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8. Abstracts of papers clinical pharmacological meeting

Author

Merkus, F., Gribnau, F., Thien, Th., Louwerenburg, Hans, Kingma, J., Gilst, Wiek, Six, A., Graeff, Pieter, Wesseling, Harry, BoeLaert, J., Schurgers, M., Matthys, E., Belpaire, F., Daneels, R., Cre, M., Boqaert, M., D'Haese, P., Verpooten, G., Lamberts, L., Liang, L., Broe, M., Meijer, P., Russel, F., Russel, A., Ginneken, C., Liedekerke, B., Lambert, W., Yousouf, M., Roose, J., Leenheer, A., Lambert, W., Bersaques, J., Vanneste, L., Leenheer, A., Marie, S., Slaghuis, G., Rozing, P., Mattie, H., Poelma, F., Hilbers, H., Jansen, A., Tukker, J., Augusti, P., Verbeke, N., Peer, A., Snoeck, E., Heykants, J., Bruynseels, J., Peeters, J., Amery, W., Rogiers, V., Vandenberghe, Y., Comet, M., Callaerts, A., Sonck, W., Guillouzo, A., Vercruysse, A., Rooy, P., Rombaut, N., Bussche, G., Tan, A., Jansen, T., Termond, E., Kloppenborg, P., Thien, Th., Benraad, Th., Velde, V., Woestenbprghs, R., Hermens, W., Romeijn, S., Deurloo, M., Merkus, F., Musch, G., Massart, D., Hengstum, M., Festen, J., Broek, W., Corstens, F., Beurskens, C., Hankel, M., Smet, M., Belle, S., May, J., Storme, G., Kuppen, P., Schuitemaker, H., Veer, L., Oosterom, A., Schrier, P., Bruijn, E., Pooter, C., Tjaden, U., Slooten, H., Roelevink, H., Smit, E., Vries, E., Ijmker, J., Uges, D., Moors, M., Mertens, K., Hecken, A., Lepeleire, I., Verbesselt, R., Tjandra-Maga, T., Schepper, P., Guelen, P., Jansen, T., Vrijhof, W., Vos, D., Scharpé, S., Verkerk, R., Lsmeire, N., Zijlstra, I., Gribnau, F., Haaijer-Ruskamp, F., Post, D., Reddingius, P., Wesseling, H., Wollersheim, H., Meiracker, A., Veld, A., Admiraal, P., Boomsma, F., Derkx, F., Schalekamp, M., Schoors, D., Dupont, A., Claessen, F., Reljenga, J., Lenders, J., Thlen, Th., Laekeman, G., Muylle, L., Hoydonck, A., Herman, A., and Peetermans, M.

Published
1988
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10. The binding of gitoxin to human plasma proteins

Author

Verbeke, N., Pellegrin, P., Vienne, Anne, and Lesne, M.

Abstract

The binding of gitoxin, digitoxin and digoxin to human plasma proteins was measured by ultracentrifugation and equilibrium dialysis. At concentrations in the range of therapeutic plasma levels, protein binding amounted, respectively, to 85, 92 and 20%, the last two values being consistent with data reported in the literature. The affinity of purified human albumin was not significantly different for the three cardiac glycosides tested. No other protein than albumin was found to bind gitoxin in human plasma.

Published
1979
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12. Dutch Pharmacological Meeting 1984

