16 results on '"Frølund S"'
Search Results
2. Sertraline inhibits the transport of PAT1 substrates in vivo and in vitro
- Author
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Nielsen, C U, Frølund, S, Abdulhadi, S, Sari, H, Langthaler, L, Nøhr, M K, Kall, M A, Brodin, B, and Holm, R
- Subjects
Male ,Amino Acid Transport Systems ,Proline ,Administration, Oral ,Biological Availability ,Peptide Transporter 1 ,Rats, Sprague-Dawley ,Xenopus laevis ,Sodium-Glucose Transporter 1 ,Tandem Mass Spectrometry ,Sertraline ,Animals ,Humans ,Intestinal Mucosa ,Chromatography ,Dose-Response Relationship, Drug ,Symporters ,Isoxazoles ,Research Papers ,Rats ,Amino Acid Transport Systems, Neutral ,Intestinal Absorption ,Area Under Curve ,Caco-2 Cells ,Hydrophobic and Hydrophilic Interactions ,Selective Serotonin Reuptake Inhibitors - Abstract
Intestinal nutrient transporters may mediate the uptake of drugs. The aim of this study was to investigate whether sertraline interacts with the intestinal proton-coupled amino acid transporter 1 PAT1 (SLC36A1).In vitro investigations of interactions between sertraline and human (h)PAT1, hSGLT1 (sodium-glucose linked transporter 1) and hPepT1 (proton-coupled di-/tri-peptide transporter 1) were conducted in Caco-2 cells using radiolabelled substrates. In vivo pharmacokinetic investigations were conducted in male Sprague-Dawley rats using gaboxadol (10 mg·kg(-1), p.o.) as a PAT1 substrate and sertraline (0-30.6 mg·kg(-1)). Gaboxadol was quantified by hydrophilic interaction chromatography followed by MS/MS detection.Sertraline inhibited hPAT1-mediated L-[(3)H]-Pro uptake in Caco-2 cells. This interaction between sertraline and PAT1 appeared to be non-competitive. The uptake of the hSGLT1 substrate [(14)C]-α-methyl-D-glycopyranoside and the hPepT1 substrate [(14)C]-Gly-Sar in Caco-2 cells was also decreased in the presence of 0.3 mM sertraline. In rats, the administration of sertraline (0.1-10 mM, corresponding to 0.3-30.6 mg·kg(-1), p.o.) significantly reduced the maximal gaboxadol plasma concentration and AUC after its administration p.o.Sertraline is an apparent non-competitive inhibitor of hPAT1-mediated transport in vitro. This inhibitory effect of sertraline is not specific to hPAT1 as substrate transport via hPepT1 and hSGLT1 was also reduced in the presence of sertraline. In vivo, sertraline reduced the amount of gaboxadol absorbed, suggesting that the inhibitory effect of sertraline on PAT1 occurs both in vitro and in vivo. Hence, sertraline could alter the bioavailability of drugs absorbed via PAT1.
- Published
- 2013
3. Sertraline inhibits the transport of PAT1 substratesin vivoandin vitro
- Author
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Nielsen, C U, primary, Frølund, S, additional, Abdulhadi, S, additional, Sari, H, additional, Langthaler, L, additional, Nøhr, M K, additional, Kall, M A, additional, Brodin, B, additional, and Holm, R, additional
- Published
- 2013
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4. The proton-coupled amino acid transporter, SLC36A1 (hPAT1), transports Gly-Gly, Gly-Sar and other Gly-Gly mimetics.
