Polyamine uptake in cultured cerebellar granule neurons

Dot, Josep; Lluch, Mónica; Blanco, Isaac; Rodríguez‐Álvarez, José

doi:10.1016/j.neuint.2003.08.007

Cited by 3 publications

(8 citation statements)

References 29 publications

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“…These data suggest that choline acts as a low-affinity antagonist of spermine uptake in S2 cells. Furthermore, these data may also explain the partial reduction of polyamine transport reported previously in other systems when Na + and K + were replaced by this ion [15][16][17][18]34].…”

Section: Ionic Requirements Of Spermine Uptake In Drosophila S2 Cellssupporting

confidence: 72%

“…Therefore we tested the affinities of several known substrates of H + -dependent transporter families. Similar to mammalian activities, spermine transport in S2 cells is inhibited by MGBG [15,39] and agmatine [34] ( Figure 5A). In addition, we find that most, if not all, substrates of the Slc22 cation/anion family of transporters [40] also inhibit spermine transport ( Figure 5B).…”

Section: Pharmacological Profile Of the Spermine/spermidine Transportsupporting

confidence: 56%

“…Although polyamine transport has been widely reported, the bioenergetic mechanisms and the transport proteins that are responsible for most of these activities remain unknown [15][16][17][19][20][21][22][23][24]. We find that Drosophila S2 cells show high-affinity spermine and spermidine uptake through a temperature-dependent saturable mechanism, and the results of the present study suggest that this activity may be sensitive to the H + gradients across the plasma membrane.…”

Section: Discussionmentioning

confidence: 48%

“…Despite the potential significance of polyamine uptake activity for both neuronal activity and cell growth, polyamine transport in eukaryotes is poorly understood. In mammals, polyamine uptake across the plasma membrane has been proposed to be carriermediated, energy-dependent and saturable [14], and many reports suggest that transport may be Na + -independent [15][16][17][18]. However, the bioenergetics of polyamine transport and the ionic gradients to which it may be coupled remain unclear.…”

Section: Introductionmentioning

confidence: 99%

“…However, the bioenergetics of polyamine transport and the ionic gradients to which it may be coupled remain unclear. Moreover, although the existence of polyamine transport activities in both prokaryotic and some eukaryotic cells has been thoroughly established [15][16][17][19][20][21][22][23][24], only the prokaryote and unicellular eukaryote transporters have been identified [25][26][27][28][29][30].…”

Section: Introductionmentioning

confidence: 99%

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Transport of polyamines in Drosophila S2 cells: kinetics, pharmacology and dependence on the plasma membrane proton gradient

Romero-Calderón

Krantz

2005

Biochemical Journal

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Polyamine transport activities have been described in diverse multicellular systems, but their bioenergetic mechanisms and molecular identity remain unclear. In the present paper, we describe a high-affinity spermine/spermidine transport activity expressed in Drosophila S2 cells. Ion-replacement experiments indicate that polyamine uptake across the cell membrane is Na+-, K+-, Cl-- and Ca2+-independent, but pH-sensitive. Additional experiments using ionophores suggest that polyamine uptake may be H+-coupled. Pharmacological experiments show that polyamine uptake in S2 cells is selectively blocked by MGBG {methylglyoxal bis(guanylhydrazone) or 1,1'-[(methylethanediylidine)-dinitrilo]diguanidine} and paraquat (N,N-dimethyl-4,4'-bipyridylium), two known inhibitors of polyamine uptake in mammalian cells. In addition, inhibitors known to block the Slc22 (solute carrier 22) family of organic anion/cation transporters inhibit spermine uptake in S2 cells. These data and the genetic tools available in Drosophila will facilitate the molecular identification and further characterization of this activity.

