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11. Liquid chromatography coupled on-line to flow cytometry for Postcolumn Homogeneous biochemical detection

Author

Schenk, T., Molendijk, A., Irth, H., Tjaden, U. R., and van der Greef, J.

Subjects
Liquid chromatography -- Research, Chemistry
Abstract

The feasibility of flow cytometry as read-out principle for homogeneous cell- or bead-based assays coupled on-line to LC is demonstrated using digoxin-coated beads (Dig-Beads) and fluorescent-labeled anti-digoxin (AD-FITC) as model system. The assay is carried out in a postcolumn continuous-flow reaction detection system where the AD-FITC and Dig-Beads are simultaneously added to the eluate of an LC separation column. Binding of AD-FITC to Dig-Beads results in a constant amount of fluorescence associated with the beads, which is detected by the flow cytometer. The presence of active compounds, such as digoxin and its analogues, in the sample will results in a decrease of the AD-FITC-Dig-Bead complex and, consequently, in the bead-associated fluorescence. Hence, the bead-associated fluorescence detected is inversely related to the digoxin concentration. A data-handling algorithm was developed in-house for adequate analysis of raw data output from the flow cytometer. Various conditions that influence the performance of this novel LC-biochemical detection (LC-BCD) system were investigated to determine the optimal settings of the bead-based biochemical interaction. The optimized flow injection bead-based assay was capable of detecting very low concentrations of digoxigenin (0.5 nmol/L), digoxin (0.1 nmol/L), and gitoxigenin (50 nmol/L). The applicability of LC coupled on-line to flow cytometry was demonstrated by the individual detection of digoxin, digoxigenin, and gitoxigenin in a single LC analysis. The successful coupling of LC on-line to flow cytometry principally enables the use of a wide range of new homogeneous assay formats in LC-BCD, such as membrane-bound receptor assays, cell-binding assays, and functional cell-based assays. Next to the ability to use insoluble targets, and also multiplexing assays, i.e., performing a number of assays simultaneously, using color- or size-coded beads becomes at hand in LC-BCD.

Published
2003

15. Abstracts of lectures and posters pharmaceutical and biomedical analysis meeting

Author

Ackermans, Mariëtte, Endert, Erik, Aluoch, J., Ouintens, I., Roets, E., Hoogmartens, J., Barka, G., Opper, C., Kerkdijk, H., Witte, D. T., Bruggeman, F. J., Franke, J. P., Copinga, S., Jansen, J. M., de Zeeuw, R. A., Bosman, I. J., Ensing, K., Dekker, I., Dams, Ir. A. B. J. M., de Pooter, Ch. M. J., Fichtinger-Schepman, A. M. J., Scalliet, P. G., Maes, R. A., Berends, F., Van Oosterom, A. T., de Bruijn, E. A., Fay, L. A., Verstappen, C. J., Pluijms, W., Irth, H., Oosterkamp, A. J., van der Welle, W., Khan, K., Paesen, J., Jacobs, Peter L., de Vries, Marcel P., Lammers, Norbert, Biermans, Frans, de Witte, Eric, Mussche, Philippe, Lamoree, M. H., Reinhoud, N. J., Tjaden, U. R., Niessen, W. M. A., van der Greef, J., Solie, A., Paulus, Aran, Klockow, Antje, Bruin, Gerard J. M., Reubsaet, J. L. E., Beijnen, J. H., Bult, A., Teeuwsen, J., Koster, E. H. M., Waterval, J. C. M., Underberg, W. J. M., Cypers, W., Claeys, P., Simonian, M. H., Rongen, Herman A. H., van der Horst, Helma M., Bult, Auke, van Bennekom, Wout P., Šmisterová, J., Thoithi, G., Van Schepdael, A., Wouters, K., Herdewijn, P., Vendrig, D., Gout, E., van Santvoort, P. M. J., Hamelinck, R. L. A. E., van Zeeland, M. J. M., Janssen, P. S. L., Vervoort, R. J. M., Derksen, M. W. J., Maris, F. A., Yongxin, Zhu, Hendrix, C., Busson, R., and Janssen, G.