Author

Timmerman, H., Koeman, J. H., den Tonkelaar, E. H., Merkus, F. W. H. M., Struyker-Boudier, H. A. J., Bolt, G. R., Saxena, P. R., Bos, R. P., Breed, A. S. P. M., Theuws, J. L. G., Henderson, P. Th., de Brauw, L. M., de Bruijn, E. A., van de Velde, C. J. H., Tjaden, U. R., Kothuis, B. J. L., van Oosterom, A. T., Reeuwijk, H. J. E. M., Pinedo, H. M., van der Hoeven, R., Bultsma, T., Linschoten, M. R., Peter, J., Burbach, H., de Kloet, E. Ronald, Castelein, O., Verbeke, N., Leuven, K. U., Conings, L., Doods, H. N., Kalkman, H. O., de Jonge, A., Wilffert, B., Thoolen, M. J. M. C., Timmermans, P. B. M. W. M., van Zwieten, P. A., van Driel, J. B. M., Klaassen, A. B. M., Kuypers, W., Beld, A. J., Rodrigues de Miranda, J. F., Driessen, O., van der Velde, E. A., Engels, F., Oosting, R. S., Nijkamp, F. P., Evelo, C. T. A., Neis, J. M., Peters, J. G. P., ten Broeke, M. A. M., Vulders, C. A. J. M., Franssen, M. J. A. M., van Herwaarden, C. L. A., van de Putte, L. B. A., Gribnau, F. W. J., van der Graaff, M., Vermeulen, N. P. E., Hofman, P. H., Breimer, D. D., 't Hart, B. J., Wilting, J., de Gier, J. J., Hazelhoff, Bernard, de Vries, Jan B., Oijkstra, Durk, Mulder, Theo, Wynberg, Hans, Horn, Alan, van Doorn, R., Leijdekkers, Ch. -M., Anzion, R., Hengstum, M. v., Festen, J., Buijs, W., Broek, W. v. d., Groothedde, R., Corstens, F., van Heuven-Nolsen, P., de Wildt, D. J., Hillen, F. C., van Noordwijk, J., Janssen, Lambert H. M., Jansen, P. A. F., Meyboom, R. H. B., Vree, T. B., Jelinek, J., Schönbaum, E., Lomax, P., de Jong, W., Sandor, P., Cox van Put, J. J., Jongeneelen, F. J., Leijdekkers, Ch. M., Kerklaan, P. R. M., Zoetemelk, C. E. M., Mohn, G. R., Grote, J. J., Kuijpers, W., Kleinbloesem, C. H., van Brummelen, P., van Harten, J., Koopmans, P. P., Kateman, W., Tan, Y., van Ginneken, C. A. M., van Koppen, C. J., van der Beek, E. M., Lammers, J. W. J., Krielaart, M. J., Laban, E., Charbon, G. A., Folgering, H. Th. M., Lenders, J. W. M., Sluiter, H. E., Willemsen, J., Thien, Th., Mooy, J., Schols, M., Baak, M. v., Hooff, M. v., Rahn, K. H., Mulder, Theo B. A., Grol, Cor J., Dijkstra, Durk, Horn, Alan S., Neef, C., Meijer, D. K. F., van Gemert, P. J. L., Roelofs, H. M. J., Osterhuis, B. O, ten Berge, R. J. M., Schellekens, P. T. A., van Boxtel, C. J., Peeters, P. A. M., Raghoebar, M., Tiemessen, H. L. G. H., Raaijmakers, J. A. M., van Rozen, A. J., Terpstra, G. K., Wassink, G. A., Kreukniet, J., Remeyer, L. R., Reeuwijk, H. J. E., Touw, D. J., Rollema, Hans, Mastebroex, Dora, Russel, F. G. M., Wouterse, A. C., Rijk, M. C. M., Salden, H. J. M., De Schaepdryver, A. F., Lefebvre, R. A., Bogaert, M. G., Scheres, H. M. E., Salden, H. J. H., Siero, H. L. M., Slee, P. H. Th. J., van den Berg, L., Huysmans, F. Th. M., Koene, R. A. P., Smits, J. F. M., Nievelstein, H. M. N., Struyker Boudier, H. A. J., Raaijmakers, J. A. H., Huidekoper, H. J., Thljssen, H. H. W., Baars, L. C. M., Mathy, M. J., Veldhoven, C. M. M., AriËns, E. J., Ruland, C. M., de Vos, Cor, de Graaf, Joop, van Aalst, Gerard, Steenbergen, Hans, Hekster, Y. A., Tijhuis, M. W., Nouws, J. F. M., Wollersheim, H., Fennis, J., van 't Laar, A., Wijnands, W. J., van der Gen, A., Jzerman, A. P. I., Aué, G., Dorlas, R., Krajnc, E. I., Loeber, J. G., van Leeuwen, F. X. R., Wester, P. W., Vos, J. G., Vaessen, H. A. M. G., Heijden, C. A. v. d., Canton, J. H., de Klerk, A., Krajc, E. I., Kruizinga, W., van Ommen, B., Rozing, J., van der Heijden, C. A., van der Voet, G. B., de Wolff, F. A., Edelbroek, Peter M., de Reus, Margot J. H., van den Berg, Tjeerd, and de Wolff, Frederik A.

Published
1984
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13. HPLC Method for the Determination of Chloroquine and its Main Metabolite in Biological Samples

Author

Augustijns, P. and Verbeke, N.

Abstract

An ion-pair reversed phase HPLC-method for the determination of chloroquine and desethylchloroquine in plasma, blood and filter-paper-absorbed blood spots is described.Using 75 μl samples, concentrations ranging from 2 to 1000 ng/ml can be measured.Intraday precision as well as interday precision are lower than 6 % (RSD).The filter-paper method could be used for the determination of chloroquine and desethylchloroquine in samples originating from areas with a lack of laboratory equipment.The procedure is sensitive enough to be used in monitoring of drug levels as well as for pharmacokinetic studies.

Published
1990
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14. A Microassay Method for the Determination of Theophylline in Biological Samples Using HPLC with Electrochemical Detection

Author

Augustijns, P. and Verbeke, N.

