Home Life sciences and mass spectrometry: some personal reflections
Article
Licensed
Unlicensed Requires Authentication

Life sciences and mass spectrometry: some personal reflections

  • Jasna Peter-Katalinic

    Jasna Peter-Katalinic received her PhD at the University of Zuerich, Switzerland. She is retired associated professor from Institute for Medical Physics and Biophysics at the University of Münster, and retired full professor at the University of Rijeka, Croatia. She served as the acting director of IMPB from April 2003 to May 2004, received 1st Life Science Prize of the German Society for Mass Spectrometry in 2002, and was from 2015 to 2020 the 1st president of the Croatian Proteomics Society.

     ORCID logo EMAIL logo
Published/Copyright: October 5, 2021
Biological Chemistry
From the journal Biological Chemistry Volume 402 Issue 12

Abstract

Molecular analysis of biological systems by mass spectrometry was in focus of technological developments in the second half of the 20th century, in which the issues of chemical identification of high molecular diversity by biophysical instrumental methods appeared as a mission impossible. By developing dialogs between researchers dealing with life sciences and medicine on one side and technology developers on the other, new horizons toward deciphering, identifying and quantifying of complex systems became a reality. Contributions toward this goal can be today considered as pioneering efforts delivered by a number of researchers, including generations of motivated students and associates.

Keywords: hyphenation; life sciences; mass spectrometry; omics; separation methods
Corresponding author: Jasna Peter-Katalinic, Institute for Medical Physics and Biophysics (IMPB), University of Münster, Robert-Koch-Str. 31, D-48149 Münster, Germany; and Department of Biotechnology, University of Rijeka, Radmile Matejcic 2, 51000 Rijeka, Croatia, E-mail:

This article is a contribution to the issue highlighting the 25th Anniversary of the Interdisciplinary Centre for Clinical Research (IZKF) Münster.

Funding source: Deutsche Forschungsgemeinschaft http://dx.doi.org/10.13039/501100001659

Award Identifier / Grant number: PE 415/14-1

Funding source: Deutsche Krebshilfe http://dx.doi.org/10.13039/501100005972

Funding source: Ministry of Science and Technology, Croatia http://dx.doi.org/10.13039/501100006589

Funding source: European Commission http://dx.doi.org/10.13039/501100000780

About the author

Jasna Peter-Katalinic

Jasna Peter-Katalinic received her PhD at the University of Zuerich, Switzerland. She is retired associated professor from Institute for Medical Physics and Biophysics at the University of Münster, and retired full professor at the University of Rijeka, Croatia. She served as the acting director of IMPB from April 2003 to May 2004, received 1st Life Science Prize of the German Society for Mass Spectrometry in 2002, and was from 2015 to 2020 the 1st president of the Croatian Proteomics Society.

Acknowledgments

Warm thanks to all members of my group “Biomedical Analysis” (1996–2008), guest scientists and to all collaborators at WWU Muenster and beyond. The here reviewed work was inspired initially joining the laboratory of H. Egge at the U. Bonn (1982), the Institute for Medical Physics and Biophysics (IMPB) at WWU Muenster led by F. Hillenkamp (1996) and Department of Biotechnology, U. Rijeka, Croatia (2009).

  1. Author contributions: All the authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.

  2. Research funding: My research was enabled through generous financial support by U. Muenster and IMPB QTOF instrument grant (HbfG) (1997), German Research Foundation (Deutsche Forschungsgemeinschaft, DFG, grant PE 415/14-1 to J.P.-K. 1999, Sonderforschungsbereich SFB 492 project Z2: 2000–2002 and 2003–2005 to J.P.-K.), Interdisciplinary Center for Clinical Research (IZKF C10 1998–2001, H1 2002–2004), Innovative Medical Research (IMF, projects PE 1 1 I/97-1, PE 5 2 98/01, PE 4 1 00/03, PE 4 2 00 02, PE 5 1 02 01 to J.P.-K), Deutsche Krebshilfe (coPI-grant I0-2041-Br I), EU (collaborative grant to A. Malorni, U. Napoli, Italy 1997–1999, FP6 GLYFDIS – Glycans in Body Fluids – Potential for Disease Diagnostics, 2006–2010), Nano2Life (EU FP6 LOCCANDIA – Lab-on-Chip based protein profiling for CANcer DIAgnosis, 2006–2009), DFG: Understanding Structure/Function Relationships of Carbohydrate/Protein-Interactions (MCGS) First Indo-German graduate school 2009–2013, and the Croatian Science Foundation (HRZZ, to J.P.-K., 2011–2013). The MS lab at U. Rijeka was financed by an infrastructure grant from Croatian Ministry of Science and Sports, as a partner of the WorldBank, to U. Rijeka (2012). J.P.-K. is retired from Institute of Medical Physics and Biophysics, University of Muenster, Germany (2008) and from Department of Biotechnology, University of Rijeka, Croatia (2013).