Published
1994
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30. The Discovery of Two Novel Biomarkers in a High-Fat Diet C56bl6 Obese Mouse Model for Non-Adipose Tissue: A Comprehensive LCMS Study at Hind Limb, Heart, Carcass Muscle, Liver, Brain, Blood Plasma and Food Composition Following a Lipidomics LCMS-Based Approach

Author

de Vries, Verheij, van der Greef J, and van Ginneken

Subjects
medicine.medical_specialty, business.industry, Adipose tissue, Type 2 diabetes, Hindlimb, medicine.disease, chemistry.chemical_compound, Endocrinology, chemistry, Diabetes mellitus, Internal medicine, Phosphatidylcholine, Blood plasma, Lipidomics, medicine, Immunology and Allergy, Biomarker (medicine), business
Abstract

Aim/Objective: This study was designed to find via a highfat (HF) diet induced insulin resistant (IR) and/or type-2 diabetes (T2DM) C57Bl/6 mouse model potential novel biomarkers. Major aiming is to find following this lipidomics based approach novel safe biomarkers applicable for humans with IR/T2DM that can be used in the assessment of diagnosis, intensive treatment, clinical use and new drug development. In addition, the biomarker has to be found in blood-plasma simultaneously while is not a component of the HF-diet. Methods: Reversed phase liquid chromatography coupled to mass spectrometry (LC-MS) were used to quantify and qualify the rearrangement and repartitioning of fat stores in the heart-, hind limb-, carcass-muscle, liver, brain, and blood plasma of this mice model following a systems biology lipidomics based approach. Results: Two potential biomarkers were found for this HFdiet mouse model. The first biomarker was a 20:3 cholesteryl-ester (20:3-ChE) which significantly increased (P ≤ 0.016) in the fatty heart with 1317% while it rose very significantly (P ≤ 0.00001) in blood plasma with 1013% in the HF diet group in comparison to the control-group. (Co). The second biomarker was a 36:1 phosphatidylcholine (36:1-PC), which rose significantly (P ≤ 0.025) mainly in heart muscle with 400% while concentrations increased significantly strongly (P ≤ 0.002) in blood plasma with 1493% in the high-fat diet vs. Co. As an earlier defined prerequisite, both compounds were not found in the food. Conclusion: The 20:3-ChE biomarker (dihomo-γ-linolenic; 20:3 n-6) has been classified as a potential type 2 diabetes biomarker (T2DM) biomarker in a human cohort of the uppsala longitudinal study of adult men (ULSAM). In addition, we give a biochemical explanation for the 36:1- PC as hypoxic biomarker for cardiovascular diseases (CVD) diagnosis and therapy. Both biomarkers are interesting candidates for further validation in human cohorts.

Published
2016
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31. Abstracts of papers Pharmaceutical and biomedical analysis meeting