- Author
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Frølund, S, Holm, R, Brodin, B, Nielsen, CU, Frølund, S, and Nielsen, C U
- Subjects
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MEMBRANE proteins , *GLYCINE , *PEPTIDES , *BIOLOGICAL transport , *XENOPUS , *ANTICONVULSANTS , *ENZYME inhibitors - Abstract
BACKGROUND AND PURPOSE The intestinal proton-coupled amino acid transporter, SLC36A1, transports zwitterionic α-amino acids and drugs such as vigabatrin, gaboxadol and δ-aminolevulinic acid. We hypothesize that SLC36A1 might also transport some dipeptides. The aim of the present study was to investigate SLC36A1-mediated transport of Gly-Gly and Gly-Gly mimetics, and to investigate Gly-Sar transport via SLC36A1 and the proton-coupled dipeptide/tripeptide transporter, SLC15A1 in Caco-2 cells. EXPERIMENTAL APPROACH Transport of a compound via SLC36A1 was determined by its ability to induce an increase in the inward current of two-electrode voltage clamped SLC36A1 cRNA-injected Xenopus laevis oocytes. SLC36A1-mediated L-[³H]Pro uptake in Caco-2 cells was measured in the absence and presence of Gly-Gly or Gly-Sar. In addition, apical [¹⁴C]Gly-Sar uptake was measured in the absence and presence of the SLC36A1 inhibitor 5-hydroxy-L-tryptophan (5-HTP) or the SLC15A1 inhibitor L-4,4'-biphenylalanyl-L-proline (Bip-Pro). KEY RESULTS In SLC36A1-expressing oocytes, an inward current was induced by Gly-Sar, Gly-Gly, δ-aminolevulinic acid, β-aminoethylglycine, δ-aminopentanoic acid, GABA, Gly and Pro, whereas Val, Leu, mannitol, 5-HTP and the dipeptides Gly-Ala, Gly-Pro and Gly-Phe did not evoke currents. In Caco-2 cell monolayers, the apical uptake of 30 mM Gly-Sar was inhibited by 20 and 22% in the presence of 5-HTP or Bip-Pro, respectively, and by 48% in the presence of both. CONCLUSION AND IMPLICATIONS Our results suggest that whereas Gly-Gly amid bond bioisosteres are widely accepted by the hPAT1 carrier, dipeptides in general are not; and therefore, Gly-Sar might structurally define the size limit of dipeptide transport via SLC36A1. [ABSTRACT FROM AUTHOR]
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- 2010
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5. Delta-aminolevulinic acid is a substrate for the amino acid transporter SLC36A1 (hPAT1).
- Author
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Frølund, S, Marquez, OC, Larsen, M, Brodin, B, Nielsen, CU, Frølund, S, Marquez, O C, and Nielsen, C U
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KETONIC acids , *AMINO acids , *CHROMOGENIC compounds , *PHOTOCHEMOTHERAPY , *PROSTATE cancer , *BLADDER cancer , *DRUG administration - Abstract
Background and Purpose: delta-Aminolevulinic acid (ALA) is used in cancer patients for photodynamic diagnosis or therapy. Oral administration of ALA has been used in patients with prostate and bladder cancer. The present aim was to investigate the mechanism of intestinal absorption of ALA and its transport via the amino acid transporter SLC36A1.Experimental Approach: In vitro investigations of ALA affinity for and uptake via SLC36A1 and SLC15A1 were performed in Caco-2 cell monolayers. Interaction of ALA with SLC15A1 was investigated in MDCK/SLC15A1 cells, whereas interactions with SLC36A1 were investigated in COS-7 cells transiently expressing SLC36A1.Key Results: ALA inhibited SLC36A1-mediated L-[(3)H]Pro and SLC15A1-mediated [(14)C]Gly-Sar uptake in Caco-2 cell monolayers with IC(50) values of 11.3 and 2.1 mM respectively. In SLC36A1-expressing COS-7 cells, the uptake of [(14)C]ALA was saturable with a K(m) value of 6.8 +/- 3.0 mM and a V(max) of 96 +/- 13 pmol x cm(-2) x min(-1). Uptake of [(14)C]ALA was pH and concentration dependent, and could be inhibited by glycine, proline and GABA. In a membrane potential assay, translocation of ALA via SLC36A1 was concentration dependent, with a K(m) value of 3.8 +/- 1.0 mM. ALA is thus a substrate for SLC36A1. In Caco-2 cells, apical [(14)C]ALA uptake was pH dependent, but Na(+) independent, and completely inhibited by 5-hydroxy-L-tryptophan and L-4,4'-biphenylalanyl-l-proline. CONCLUSIONS AND IMPLICATIONS. ALA was a substrate for SLC36A1, and the apical absorption in Caco-2 cell was only mediated by SLC36A1 and SLC15A1. This advances our understanding of intestinal absorption mechanisms of ALA, as well as its potential for drug interactions. [ABSTRACT FROM AUTHOR]- Published
- 2010
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6. Potential involvement of the proton-coupled amino acid transporter PAT1 (SLC36A1) in the delivery of pharmaceutical agents
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Frølund, S., primary, Nøhr, M.K., additional, Holm, R., additional, Brodin, B., additional, and Nielsen, C.U., additional
- Published
- 2013
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7. Function and expression of the proton-coupled amino acid transporter PAT1 along the rat gastrointestinal tract: implications for intestinal absorption of gaboxadol
- Author
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Broberg, ML, primary, Holm, R, additional, Tønsberg, H, additional, Frølund, S, additional, Ewon, KB, additional, Nielsen, AL, additional, Brodin, B, additional, Jensen, A, additional, Kall, MA, additional, Christensen, KV, additional, and Nielsen, CU, additional
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- 2012
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8. δ-Aminolevulinic acid is a substrate for the amino acid transporter SLC36A1 (hPAT1)
- Author
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Frølund, S, primary, Marquez, OC, additional, Larsen, M, additional, Brodin, B, additional, and Nielsen, CU, additional
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- 2010
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9. In vivo and in vitro evaluations of intestinal gabapentin absorption: effect of dose and inhibitors on carrier-mediated transport.