  3. Conflict of interest statement: The authors declare no conflicts of interest regarding this article.

References

Barber, M., Bordoli, R.S., Sedgwick, R.D., and Tyler, A.N. (1981). Fast atom bombardment of solids as an ion source in mass spectrometry. Nature 293: 270–275, https://doi.org/10.1038/293270a0.Search in Google Scholar

Bartkowiak, K., Wieczorek, M., Buck, F., Harder, S., Moldenhauer, J., Effenberger, K.E., Pantel, K., Peter-Katalinic, J., and Brandt, B.H. (2009). Two-dimensional differential gel electrophoresis of a cell line derived from a breast cancer micrometastasis revealed a stem/progenitor cell protein profile. J. Proteome Res. 8: 2004–2014, https://doi.org/10.1021/pr8009758.Search in Google Scholar

Bartkowiak, K., Effenberger, K.E., Harder, S., Andreas, A., Buck, F., Pantel, K., Peter-Katalinic, J., and Brandt, B.H. (2010). Discovery of a novel unfolded protein response phenotype of cancer stem/progenitor cells from the bone marrow of breast cancer patients. J. Proteome Res. 9: 3158–3168, https://doi.org/10.1021/pr100039d.Search in Google Scholar

Bindila, L., Steiner, K., Mormann, M., Schäffer, C., Messner, P., and Peter-Katalinic, J. (2007). Sequencing of O-glycopeptides derived from S-layer glycoproteins containing very large carbohydrate chains by Fourier transform ion cyclotrone resonance infrared multiphoton dissociation mass spectrometry. Anal. Chem. 79: 3271–3279, https://doi.org/10.1021/ac0617363.Search in Google Scholar

Bruntz, R., Dabrowski, U., Dabrowski, J., Ebersold, A., Peter-Katalinic, J., and Egge, H. (1988). Fucose-containing oligosaccharides from human milk from a donor of blood group 0 Lea nonsecretor. Biol. Chem. Hoppe-Seyler 369: 257–273, https://doi.org/10.1515/bchm3.1988.369.1.257.Search in Google Scholar

Čaval, T., Heck, A.J.R., and Reiding, K.R. (2021). Meta-heterogeneity: evaluating and describing the diversity in glycosylation between sites on the same glycoprotein. Mol. Cell. Proteomics 20: 1–14.10.1074/mcp.R120.002093Search in Google Scholar

Cederkvist, H., Zamfir, A., Bahrke, S., Eijsink, V.G.H., Sorle, M., Peter-Katalinic, J., and Peter, M.G. (2006). Identification of a high-affinity binding oligosaccharide by (+) nanospray quadrupole time-of-flight mass spectrometry of a non-covalent enzyme-ligand complex. Angew. Chem. Int. Ed. 45: 2429–2434, https://doi.org/10.1002/anie.200503168.Search in Google Scholar

Chughtai, K. and Heeren, R.M.A. (2010). Mass spectrometric imaging for biomedical tissue analysis. Chem. Rev. 110: 3237–3277, https://doi.org/10.1021/cr100012c.Search in Google Scholar

Dreisewerd, K. (2014). Recent methodological advances in MALDI mass spectrometry. Anal. Bioanal. Chem. 406: 2261–2278, https://doi.org/10.1007/s00216-014-7646-6.Search in Google Scholar

Egge, H., Kordowicz, M., Peter-Katalinic, J., and Hanfland, P. (1985a). Immunochemistry of I/i-active oligo- and polyglycosyl-ceramides from rabbit erythrocyte membranes. J. Biol. Chem. 260: 4927–4935, https://doi.org/10.1016/s0021-9258(18)89161-x.Search in Google Scholar

Egge, H., Peter-Katalinic, J., Reuter, G., Schauer, R., Ghidoni, R., Sonnino, S., and Tettamanti, G. (1985b). Analysis of gangliosides using fast atom bombardment mass spectrometry. Chem. Phys. Lipids 37: 127–141, https://doi.org/10.1016/0009-3084(85)90080-5.Search in Google Scholar