Author

Both-Miedema, R., Jansen, E. H. J. M., Claessens, H. A., Hendriks, P. J. M., Ackermans, M. T., Sparidans, R. W., Everaerts, F. M., de Groot, G., Koops, R., Wubs, K. L., Koops, R., de Jong, J., Cheung, S. F., Maessen, P. A., Pinedo, H. M., van der Vijgh, W. J. F., den Hartigh, J., Langebroek, R., Vermeij, P., Doom, L., van Leeuwen, F. X. R., Heeremans, C. E. M., van der Hoeven, R. A. M., Niessen, W. M. A., Tjaden, U. R., van der Greef, J., Hempenius, J., Staal, B., Jeuring, H. J., Mensink, C. K., Jonkman, J. H. G., Hindriks, H., Maris, F., Pasters, A., de Smet, M., Massart, D., Janssen, P. S. L., Hamelinck, R. L. A. E., Melgers, P. A. T. A., van Nispen, J. W., van Zeeland, M. J. M., van de Ven, M. H. J. M., Vink, J., Lambrechts, H., Pattyn, G., Van Oosterom, A. T., de Bruijn, E. A., Leeuwenkamp, O. R., Barto, R., Greuter, H., Lips, P., Netelenbos, J. C., Maris, F. A., Vervoort, R. J. M., Vrieling, M. B., Reinerink, E. J. M., van den Berg, R. H., Roets, E., Aerden, L., Hoogmartens, I., Rose, S. V., Crombeen, J. P., van Bueren, L. G. D. Lammerts, Rosing, H., Elferink, F., van de Vaart, F. J., Schoots, A. C., De Vries, P. H. J. M., Verheggen, T. P. E. M., Steijger, O. M., Hoksbergen, E., Baumann, R. A., Holthuis, J. J. M., Brinkman, U. A. Th., Takkenberg, B., van Ingen, H. E., Ackermans, M., Endert, E., Tjaden, UR, Reeuwijk, HJEM, van der Greef, J., Pattyn, G., van Oosterom, A. T., de Bruijn, E. A., van de Water, C., Haagsma, N., van den Ham, W. A., Piersma, A. H., van Ginkel, L. A., Stephany, R. W., Farla, J. C. M., van Rossum, H. J., van Gijn, R., Beijnen, J. H., de Clippeleir, J. J. M., Horenblas, S., Underberg, W. J. M., van Tellingen, O., Beilnen, J. H., van der Woude, H. R., Nooven, W. J., van Twillert, K., Zeijlmans, P. W. M., Olling, M., Derks, H. G. J. M., Naidong, Weng, Cachet, Th., Hoogmartens, J., Wieling, J., Coencgracht, P. M. J., Doornbos, D. A., and Windhorst, G.

Published
1989
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32. Correlated measurement error hampers association network inference

Author

Kaduk, M., Hoefsloot, H.C.J., Vis, D.J., Reijmers, T., van der Greef, J., Smilde, A.K., Hendriks, M.M.W.B., and Biosystems Data Analysis (SILS, FNWI)

Subjects
Partial correlation, Complex networks, Liquid chromatography, Time series analysis, Biomedical Innovation, Cholesterol ester, Triacylglycerol, False positive result, Measurement error, Life, Metabolomics, Biology, False negative result, Indirect association, Chromatography, Lysophosphatidylcholine, Mass spectrometry, Data visualization, Fipid, Large amounts of data, Uncorrelated errors, Fatty acid, Lipid blood level, Triacylglycerol blood level, Normal human, Lipid metabolism, Measurement design, Lipidomics, Fatty acid blood level, Fatty acid desaturation, Measurement designs, Diacylglycerol, ELSS - Earth, Life and Social Sciences, MHR - Metabolic Health Research, Controlled study, Healthy Living, Figures-of-merit, Biological variation, Human
Abstract

Modern chromatography-based metabolomics measurements generate large amounts of data in the form of abundances of metabolites. An increasingly popular way of representing and analyzing such data is by means of association networks. Ideally, such a network can be interpreted in terms of the underlying biology. A property of chromatography-based metabolomics data is that the measurement error structure is complex: apart from the usual (random) instrumental error there is also correlated measurement error. This is intrinsic to the way the samples are prepared and the analyses are performed and cannot be avoided. The impact of correlated measurement errors on (partial) correlation networks can be large and is not always predictable. The interplay between relative amounts of uncorrelated measurement error, correlated measurement error and biological variation defines this impact. Using chromatography-based time-resolved lipidomics data obtained from a human intervention study we show how partial correlation based association networks are influenced by correlated measurement error. We show how the effect of correlated measurement error on partial correlations is different for direct and indirect associations. For direct associations the correlated measurement error usually has no negative effect on the results, while for indirect associations, depending on the relative size of the correlated measurement error, results can become unreliable. The aim of this paper is to generate awareness of the existence of correlated measurement errors and their influence on association networks. Time series lipidomics data is used for this purpose, as it makes it possible to visually distinguish the correlated measurement error from a biological response. Underestimating the phenomenon of correlated measurement error will result in the suggestion of biologically meaningful results that in reality rest solely on complicated error structures. Using proper experimental designs that allow for the quantification of the size of correlated and uncorrelated errors, can help to identify suspicious connections in association networks constructed from (partial) correlations. © 2014 Elsevier B.V. Chemicals/CAS: lipid, 66455-18-3; lysophosphatidylcholine, 93794-93-5

