.Key words: Hematopoietic progenitor; Histamine; Bidirectional transport; Interleukin-3 Histamine uptake is temperature-dependent and partially requires sodium exchange [13]. Although we have provided evidence that this phenomenon is not mediated by classical histamine receptors, Ha receptor antagonists, such as thioperamide and MR16155, are potent inhibitors. Conversely to the polyamine transport system, which exists in numerous cell types and has been extensively studied [14,15], histamine transport seems to be restricted to astrocytes, endothelial and glial cells, and is still poorly understood [16][17][18]. It has been suggested that astrocytes could use the same means of transport for histamine uptake and release [18]. Herein, we provide evidence for a bidirectional transporter in bone marrow cells (BMC) and in the IL-3-dependent cell line FDCP1, as assessed by the finding that the inhibitors of histamine uptake likewise decrease release of preloaded histamine. We also show that this system is involved in the release of endogenous histamine which is newly synthesized in response to IL-3 or calcium ionophore since we found a decrease in histamine release accompanied by an increase in intracellular histamine contents in the presence of H3 receptor antagonists.

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Polyamine membrane transport regulation

Cited by 71 publications

References 41 publications

Characterization of metformin transport system in NIH 3T3 cells

Characterization of metformin transport system in NIH 3T3 cells

Transport Interactions between Paraquat and Polyamines in Roots of Intact Maize Seedlings

Evidence for bidirectional histamine transport by murine hematopoietic progenitor cells

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