Egge, H. and Peter-Katalinic, J. (1987). Fast atom bombardment mass spectrometry for structural elucidation of glycoconjugates. Mass Spectrom. Rev. 6: 331–393, https://doi.org/10.1002/mas.1280060302.Search in Google Scholar

Fenn, J.B., Mann, M., Meng, C.K., Wong, S.F., and Whitehouse, C.M. (1989). Electrospray ionization for mass spectrometry of large biomolecules. Science 246: 64–71, https://doi.org/10.1126/science.2675315.Search in Google Scholar

Froesch, M., Bindila, L., Zamfir, A., and Peter-Katalinic, J. (2003). Sialylation analysis of O-glycosylated sialylated peptides from urine of patients suffering from Schindler’s disease by Fourier transform ion cyclotron resonance mass spectrometry and sustained off-resonance irradiation collision-induced dissociation. Rapid Commun. Mass Spectrom. 17: 2822–2832, https://doi.org/10.1002/rcm.1273.Search in Google Scholar

Hillenkamp, F. and Peter-Katalinic, J. (Eds.) (2007). MALDI MS: a practical guide to instrumentation, methods and applications, 1st ed. Wiley-VCH, Weinheim, p. 345; 2nd revised ed. (2013), 480 pages, Wiley-VCH, Weinheim.Search in Google Scholar

Hofsteenge, J., Huwiler, K., Maček, B., Hess, D., Lawler, J., Mosher, D., and Peter-Katalinic, J. (2001). C-mannosylation and O-fucosylation of the thrombospondin type I module. J. Biol. Chem. 276: 6485–6498, https://doi.org/10.1074/jbc.m008073200.Search in Google Scholar

Karas, M. and Hillenkamp, F. (1988). Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Anal. Chem. 60: 2299–2301, https://doi.org/10.1021/ac00171a028.Search in Google Scholar

Kirsch, S., Zarei, M., Cindrić, M., Müthing, J., Bindila, L., and Peter-Katalinic, J. (2008). On-line nanoHPLC/QTOF MS and tandem MS for separation, detection and accurate structural elucidation of human erythrocytes neutral glycosphingolipid mixture. Anal. Chem. 80: 4711–4722, https://doi.org/10.1021/ac702175f.Search in Google Scholar

Kniep, B., Peter-Katalinic, J., Müthing, J., Majdic, O., Pickl, W.F., and Knapp, W. (1996). The CDw65 monoclonal antibodies VIM-8 and VIM-11 bind to the neutral glycolipid V3FucnLc8Cer. J. Biochem. 119: 456–462, https://doi.org/10.1093/oxfordjournals.jbchem.a021263.Search in Google Scholar

Mann, M. and Wilm, M.S. (1994). Error tolerant identification of peptides in sequence databases by peptide sequence tags. Anal. Chem. 66: 4390–4399, https://doi.org/10.1021/ac00096a002.Search in Google Scholar

Metelmann, W., Müthing, J., and Peter-Katalinic, J. (2000). NanoESI-QTOF MS/MS analysis of a ganglioside mixture from human granulocytes. Rapid Commun. Mass Spectrom. 14: 543–550, https://doi.org/10.1002/(sici)1097-0231(20000415)14:7<543::aid-rcm908>3.0.co;2-j.10.1002/(SICI)1097-0231(20000415)14:7<543::AID-RCM908>3.0.CO;2-JSearch in Google Scholar

Metelmann, W., Vukelic, Z., and Peter-Katalinic, J. (2001). Nano-ESI quadrupole time-of-flight mass spectrometry of gangliosides from human brain tissue. J. Mass Spectrom. 36: 21–29, https://doi.org/10.1002/jms.100.Search in Google Scholar

Mormann, M., Maček, B., Gonzalez de Peredo, A., Hofsteenge, J., and Peter-Katalinic, J. (2004). Structural studies on protein O-fucosylation by electron capture dissociation. Int. J. Mass Spectrom. 234: 11–21, https://doi.org/10.1016/j.ijms.2003.12.005.Search in Google Scholar

Münzenberg, G. (2013). Development of mass spectrometers from Thomson and Aston to present. Int. J. Mass Spectrom. 349–350: 9–18, https://doi.org/10.1016/j.ijms.2013.03.009.Search in Google Scholar

National Research Council (2000). Committee on mapping and sequencing the human genome. Mapping and sequencing the human genome. Washington, DC: National Academy Press.Search in Google Scholar