Published
2014

33. Abstracts of papers

Author

Barends, D. M., Lingeman, H., van der Doelen, W., Beek, W. M. J., Keukens, H. J., Aerts, M. M. L., Beijnen, J. H., Driebergen, R. J., Hodes, T. J. M., Holthuis, J. J. M., Reinhoudt, D. N., Underberg, W. J. M., Dams, A., de Groot, G., de Wildt, D. J., Lansemeyer, J. J. M., Sangster, B., Delbressine, L., Moonen, M., Oosterhout, M. v., Wagenaars, G., Kaspersen, F., De Smet, M., Van Belle, S., Storme, C., Massart, D. L., de Waal, H. A. J., Kraak, J. C., Haessen, F. J. M. J., Dreijer-van der Glas, S. M., Bult, A., Drenth, B. F. H., Hellingwerf, K. J., den Hartigh, J., Blauw, J. S., Beljnen, J. H., van Oort, W. J., Postma, S. J., Verboom, W., Lelieveid, P., Drost, R. H., van Ooijen, R. D., Ionescu, T. I., van Rossum, J. M., Maes, R. A. A., Elferink, F., van der Vijgh, W. J. F., Klein, I., Pinedo, H. M., Haagsma, N., Dieleman, B., Gortemaker, B. G. M., van de Water, C., Mengelers, M. J. B., Schreuder, C., Hulshoff, A., Jacobs, P. L., Scnmeits, G. J. H., Nieuwenhuyse, H., Vink, J., Jansen, H., van der Velde, E. G., Brinkman, U. A. Th., Frei, R. W., Veening, H., Kok, W. Th., Voogt, W. H., Kuijpers, P. H., Zeeman, J., de Jong, G. J., Musch, G., Muskiet, Frits A. J., Nibbering, N. M. M., Reeuwijk, H. J. E. M., Tjaden, U. R., Spanjers, L. G. C., de Kleijn, J. P., Kerkdijk, H. C., van de Laar, Gerrit L. M., Paanakker, Jan E., van der Houwen, O. A. G. J., Teeuwsen, J., Gorp, J. v., Salemink, P., Vermeulen, M., Kolkman, L., Welling, G. W., van der Zee, R., Wellinq-Wester, S., and van der Greef, J.

Published
1985
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36. Abstracts of papers Pharmaceutical and biomedical analysis meeting