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Section: Ionic Requirements Of Spermine Uptake In Drosophila S2 Cellssupporting

confidence: 72%

Section: Pharmacological Profile Of the Spermine/spermidine Transportsupporting

confidence: 56%

Section: Discussionmentioning

confidence: 48%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Transport of polyamines in Drosophila S2 cells: kinetics, pharmacology and dependence on the plasma membrane proton gradient

Romero-Calderón

Krantz

2005

Biochemical Journal

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Molecular characterization of a human cation‐Cl⁻ cotransporter (SLC12A8A, CCC9A) that promotes polyamine and amino acid transport

Daigle

Carpentier

Frenette‐Cotton

et al. 2009

Journal Cellular Physiology

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Cation-Cl- cotransporters (CCCs) belong to a large family of proteins that includes 9 isoforms, two of which have still not been ascribed a transport function (CCC8 and CCC9) while the others are all known to promote Cl(-)-coupled Na+ and/or K+ movement at the cell surface. The CCCs are also included in a larger family termed amino acid-polyamine-organocation carriers (APCs). In contrast to the CCCs, however, polyamine (PA) transporters have thus far been isolated from unicellular species exclusively and do not all belong to the APC family. In this work, we have found that a splice variant of CCC9 (CCC9a) promotes PA-amino acid transport at the surface of HEK-293 cells. We have also found that the influx of PAs in CCC9a-expressing cells is inhibited by pentamidine as well as furosemide, and that it increases further in the presence of specific amino acids but not of Na+, K+, or Cl-. Hence, a group of substrates that are directly transported by CCC9 and the molecular identity of a PA transport system in animal cells may have been uncovered for the first time. These findings are of special interest given that intracellular PAs play a key role in cell proliferation.

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Spinal CK2 regulates nociceptive signaling in models of inflammatory pain

Shi

Liang

et al. 2005

Pain

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Casein kinase 2 (CK2) is a widely expressed protein kinase. Over the last several years a long list of protein substrates has evolved, many of which have proven or hypothesized roles in nociceptive signal transmission. However, CK2 has not itself been demonstrated to participate in nociception prior to this time. We set out to test the hypothesis that spinal CK2 regulates nociception using several pain models. Our first studies focused on the ability of the selective CK2 inhibitors 4,5,6,7-tetrabromobenzotriazole (TBBT) and 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole (DRB) to reduce formalin-stimulated pain behaviors in mice. Both phases of the response to subcutaneous formalin were strongly inhibited by intrathecal administration of TBBT or DRB in dose-dependent fashion. Likewise, using the complete Freund's adjuvant (CFA) model of chronic inflammatory pain, TBBT was observed to strongly reduce mechanical allodynia. The inhibition of spinal CK2 with either inhibitor did not, however, alter withdrawal latencies in the hotplate thermal pain model while intrathecal morphine was very effective. Immunohistochemical studies demonstrated all three known CK2 subunits, alpha, alpha' and beta to be expressed in spinal cord tissue as did real-time PCR experiments. While mRNA levels for each of the subunits was transiently enhanced after formalin or CFA hindpaw injection, overall spinal cord protein levels were not elevated in a sustained fashion. Our results indicate that CK2 participates in inflammatory nociception both in the acute and chronic phases. Simple changes in the abundance of spinal CK2 subunits do not likely underlie these phenomena, however.

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Polyamine uptake in cultured cerebellar granule neurons

Cited by 3 publications

References 29 publications

Transport of polyamines in Drosophila S2 cells: kinetics, pharmacology and dependence on the plasma membrane proton gradient

Transport of polyamines in Drosophila S2 cells: kinetics, pharmacology and dependence on the plasma membrane proton gradient

Molecular characterization of a human cation‐Cl⁻ cotransporter (SLC12A8A, CCC9A) that promotes polyamine and amino acid transport

Spinal CK2 regulates nociceptive signaling in models of inflammatory pain

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Polyamine uptake in cultured cerebellar granule neurons

Cited by 3 publications

References 29 publications

Transport of polyamines in Drosophila S2 cells: kinetics, pharmacology and dependence on the plasma membrane proton gradient

Transport of polyamines in Drosophila S2 cells: kinetics, pharmacology and dependence on the plasma membrane proton gradient

Molecular characterization of a human cation‐Cl− cotransporter (SLC12A8A, CCC9A) that promotes polyamine and amino acid transport

Spinal CK2 regulates nociceptive signaling in models of inflammatory pain

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Molecular characterization of a human cation‐Cl⁻ cotransporter (SLC12A8A, CCC9A) that promotes polyamine and amino acid transport