- Author
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Larsen MS, Frølund S, Nøhr MK, Nielsen CU, Garmer M, Kreilgaard M, and Holm R
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- Administration, Oral, Amines blood, Amino Acids, Cyclic pharmacology, Animals, Caco-2 Cells, Cyclohexanecarboxylic Acids blood, Dose-Response Relationship, Drug, Gabapentin, Humans, Injections, Intravenous, Male, Membrane Transport Modulators pharmacology, Membrane Transport Proteins adverse effects, Models, Biological, Rats, Sprague-Dawley, gamma-Aminobutyric Acid blood, Amines administration & dosage, Amines pharmacokinetics, Cyclohexanecarboxylic Acids administration & dosage, Cyclohexanecarboxylic Acids pharmacokinetics, Intestinal Absorption drug effects, Intestinal Mucosa metabolism, Membrane Transport Proteins metabolism, gamma-Aminobutyric Acid administration & dosage, gamma-Aminobutyric Acid pharmacokinetics
- Abstract
Purpose: Gabapentin exhibits saturable absorption kinetics, however, it remains unclear which transporters that are involved in the intestinal transport of gabapentin. Thus, the aim of the current study was to explore the mechanistic influence of transporters on the intestinal absorption of gabapentin by both in vivo and in vitro investigations, Methods: Pharmacokinetic parameters were determined following a range of intravenous (5-100 mg/kg) and oral doses (10-200 mg/kg) in rats. Transepithelial transport (50 μM-50 mM) and apical uptake of gabapentin (0.01-50 mM) were investigated in Caco-2 cells. The effect of co-application of the LAT-inhibitor, BCH, and the b(0,+)-substrate, L-lysine, on intestinal transport of gabapentin was evaluated in vivo and in vitro., Results: Gabapentin showed dose-dependent oral absorption kinetics and dose-independent disposition kinetics. Co-application of BCH inhibited intestinal absorption in vivo and apical uptake in vitro, whereas no effect was observed following co-application of L-lysine., Conclusions: The present study shows for the first time that BCH was capable of inhibiting intestinal absorption of gabapentin in vivo. Furthermore, in Caco-2 cell experiments BCH inhibited apical uptake of gabapentin. These findings may imply that a BCH-sensitive transport-system was involved in the apical and possibly the basolateral transport of gabapentin across the intestinal wall.
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- 2015
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10. Pharmacokinetic aspects of the anti-epileptic drug substance vigabatrin: focus on transporter interactions.
- Author
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Nøhr MK, Frølund S, Holm R, and Nielsen CU
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- Animals, Drug Interactions, Food-Drug Interactions, Humans, Intestinal Absorption, Anticonvulsants pharmacokinetics, Membrane Transport Proteins physiology, Vigabatrin pharmacokinetics
- Abstract
Drug transporters in various tissues, such as intestine, kidney, liver and brain, are recognized as important mediators of absorption, distribution, metabolism and excretion of drug substances. This review gives a current status on the transporter(s) mediating the absorption, distribution, metabolism and excretion properties of the anti-epileptic drug substance vigabatrin. For orally administered drugs, like vigabatrin, the absorption from the intestine is a prerequisite for the bioavailability. Therefore, transporter(s) involved in the intestinal absorption of vigabatrin in vitro and in vivo are discussed in detail. Special focus is on the contribution of the proton-coupled amino acid transporter 1 (PAT1) for intestinal vigabatrin absorption. Furthermore, the review gives an overview of the pharmacokinetic parameters of vigabatrin across different species and drug-food and drug-drug interactions involving vigabatrin.