Author

Bandhoe, A. U., Paalman, A. C. A., Underberg, W. J. M., Beijnen, J. H., Bekers, O., Otagiri, M., Bult, A., Beuman, Gert, van der Heijden, Jacques, Janss, Jenny, Ceelen, P. R. J., Feenstra-Bielders, G. G. L. M., Groeneveld, D. J., de Boer, D., Rutten, M. J. A., de Jong, E. G., Maes, R. A. A., van Rossum, J. M., de Groot, G., Kopps, R., Savelkoul, T. J. F., van Vloten, P., de Jonag, E. G., van Ooyen, R., Kiffers, J., de Kroon, I. F. I., Langendijk, P. N. J., de Goede, P. N. F. C., De Smet, M., Musch, C., Peeters, A., Buydens, L., Massart, D. L., De Turck, K., Cachet, Th., Hoogmartens, J., Delrue, M., Lannoo, P., Drenth, B. F. H., Beckeringh, F. J., Bosman, J., Feitsma, K. G., van Nijhuisvan Dam, A., Driebergen, R. J., van Gorp, J. A., Ensing, K., Farlam, A., de Jong, G. J., Frel, R. W., Brinkman, U. A. Th., Gerding, T. K., van de Grampel, V. J. M., Niemeijer, N. R., de Zeeuw, R. A., Tepper, P. G., Horn, A. S., Halvax, J. J., Wiese, G., van Bennekom, W. P., Hindriks, Rik, Buydens, Lutgarde, Peeters, Anne, de Smet, Marina, Massart, Luc, Blokland, Aric, Vink, Jan, Keizers, S., de Jong, E. G., Niessen, W. M. A., Verhey, E. R., LaVos, G. F., Tjaden, U. R., van der Greef, J., Ooms, J. A., Haak, G. S. J., Grooten, G., Pattyn, G., Sandra, P., David, F., van Oosterom, A. T., de Bruijn, E. A., Pouwelse, A. V., de Jong, D., Lammers, N. G. F. M., van den Berg, J. H. M., Quintens, I., Roets, E., Reeuwijk, H. J. E. M., Lingeman, H., Keizer, H. J., Rosing, H., Elferink, F., van de Vaart, F. J., Kloeg, P. H. A. M., Sauter, André, Stegehuis, D. S., Reinhoud, N. J., Steijger, O. M., Hilhorst, J. J. L., Holthuis, J. J. M., Underberg-Chitoe, U. K., Meenhorst, P. L., Van den Mooter, G., Hauchecorne, R., Vinckier, C., van der Horst, A., Martens, H. J. M., van der Horst, F. A. L., Post, M. H., van Ginkel, L. A., Zoontjes, P. W., van Blitterswijk, H., Stephany, R. W., van Gijn, R., Bakker, C. H., Koks, C. H. W., Rodenhuis, S., van Opstal, M. A. J., van den Horst, F. A. L., Krabbenborg, P., van Tellingen, O., Woude, H. R. v. d., van Beers, C. J. T., Nooyen, W. J., Varossieau, F. J., Los, G., Nagel, J. D., McVie, J. G., Veen, R. N., Land, J. T. Op 't, Vendrig, D. E. M. M., Teeuwsen, J., Verlaar, F. C. A. M., Trum, T. J. H. M., de Kleijn, J. P., Vervoort, R., Vrieling, M., Maris, F., Hindriks, H., Walhagen, A., Edholm, L. -E., Heeremans, C. E. M., and van der Hoeven, R. A. M.

Published
1989
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38. Abstracts of Dutch doctoral theses