Abstract

A micro assay method is presented to measure theophylline plasma levels by HPLC with electrochemical detection.Plasma samples of 10 μl were sufficient to determine theophylline levels down to 0.2 μg/ml. Intraday and interday variations were lower than 4% and 6% respectively.This method was evaluated by comparison with an immuno assay and correlation was excellent. The method is sensitive enough to allow blood sampling by the finger prick method in order to perform monitoring of drug levels.

Published
1992
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16. Free radical scavenging properties of apomorphine enantiomers and dopamine: Possible implication in their mechanism of action in parkinsonism

Author

Sam, E. and Verbeke, N.

Abstract

The influence of R(-) apomorphine, S(+) apomorphine and deopamine on the oxidation kinetics of two polyunsaturated fatty acids (PUFA) (cholesteryl linoleate (CL) and Trilinolein (TL) was investigated The oxidation was initiated by free radicals generated through thermal decomposition of 2,2'-Azobis(2-methy-propionitrile) (AMPN) in phosphate buffer (pH 7.4) thermostated at 50°C. The hydroperoxides formed were determined by iodine titration using a diode array spectrophotometer at 290 nm.

Published
1995
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18. Catechol is the major product of salicylate hydroxylation in 1-methyl-4-phenylpyridinium ion treated rats

Author

Sam, E., Sarre, S., Michotte, Y., and Verbeke, N.

Abstract

Summary: Salicylate hydroxylation using hydroxyl free radicals results into formation of 2,3-dihydroxybenzoic acid, 2,5-dihydroxybenzoic acid and catechol. Inspite of the fact that in vitro experiments have shown that catechol is a minor product, we have shown by these in vivo studies that it is a substantial product. Since catechol as well as 2,3-dihydroxybenzoic acid have not been found to be produced enzymatically from salicylates, they appear useful as in vivo indicators for monitoring hydroxyl free radicals. Administration of 1-methyl-4-phenylpyridinium ion (MPP+) to rat striatum using microdialysis results into the formation of hydroxyl radicals. Salicylate perfusion enables the estimation of the three derivatives cited above. They increase d significantly after MPP+ administration in comparison to the baseline values, with catechol being the most significant. The maximum amounts were achieved 60 min after MPP+ administration, and the mean percentage increase at this time point were 83.1% for 2,3-DBA (n=6, P=0.005), 81.25% for 2,5-DBA (n=6, P=0.011) and 1228.8% for catechol (n=4, p=0.00008). MPP+ caused substantial decrease of dopamine metabolites. Dihydroxyphenylacetic acid decreased to 13% and homovanillic acid to 11.4%.We conclude that catechol is an important indicator of hydroxyl free radical formation in this animal model which is well suited to study the role of free radicals in Parkinsonism.

Published
1998
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20. Diminished sedation during diazepam treatment for chloroquine intoxication

Author

Croes, K., Augustijns, P., Sabbe, M., Desmet, K., and Verbeke, N.

Abstract

We report a case of a woman hospitalized after chloroquine overdose whose whole blood concentration on admission was 7.87?g/ml. High blood concentrations of chloroquine induce cardiotoxicity and have been associated with death when they exceed 3.0?g/ml. Early administration of massive doses of diazepam has been described to reduce the mortality due to chloroquine toxicity, but the protective mechanism has remained unknown. This patient was treated with diazepam (2.0 mg/kg over 30 min followed by a dosage of 1.0 to 2.0 mg/kg over 24 h), yet she remained awake despite the high plasma concentrations of diazepam and nordiazepam which would normally be associated with sedation. This suggests an antagonistic effect of chloroquine on the benzodiazepine-induced sedation due to an interaction between these drugs at their site of action.

Published
1993
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25. Determination of Artesunate by Capillary Electrophoresis with Low UV Detection and Possible Applications to Analogues

Author

DHulst, A., Augustijns, P., Arens, S., Van Parijs, L., Colson, S., Verbeke, N., and Kinget, R.

Abstract

A capillary electrophoretic method with low ultraviolet (185 nm) detection is presented for the analysis of both artesunate, a hemisuccinate ester analogue of artemisinin, and succinic acid without prior derivatization. Artesunate is easily separated from its ester hydrolysis products, succinic acid and dihydroartemisinin, with the use of phosphate electrolytes at neutral pH, and this makes the method suitable for ester stability monitoring or quality control purposes. Sensitivity is shown to be strongly influenced by electrolyte and sample matrix ionic concentration ratio, which illustrates the need for careful selection of the electrolyte when direct injection of isotonic sample solutions is considered. Alkaline derivatization, which is known to generate charged compounds, is found to be useful for the analysis of neutral artemisinin derivatives, as exemplified by experiments with dihydroartemisinin.

Published
1996
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