- Published
- 2014
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11. Sertraline inhibits the transport of PAT1 substrates in vivo and in vitro.
- Author
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Nielsen CU, Frølund S, Abdulhadi S, Sari H, Langthaler L, Nøhr MK, Kall MA, Brodin B, and Holm R
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- Administration, Oral, Amino Acid Transport Systems metabolism, Amino Acid Transport Systems, Neutral metabolism, Animals, Area Under Curve, Biological Availability, Caco-2 Cells, Chromatography methods, Dose-Response Relationship, Drug, Humans, Hydrophobic and Hydrophilic Interactions, Intestinal Mucosa metabolism, Isoxazoles administration & dosage, Isoxazoles blood, Isoxazoles pharmacokinetics, Male, Peptide Transporter 1, Proline metabolism, Rats, Rats, Sprague-Dawley, Sodium-Glucose Transporter 1 antagonists & inhibitors, Sodium-Glucose Transporter 1 metabolism, Symporters metabolism, Tandem Mass Spectrometry, Xenopus laevis, Amino Acid Transport Systems antagonists & inhibitors, Amino Acid Transport Systems, Neutral antagonists & inhibitors, Intestinal Absorption drug effects, Intestinal Mucosa drug effects, Selective Serotonin Reuptake Inhibitors pharmacology, Sertraline pharmacology, Symporters antagonists & inhibitors
- Abstract
Background and Purpose: Intestinal nutrient transporters may mediate the uptake of drugs. The aim of this study was to investigate whether sertraline interacts with the intestinal proton-coupled amino acid transporter 1 PAT1 (SLC36A1)., Experimental Approach: In vitro investigations of interactions between sertraline and human (h)PAT1, hSGLT1 (sodium-glucose linked transporter 1) and hPepT1 (proton-coupled di-/tri-peptide transporter 1) were conducted in Caco-2 cells using radiolabelled substrates. In vivo pharmacokinetic investigations were conducted in male Sprague-Dawley rats using gaboxadol (10 mg·kg(-1), p.o.) as a PAT1 substrate and sertraline (0-30.6 mg·kg(-1)). Gaboxadol was quantified by hydrophilic interaction chromatography followed by MS/MS detection., Key Results: Sertraline inhibited hPAT1-mediated L-[(3)H]-Pro uptake in Caco-2 cells. This interaction between sertraline and PAT1 appeared to be non-competitive. The uptake of the hSGLT1 substrate [(14)C]-α-methyl-D-glycopyranoside and the hPepT1 substrate [(14)C]-Gly-Sar in Caco-2 cells was also decreased in the presence of 0.3 mM sertraline. In rats, the administration of sertraline (0.1-10 mM, corresponding to 0.3-30.6 mg·kg(-1), p.o.) significantly reduced the maximal gaboxadol plasma concentration and AUC after its administration p.o., Conclusions and Implications: Sertraline is an apparent non-competitive inhibitor of hPAT1-mediated transport in vitro. This inhibitory effect of sertraline is not specific to hPAT1 as substrate transport via hPepT1 and hSGLT1 was also reduced in the presence of sertraline. In vivo, sertraline reduced the amount of gaboxadol absorbed, suggesting that the inhibitory effect of sertraline on PAT1 occurs both in vitro and in vivo. Hence, sertraline could alter the bioavailability of drugs absorbed via PAT1., (© 2013 The British Pharmacological Society.)
- Published
- 2013
- Full Text
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12. Intestinal drug transport via the proton-coupled amino acid transporter PAT1 (SLC36A1) is inhibited by Gly-X(aa) dipeptides.