Author

Navis, G. J., Sterk, G. J., van Nispen, J. W., Hichens, M., Sauter, A., Lingeman, H., van den Beld, C. M. B., Tjaden, U. R., van der Greef, J., Desiderio, D. M., Cubbins, D. C., McMartin, C., Webb, R. L., Wennogle, L. P., Wysowskyi, H. E., Zimmerman, M. B., Lee, V. H. L., Sandow, J., Seidel, H., Schmiedel, R., Keller, Bradley T., Smith, Kevin R., Borchardt, Ronald T., Banks, W. A., Kastin, A. J., de Wied, D., DeLuca, P. P., Robinson, J. R., Lundin, S., Vilhardt, H., Saffran, M., Kumar, G. S., Neckers, D. G., Williams, F., Field, J. B., Jones, R. H., Panepinto, L., Harris, A. S., Moses, Alan C., Muranishi, S., Boddé, H. E., Ponec, M., Verhoef, J., Liversidge, Gary G., Boer, G. J., Kruisbrink, J., de Nijs, H., Bouwman, T. R. M., Eenink, M. J. D., Patel, Harish M., Bundgaard, H., Larsen, J. D., Nielsen, M. N., Buur, A., Tjadeh, U. R., Lemaire, M., Andres, H., Marbach, P., Widlund, L., Guilbaud, O., Wilton, P., van Bree, J. B. M. M., Audus, K. L., Deinum, Johanna, Norén, Karin, Sohtell, Morgan, Weström, B. R., Folkesson, H. G., Karlsson, B. W., Damge, C., Michel, C., Aprahamian, M., Couvreur, P., Puisieux, F., Touitou, E., Alhaique, F., Fisher, P., Memoli, A., Riccieri, F. M., Santucci, E., Hermens, W. A. J. J., Romei jn, S. G., Merkus, F. W. H. H., Schneider, C., Smith, T. W., Bremecker, K. -D., Hungerer, K. -D., Tabata, Y., Ikada, Y., Uno, K., Muramatsu, S., Bruning, J. W., Claas, F. H. J., Kardol, M. J., van Ree, J. M., Rust, C. J. J., Verduyn, W., Wiegant, V. M., Wolterink, G., van Hoogdalem, E. J., Heijligers-Feijen, C. D., de Boer, A. G., Breimer, D. D., Lambalk, C. B., van Kessel, H., de Koning, J., van Dieten, J. A. M. J., van Rees, G. P., Schoemaker, J., Devissaguet J. -Ph., Orieu K., Dray F., Ezan E., Devissaguet J. Ph., Drieu K., Dray P., Ezah E., Barnfield, D. J., Barker, Y. K., Knott, S., Miles, G. S., Warrander, A., Adam, H. K., Barker, Y., Hutchinson, F. G., Milsted, R. A. V., Moore, R. H., Swaisland, A. J., Barke, Y., Porter, E. T., Holmes, B., Barnard, M., Beijnen, J. H., Lubbers, S. C. H., van der Houwen, O. A. G. J., Lobbezoo, M. W., Underberg, W. J. M., Cachet, Th., Roets, E., Hoogmartens, J., Vanderhaeghe, H., de Bree, H., van der Stel, D. J. K., Brockhoff, O. A. M., van Berkel, M. P., Sierat, K., de Groot, G., Tepas, B. C. A., de Noord, O. E., Hempenius, J., Coenegracht, P. M. J., Jonkman, J. H. G., Doornbos, D. A., De Schutter, J. A., De Moerloose, P., Delbressine, L. P. C., Kaspersen, F. M., Blokland, A., Duchateau, A. L. L., Verstappen, T. A., Hendricks, P. J. H., Elferink, F, Leeuwenkamp, O R, Pinedo, H M, vd Vijgh, W J F, Ensing, K., Bloemhof, D. A., In 't Hout, W. G., de Zeeuw, R. A., Feitsma, Karla G., Drenth, Ben F. H., de Zeeuw, Rokus A., Gerding, T. K., Drenth, B. F. H., Horn, A. S., Groen, C. P., Tipker, J., van den Bergh-Swart, J. K., Spruit, F. J., van den Berg, J. H. M., Bramel, E. H. Groot, Bekers, O., Otagiri, M., Janssen, P. S. L., Nispen, J. W. v., Melgers, P. A. T. A., Zeeland, M. J. M. v., Hamelinck, R. L. A. E., Goverde, B. C., Aalst, G. W. M. v., Kootstra, P. R., van den Broek, H. H., Hogendoorn, E. A., Goewie, C. E., Kwakman, P. J. M., Brinkman, U. A. Th., Frei, R. W., de Jong, G. J., Lammers, N. G. F. M., Lammers, N., Ruijten, H. M., de Jong, J., Maessen, P. A., Mross, K. B., Plnedo, H. M., van der Vljgh, W. J. F., Khan, Naeem Hasan, Hoogmartens, J., Rose, S. V., van Bueren, L. G. D. Lammerts, van Amsterdam, P. H., van Beek, H., Baars, A. J., van Ginkel, L. A., Steinbuch, H. M., van Rossum, H. J., van Blitterswijk, H., Zoontjes, P. W., Heeft, E. v. d., de Jong, A. J. P. M., Stephany, R. W., van Gijn, R., de Clippeleir, J. J. M., Verweij, S. L., Paalman, A. C. A., van Opstal, M. A. J., Krabbenborg, P., Holthuis, J. J. M., van Bennekom, W. P., Bult, A., Redegeld, F. A. M., Houdkamp, E., van de Water, C., Haagsma, N., van der Stel, D. J. K., Vendrig, D. E. M. M., Mekking, A., and Teeuwsen, J.