Pandey, A. and Mann, M. (2000). Proteomics to study genes and genomes. Nature 405: 837–846, https://doi.org/10.1038/35015709.Search in Google Scholar

Pfannschmidt, G., Peter-Katalinic, J., Kordowicz, M., Egge, H., Dabrowski, J., Dabrowski, U., and Hanfland, P. (1984). Structures of fucose-containing ceramide pentasaccharides from the plasma of blood group 0 Le(a-b-) nonsecretors. FEBS (Fed. Eur. Biochem. Soc.) Lett. 174: 55–60, https://doi.org/10.1016/0014-5793(84)81077-7.Search in Google Scholar

Sagi, D., Schottstädt, C., Lesiewicz, K., Marquardt, T., and Peter-Katalinic, J. (2005). Glycoproteomics of N-glycosylation by in-gel deglycosylation and MALDI-TOF MS mapping: application to congenital disorder of glycosylation (CDG). Proteomics 5: 2689–2701.10.1002/pmic.200401312Search in Google Scholar PubMed

Sharon, M. and Robinson, C.V. (2007). The role of mass spectrometry in structure elucidation of dynamic protein complexes. Annu. Rev. Biochem. 76: 167–193, https://doi.org/10.1146/annurev.biochem.76.061005.090816.Search in Google Scholar PubMed

Steentoft, C., Bennett, E.P., Schjoldager, K.T.B.G., Vakhrushev, S.Y., Wandall, H.H., and Clausen, H. (2014). Precision genome editing: a small revolution for glycobiology. Glycobiology 24: 663–680, https://doi.org/10.1093/glycob/cwu046.Search in Google Scholar PubMed

Vakhrushev, S.Y., Mormann, M., and Peter-Katalinic, J. (2006). Identification of glycoconjugates from urine of patients suffering from congenital disorders of glycosylation by high resolution mass spectrometry and computer-assisted calculations. Proteomics 6: 983–992, https://doi.org/10.1002/pmic.200500051.Search in Google Scholar PubMed

Vakhrushev, S.Y., Langridge, J., Campusano, I., Hughes, C., and Peter-Katalinic, J. (2008). Ion mobility mass spectrometry analysis of human glycourinome. Anal. Chem. 80: 2506–2513, https://doi.org/10.1021/ac7023443.Search in Google Scholar PubMed

van Diggelen, O.P., Schindler, D., Kleijer, W.J., Huijmans, J.M.G., Galjaard, H., Linden, H.U., Peter-Katalinic, J., Egge, H., Dabrowski, U., and Cantz, M. (1987). Lysosomal α-N-acetylgalactosaminidase deficiency: a new inherited metabolic disease. Lancet 3: 804, https://doi.org/10.1016/s0140-6736(87)92542-6.Search in Google Scholar

Vukelic, Z., Metelmann, W., Müthing, J., Kos, M., and Peter-Katalinic, J. (2001). Anencephaly: structural characterization of gangliosides in defined brain regions. Biol. Chem. 382: 259–274, https://doi.org/10.1515/bc.2001.033.Search in Google Scholar

Vukelic, Z., Zarei, M., Peter-Katalinic, J., and Zamfir, A. (2006). Analysis of human hippocampus gangliosides by fully-automated chip-based nanoelectrospray tandem mass spectrometry. J. Chromatogr. A 1130: 238–245.10.1016/j.chroma.2006.05.033Search in Google Scholar

Wieruszeski, J.M., Chekkor, A., Bouquelet, S., Montreuil, J., Strecker, G., Peter-Katalinic, J., and Egge, H. (1985). Structure of two new oligosaccharides isolated from human milk: sialylated lacto-N-fucopentaoses I and II. Carbohydr. Res. 137: 127–138, https://doi.org/10.1016/0008-6215(85)85154-5.Search in Google Scholar

Zamfir, A., Vakhrushev, S., Sterling, A., Niebel, H.-J., Allen, M., and Peter-Katalinic, J. (2004a). Fully automated chip-based mass spectrometry for complex carbohydrate system analysis. Anal. Chem. 76: 2046–2054, https://doi.org/10.1021/ac035320q.Search in Google Scholar PubMed

Zamfir, A., Seidler, D.G., Schönherr, E., Kresse, H., and Peter-Katalinic, J. (2004b). On-line sheathless capillary electrophoresis/nanospray ionization mass spectrometry for the analysis of glycosaminoglycan oligosaccharides. Electrophoresis 25: 2010–2016, https://doi.org/10.1002/elps.200405925.Search in Google Scholar PubMed