- Author
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Frølund S, Langthaler L, Kall MA, Holm R, and Nielsen CU
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- Administration, Oral, Animals, Biological Transport drug effects, Caco-2 Cells, Cell Membrane Permeability drug effects, Humans, Intestinal Mucosa metabolism, Intestines drug effects, Isoxazoles pharmacology, Male, Oocytes drug effects, Oocytes metabolism, Protons, Rats, Rats, Sprague-Dawley, Xenopus laevis metabolism, Amino Acid Transport Systems metabolism, Dipeptides pharmacology, Glycine metabolism, Intestinal Absorption drug effects, Symporters metabolism
- Abstract
The oral absorption of some drug substances is mediated by nutrient transporters. As a consequence, nutrients and drugs may compete for available transporters, and interactions at the level of intestinal absorption are possible. Recently, we have identified δ-aminolevulinic acid, Gly-Gly, and Gly-Sar as substrates of the amino acid transporter PAT1. The aim of the present study is to investigate if other Gly-containing dipeptides interact with PAT1, and whether they can inhibit PAT1 mediated drug absorption, in vitro and in vivo. The in vitro methods included two-electrode voltage clamp measurements on hPAT1 expressing Xenopus laevis oocytes, which were used to investigate the PAT1-mediated transport of 17 different Gly-containing dipeptides (Gly-X(aa) or X(aa)-Gly). Also, the transepithelial transport of the PAT1 substrate gaboxadol was investigated across Caco-2 cell monolayers in the presence of different dipeptides. The in vivo part consisted of a pharmacokinetic study in rats following oral administration of gaboxadol and preadministration of 200 mg/kg dipeptide. The results showed that in hPAT1 expressing oocytes Gly-Tyr, Gly-Pro, and Gly-Phe inhibited currents induced by drug substances. In Caco-2 cell monolayers, Gly-Gly, Gly-Sar, and Gly-Pro significantly inhibited the PAT1 mediated absorptive transepithelial transport of gaboxadol; however, when orally administered to rats, Gly-Gly, Gly-Sar, Gly-Pro, or Gly-Tyr did not alter the pharmacokinetic profile of gaboxadol. In conclusion, the present study identifies selected dipeptides as inhibitors of PAT1 mediated drug absorption in various in vitro models.
- Published
- 2012
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13. Rectal absorption of vigabatrin, a substrate of the proton coupled amino acid transporter (PAT1, Slc36a1), in rats.
- Author
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Holm R, Kall MA, Frølund S, Nielsen AL, Jensen A, Broberg ML, and Nielsen CU
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- Absorption, Administration, Rectal, Amino Acid Transport Systems antagonists & inhibitors, Animals, Biological Availability, Biological Transport physiology, Caco-2 Cells, Epithelium metabolism, Humans, Intestinal Absorption drug effects, Intestinal Mucosa drug effects, Intestinal Mucosa metabolism, Male, Oocytes metabolism, Proline metabolism, Protons, Rats, Rats, Sprague-Dawley, Symporters antagonists & inhibitors, Tryptophan metabolism, Vigabatrin pharmacology, Xenopus laevis, Amino Acid Transport Systems metabolism, Amino Acid Transport Systems, Neutral metabolism, Rectum metabolism, Symporters metabolism, Vigabatrin pharmacokinetics
- Abstract
Purpose: To investigate the rectal absorption of vigabatrin in rats, based on the hypothesis that PAT1 (Slc36a1) is involved., Methods: Male Sprague-Dawley rats were dosed rectally with five different gels, varying in buffer capacity, the amount of vigabatrin, and co-administration of proline or tryptophan. Western blotting was used to detect rPAT1 in rat rectal epithelium. X. Laevis oocytes were injected with SLC36A1 cRNA for the expression of hPAT1, prior to two-electrode voltage clamp measurements., Results: rPAT1 protein was present in rat rectal epithelium. Approximately 7%-9% of a 1 mg/kg vigabatrin dose was absorbed after rectal administration, regardless of the formulation used. Increasing the dose of vigabatrin 10-fold decreased the absolute bioavailability to 4.2%. Co-administration of proline or tryptophan changed the pharmacokinetic profile, indicating a role of PAT1 in the rectal absorption of vigabatrin. Transport of vigabatrin via hPAT1 expressed in X. Laevis oocytes had a K(m) of 5.2 ± 0.6 mM and was almost completely inhibited by tryptophan., Conclusions: Although vigabatrin is a PAT1 substrate and the rPAT1 protein is expressed in the rectum epithelium, vigabatrin has low rectal absorption in rats.
- Published
- 2012
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14. Gaboxadol has affinity for the proton-coupled amino acid transporter 1, SLC36A1 (hPAT1)--A modelling approach to determine IC(50) values of the three ionic species of gaboxadol.