Published
1988
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39. Abstracts of posters symposium disposition and delivery of peptide drugs

Author

Bundgaard, H., Larsen, J. D., Nielsen, M. N., Buur, A., Lingeman, H., Tjadeh, U. R., van den Beld, C. M. B., van der Greef, J., Lemaire, M., Andres, H., Marbach, P., Widlund, L., Guilbaud, O., Wilton, P., van Bree, J. B. M. M., Audus, K. L., Deinum, Johanna, Norén, Karin, Sohtell, Morgan, Weström, B. R., Folkesson, H. G., Lundin, S., Karlsson, B. W., E. Touitou, Alhalque, F., Fisher, P., Memoli, A., Ricciari, F. M., Santucci, E., Hermens, W. A. J. J., Romeijn, S. G., Merkus, F. W. H. M., Schneider, C., Smith, T. W., Bremecker, K. -D., Hungerer, K. -D., Tabata, Y., Ikada, Y., Uno, K., Muramatsu, S., Bruning, J. W., Class, F. J. J., Kardol, M. J., van Ree, J. H., Rust, C. J. J., Verduyn, W., Wiagant, V. M., Wolterink, G., van Hoogdalem, E. J., Heijligers-Feijen, C. D., Verhoef, J., de Boer, A. D., Breimer, D. D., Lambalk, C. B., van Kessel, H., de Koning, J., van Dieten, J. A. M. J., van Rees, G. P., Schoemaker, J., Devissaguet, J -Ph., Drieu, K., Dray, F., Ezan, E., Barnfield, D. J., Barker, Y. K., Knott, S., Miles, G. S., Warrander, A., Adam, H. K., Barker, Y., Hutchinson, F. G., Milsted, R. A. V., Moore, R. H., Swaisland, A. J., Holmes, B., Moore, R. H., Barker, Y., and Porter, E. T.

Published
1988
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43. Similarities and differences in lipidomics profiles among healthy monozygotic twin pairs.

Author

Draisma, H.H.M., Reijmers, Th.H., Bobeldijk-Pastorova, I, Meulman, J.J., van Burk, G.F., Bartels, M., Ramaker, R., van der Greef, J., Boomsma, D.I., Hankemeier, T., Draisma, H.H.M., Reijmers, Th.H., Bobeldijk-Pastorova, I, Meulman, J.J., van Burk, G.F., Bartels, M., Ramaker, R., van der Greef, J., Boomsma, D.I., and Hankemeier, T.

Abstract

Differences in genetic background and/or environmental exposure among individuals are expected to give rise to differences in measurable characteristics, or phenotypes. Consequently, genetic resemblance and similarities in environment should manifest as similarities in phenotypes. The metabolome reflects many of the system properties, and is therefore an important part of the phenotype. Nevertheless, it has not yet been examined to what extent individuals sharing part of their genome and/or environment indeed have similar metabolomes. Here we present the results of hierarchical clustering of blood plasma lipid profile data obtained by liquid chromatographymass spectrometry from 23 healthy, 18-year-old twin pairs, of which 21 pairs were monozygotic, and 8 of their siblings. For 13 monozygotic twin pairs, within-pair similarities in relative concentrations of the detected lipids were indeed larger than the similarities with any other study participant. We demonstrate such high coclustering to be unexpected on basis of chance. The similarities between dizygotic twins and between nontwin siblings, as well as between nonfamilial participants, were less pronounced. In a number of twin pairs, within-pair dissimilarity of lipid profiles positively correlated with increased blood plasma concentrations of C-reactive protein in one twin. In conclusion, this study demonstrates that in healthy individuals, the individual genetic background contributes to the blood plasma lipid profile. Furthermore, lipid profiling may prove useful in monitoring health status, for example, in the context of personalized medicine. © 2008 Mary Ann Liebert, Inc.