Zamfir, A., Bindila, L., Lion, N., Allen, M., Girault, H.H., and Peter-Katalinic, J. (2005). Chip electrospray mass spectrometry for carbohydrate analysis. Electrophoresis 26: 3650–3673, https://doi.org/10.1002/elps.200500101.Search in Google Scholar PubMed

Zarei, M., Kirsch, S., Müthing, J., Bindila, L., and Peter-Katalinic, J. (2008). Automated normal phase – nano high performance liquid chromatography/matrix assisted laser desorption/ionization mass spectrometry for analysis of neutral and acidic glycosphingolipids. Anal. Bioanal. Chem. 391: 289–297, https://doi.org/10.1007/s00216-008-1932-0.Search in Google Scholar PubMed

Zhang, B. and Kuester, B. (2019). Proteomics is not an island: multi-omics integration is the key to understanding biological systems. Mol. Cell. Proteomics 18: S1–S8, https://doi.org/10.1074/mcp.e119.001693.Search in Google Scholar
Received: 2021-04-29
Accepted: 2021-09-15
Published Online: 2021-10-05
Published in Print: 2021-11-25

© 2021 Walter de Gruyter GmbH, Berlin/Boston

Articles in the same Issue

  1. Frontmatter
  2. Highlight: Molecular Determinants of Health and Disease - 25th Anniversary of the InterdisciplinaryCenter Clinical Research Münster
  3. Molecular determinants of health and disease
  4. Role of the gut microbiota in airway immunity and host defense against respiratory infections
  5. Dynamic phospho-modification of viral proteins as a crucial regulatory layer of influenza A virus replication and innate immune responses
  6. Molecular mechanisms of vasculopathy and coagulopathy in COVID-19
  7. Astrocytic potassium and calcium channels as integrators of the inflammatory and ischemic CNS microenvironment
  8. Epitranscriptomic modifications in acute myeloid leukemia: m6A and 2′-O-methylation as targets for novel therapeutic strategies
  9. Molecular determinants of therapy response of venetoclax-based combinations in acute myeloid leukemia
  10. Pseudomonas aeruginosa and Staphylococcus aureus virulence factors as biomarkers of infection
  11. Controllers of cutaneous regulatory T cells: ultraviolet radiation and the skin microbiome
  12. The paracaspase MALT1 in psoriasis
  13. The cAMP responsive element modulator (CREM) is a regulator of CD4+ T cell function
  14. Quantifying salt sensitivity
  15. Life sciences and mass spectrometry: some personal reflections
https://doi.org/10.1515/hsz-2021-0244
Keywords for this article
hyphenation; life sciences; mass spectrometry; omics; separation methods

Articles in the same Issue

  1. Frontmatter
  2. Highlight: Molecular Determinants of Health and Disease - 25th Anniversary of the InterdisciplinaryCenter Clinical Research Münster
  3. Molecular determinants of health and disease
  4. Role of the gut microbiota in airway immunity and host defense against respiratory infections
  5. Dynamic phospho-modification of viral proteins as a crucial regulatory layer of influenza A virus replication and innate immune responses
  6. Molecular mechanisms of vasculopathy and coagulopathy in COVID-19
  7. Astrocytic potassium and calcium channels as integrators of the inflammatory and ischemic CNS microenvironment
  8. Epitranscriptomic modifications in acute myeloid leukemia: m6A and 2′-O-methylation as targets for novel therapeutic strategies
  9. Molecular determinants of therapy response of venetoclax-based combinations in acute myeloid leukemia
  10. Pseudomonas aeruginosa and Staphylococcus aureus virulence factors as biomarkers of infection
  11. Controllers of cutaneous regulatory T cells: ultraviolet radiation and the skin microbiome
  12. The paracaspase MALT1 in psoriasis
  13. The cAMP responsive element modulator (CREM) is a regulator of CD4+ T cell function
  14. Quantifying salt sensitivity
  15. Life sciences and mass spectrometry: some personal reflections
Sign up now to receive a 20% welcome discount
Institutional Access
How does access work?
Have an idea on how to improve our website?
Please write us.
© 2025 De Gruyter Brill
Downloaded on 6.9.2025 from https://www.degruyterbrill.com/document/doi/10.1515/hsz-2021-0244/html
Scroll to top button