- Author
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Frølund S, Rapin N, and Nielsen CU
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- Caco-2 Cells, Humans, Hydrogen-Ion Concentration, Inhibitory Concentration 50, Isoxazoles chemistry, Models, Molecular, Amino Acid Transport Systems drug effects, GABA Agonists pharmacology, Isoxazoles pharmacology, Symporters drug effects
- Abstract
The human proton-coupled amino acid transporter, SLC36A1 (hPAT1), is situated in the apical membrane of small intestinal epithelium. It is involved in cellular uptake of amino acids and orally administered drug substances such as δ-aminolevulinic acid, vigabatrin and gaboxadol. Gaboxadol (Gbx) is a selective extrasynaptic GABA(A) receptor agonist with high oral bioavailability in rat, dog and human. It is a zwitterionic compound with pK(a) values of 4.3 and 8.1. Dependent on the pH of the solution Gbx will be present as three individual ionic species, i.e. cationic (Gbx(+)), zwitterionic (Gbx(+/-)) and anionic (Gbx(-)). The aim of the present study was to elucidate the individual affinities of Gbx(+), Gbx(+/-) and Gbx(-) for SLC36A1. The ability of Gbx to concentration-dependently inhibit a SLC36A1 mediated l-[(3)H]proline uptake was investigated in Caco-2 cell monolayers at apical pH 5.0-6.8. The IC(50) values were computed using an in silico model relying on a genetic algorithm. The IC(50) values of Gbx(+), Gbx(+/-) and Gbx(-) were estimated to 2.6mM, 16mM and >1000mM. This indicates that the positive charge is essential for Gbx binding to SLC36A1. The negative charge is tolerated in the zwitterionic form, whereas no affinity is observed for the anionic form., (Copyright © 2010 Elsevier B.V. All rights reserved.)
- Published
- 2011
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15. Assessment of structurally diverse philanthotoxin analogues for inhibitory activity on ionotropic glutamate receptor subtypes: discovery of nanomolar, nonselective, and use-dependent antagonists.
- Author
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Frølund S, Bella A, Kristensen AS, Ziegler HL, Witt M, Olsen CA, Strømgaard K, Franzyk H, and Jaroszewski JW
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- Animals, Excitatory Amino Acid Antagonists chemistry, Excitatory Amino Acid Antagonists pharmacology, Female, Oocytes drug effects, Oocytes physiology, Patch-Clamp Techniques, Phenols chemistry, Phenols pharmacology, Polyamines chemistry, Polyamines pharmacology, Protein Subunits antagonists & inhibitors, Structure-Activity Relationship, Xenopus laevis, Excitatory Amino Acid Antagonists chemical synthesis, Phenols chemical synthesis, Polyamines chemical synthesis, Receptors, AMPA antagonists & inhibitors, Receptors, N-Methyl-D-Aspartate antagonists & inhibitors, Wasp Venoms chemistry
- Abstract
An array of analogues of the wasp toxin philanthotoxin-433, in which the asymmetric polyamine moiety was exchanged for spermine and the headgroup replaced with a variety of structurally diverse moieties, was prepared using parallel solid-phase synthesis approaches. In three analogues, the spermine moiety was extended with an amino acid tail, six compounds contained an N-acylated cyclohexylalanine, and four analogues were based on a novel diamino acid design with systematically changed spacer length between N-cyclohexylcarbonyl and N-phenylacetyl substituents. The analogues were studied using two-electrode voltage-clamp electrophysiology employing Xenopus laevis oocytes expressing GluA1(i) AMPA or GluN1/2A NMDA receptors. Several of the analogues showed significantly increased inhibition of the GluN1/2A NMDA receptor. Thus, an analogue containing N-(1-naphtyl)acetyl group showed an IC(50) value of 47 nM. For the diamino acid-based analogues, the optimal spacer length between two N-acyl groups was determined, resulting in an analogue with an IC(50) value of 106 nM.
- Published
- 2010
- Full Text
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16. [Chiropractic--treating both joints and muscles].
- Author
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Ostergaard K and Frølund S
- Subjects
- Humans, Manipulation, Orthopedic methods, Chiropractic methods, Musculoskeletal Diseases therapy
- Published
- 1994
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