Published
2008
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47. Discovery of early-stage biomarkers for diabetic kidney disease using ms-based metabolomics (FinnDiane study)

Author

van der Kloet, F. M., primary, Tempels, F. W. A., additional, Ismail, N., additional, van der Heijden, R., additional, Kasper, P. T., additional, Rojas-Cherto, M., additional, van Doorn, R., additional, Spijksma, G., additional, Koek, M., additional, van der Greef, J., additional, Mäkinen, V. P., additional, Forsblom, C., additional, Holthöfer, H., additional, Groop, P. H., additional, Reijmers, T. H., additional, and Hankemeier, T., additional

Published
2011
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48. Direct peptide profiling by mass spectrometry of single identified neurons reveals complex neuropeptide-processing pattern

Author

Kw, Li, Rm, Hoek, Smith F, Cr, Jiménez, Rc, Schors, Peter van Veelen, Chen S, van der Greef J, Dc, Parish, and Pr, Benjamin

Subjects
Neurons, Molecular Sequence Data, Neuropeptides, Chromatography, Gel, Animals, Amino Acid Sequence, Protein Precursors, Peptide Mapping, Protein Processing, Post-Translational, Mass Spectrometry, Peptide Fragments, Ganglia, Invertebrate, Lymnaea
Abstract

A novel strategy combining peptide fingerprinting of single neurons by matrix-assisted laser desorption ionization mass spectrometry, molecular cloning, peptide chemistry, and electrospray ionization mass spectrometry was used to study the intricate processing pattern of a preprohormone expressed in identified neurons, the neuroendocrine light yellow cells (LYCs) of the gastropod mollusc, Lymnaea stagnalis. The cDNA encoding the precursor, named prepro-LYCP (LYCPs, light yellow cell peptides), predicts a straightforward processing into three peptides, LYCP I, II, and III, at conventional dibasic processing sites flanking the peptide domains on the precursor. However, matrix-assisted laser desorption ionization mass spectrometry of single LYCs revealed trimmed variant peptides derived from LYCP I and II. The variants were much more abundant than the intact peptides, indicating that LYCP I and II serve as intermediates in a peptide-processing sequence. Using the molecular masses of the peptides as markers to guide their isolation by well established purification methods, the structural identities of the peptides could be confirmed by amino acid sequencing. Furthermore, matrix-assisted laser desorption ionization mass spectrometry could detect colocalization of a novel peptide with the LYCPs.

Published
1994

49. Neuropeptide expression and processing as revealed by direct matrix-assisted laser desorption ionization mass spectrometry of single neurons

Author

Cr, Jiménez, Peter van Veelen, Kw, Li, Wc, Wildering, Wp, Geraerts, Ur, Tjaden, and van der Greef J

Subjects
Nerve Endings, Neurons, Invertebrate Hormones, Lasers, Neuropeptides, Nervous System, Axons, Mass Spectrometry, Animals, Calcium, Female, Protein Precursors, Protein Processing, Post-Translational, Lymnaea
Abstract

Neuropeptides were directly detected in single identified neurons and the neurohemal area of peptidergic (neuroendocrine) systems in the Lymnaea brain by using matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS). The samples were placed in matrix solution and ruptured to allow mixing of cell contents with the matrix solution. After formation of matrix crystals, the analytes were analyzed by MALDI-MS. It was surprising that clean mass spectra were produced, displaying extreme sensitivity of detection. In one of the neuroendocrine systems studied, we could demonstrate for the first time, by comparing the peptide patterns of soma and of neurohemal axon terminals, that processing of the complex prohormone expressed in this system occurs entirely in the soma. In the other system studied, novel peptides could be detected in addition to peptides previously identified by conventional molecular biological and peptide chemical methods. Thus, complex peptide processing and expression patterns could be predicted that were not detected in earlier studies using conventional methods. As the first MALDI-MS study of direct peptide fingerprinting in the single neuron, these experiments demonstrate that MALDI-MS forms a new and valuable approach to the study of the synthesis and expression of bioactive peptides, with potential application to single-cell studies in vertebrates, including humans.

Published
1994

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