Albert J. R. Heck

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Albert J.R. Heck
AlbertHeck.jpg
Born (1964-11-25) 25 November 1964 (age 59)
Goes, The Netherlands
NationalityDutch
Alma mater University of Amsterdam
Known forProteomics, Native Mass Spectrometry
Awards Descartes-Huygens Prize (2006)
Spinoza Prize (2017)
Sir Hans Krebs Medal (2018)
Scientific career
Fields Physics, Chemistry, Biology
Institutions Utrecht University, University of Warwick, Stanford University, University of Amsterdam
Doctoral advisor Nico M. M. Nibbering

Albert J.R. Heck (born 25 November 1964) is a Dutch scientist and professor at Utrecht University, the Netherlands in the field of mass spectrometry and proteomics. He is known for his work on technologies to study proteins in their natural environment, with the aim to understand their biological function. Albert Heck was awarded the Spinoza Prize in 2017, the highest scientific award in the Netherlands.

Contents

Biography

Albert Heck was born in Goes, Netherlands. He studied chemistry at the VU University in Amsterdam, and received his PhD degree from the University of Amsterdam in 1993. After a postdoctoral period at Stanford University in the lab of Richard Zare and Sandia National Laboratories (Livermore) he became a postdoctoral fellow and later lecturer at University of Warwick.

In 1998 he accepted a chair at Utrecht University as head of the Biomolecular Mass Spectrometry and Proteomics Group. [1] His group is part of the Departments of Chemistry and Pharmaceutical Sciences of the Faculty of Science. [2] From 2006 until 2012 Heck was scientific director of the Bijvoet Centre for Biomolecular Research, and from 2015 to 2018 scientific director of the Utrecht Institute for Pharmaceutical Science at Utrecht University. In 2017 he received a Distinguished Faculty professorship of Utrecht University. [3]

Research

The research of Albert Heck is focused on the development and use of mass spectrometry to study all cellular proteins. Within his research group, there are three main lines of research, improvement of instrumentation and analytical methods, proteomics and mass spectrometry based structural biology, including native protein mass spectrometry and cross-linking mass spectrometry.

Albert Heck is regarded as one of the pioneers of native mass spectrometry. [4] [5] [6] Among the complexes that he studied using native mass spectrometry are intact viruses of up to 18 megadalton, [7] [8] ribosomes, [9] antibodies in complex with their antigens [10] or proteins of the complement system. [11] [12] He has developed, in collaboration with Alexander Makarov mass spectrometers with extended mass ranges, specifically suited for the analyses of very large protein complexes, which were later commercialized by the company ThermoFisher Scientific as the Orbitrap EMR and UHMR.

In proteomics, Heck is most renowned for his work on quantitative proteomics, [13] [14] interactomics, [15] and the analysis of post-translational modification of proteins using mass spectrometry, with a focus on protein phosphorylation [16] and protein glycosylation. [17] This started with the introduction of the material TiO2 as a method for the targeted analysis of phosphopeptides in 2004. [18] The methods developed by Heck have been adopted by many scientists in other fields, to study how protein expression and phosphorylation are regulated in human cells and tissues by different biological processes and disease states. [19] [20]

Additionally, he advocated the use of complementary proteases in shot-gun proteomics [21] [22] and he introduced and developed novel peptide fragmentation strategies to elucidate site specific post-translational modifications. [23] The latter improves determination of peptide and protein sequence information, which is particular helpful for the analysis of glycopeptides [24] and HLA antigens. [25] [26] Heck also contributed to the field of cross-linking mass spectrometry, through proteome wide cross-linking experiments, [27] and the development of novel fragmentation methods and the software suite XlinkX. [28]

Albert Heck is closely involved in coordinating access to proteomics infrastructures in the Netherlands and in Europe. Since 2003 Heck is scientific director of the Netherlands Proteomics Centre. [29] From 2011 to 2015 he was coordinator of PRIME-XS, [30] and since 2019 he coordinates EPIC-XS, [31] both collaborative projects funded by the European Union to enable access to proteomics technology for researchers throughout Europe.

Honours and awards

Heck received numerous awards and prizes for his scientific contributions. He received The KNCV golden medal in 2001, [32] the Descartes-Huygens Prize from the Académie de Sciences in 2006, [33] the Life Science Award of the German Mass Spectrometry Society in 2010, the Discovery Award in Proteomic Sciences from the Human Proteome Organization in 2013 [34] and the UePA Pioneer Proteomics Award in 2014.

Since 2014 he is a member of the European Molecular Biology Organization. [35] [36] In 2014, Heck was elected a member of the Royal Netherlands Academy of Arts and Sciences. [37] The American Chemical Society honoured Albert Heck with the 'Frank H. Field and Joe L. Franklin Award for Outstanding Achievements in Mass Spectrometry' in 2015. [38]

In 2017, he was awarded the Spinoza Prize, the highest scientific distinction in the Netherlands for his "major contribution to the worldwide breakthrough of systematically mapping all proteins in human cells and their biological functions by means of mass spectrometry". [39]

In 2018, he received the Sir Hans Krebs Medal of the Federation of European Biochemical Societies (FEBS) and the Thomson Medal Award of the International Mass Spectrometry Society (IMSC). [40]

Related Research Articles

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<span class="mw-page-title-main">Tandem mass spectrometry</span> Type of mass spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is a technique in instrumental analysis where two or more stages of analysis using one or more mass analyzer are performed with an additional reaction step in between these analyses to increase their abilities to analyse chemical samples. A common use of tandem MS is the analysis of biomolecules, such as proteins and peptides.

<span class="mw-page-title-main">Electron-capture dissociation</span>

Electron-capture dissociation (ECD) is a method of fragmenting gas-phase ions for structure elucidation of peptides and proteins in tandem mass spectrometry. It is one of the most widely used techniques for activation and dissociation of mass selected precursor ion in MS/MS. It involves the direct introduction of low-energy electrons to trapped gas-phase ions.

<span class="mw-page-title-main">Citrullination</span> Biological process

Citrullination or deimination is the conversion of the amino acid arginine in a protein into the amino acid citrulline. Citrulline is not one of the 20 standard amino acids encoded by DNA in the genetic code. Instead, it is the result of a post-translational modification. Citrullination is distinct from the formation of the free amino acid citrulline as part of the urea cycle or as a byproduct of enzymes of the nitric oxide synthase family.

<span class="mw-page-title-main">Orbitrap</span>

In mass spectrometry, Orbitrap is an ion trap mass analyzer consisting of an outer barrel-like electrode and a coaxial inner spindle-like electrode that traps ions in an orbital motion around the spindle. The image current from the trapped ions is detected and converted to a mass spectrum using the Fourier transform of the frequency signal.

The Association of Biomolecular Resource Facilities (ABRF) is dedicated to advancing core and research biotechnology laboratories through research, communication, and education. ABRF members include over 2000 scientists representing 340 different core laboratories in 41 countries, including those in industry, government, academic and research institutions.

<span class="mw-page-title-main">Ruedi Aebersold</span> Swiss biologist (born 1954)

Rudolf Aebersold is a Swiss biologist, regarded as a pioneer in the fields of proteomics and systems biology. He has primarily researched techniques for measuring proteins in complex samples, in many cases via mass spectrometry. Ruedi Aebersold is a professor of Systems biology at the Institute of Molecular Systems Biology (IMSB) in ETH Zurich. He was one of the founders of the Institute for Systems Biology in Seattle, Washington, where he previously had a research group.

<span class="mw-page-title-main">Electron-transfer dissociation</span>

Electron-transfer dissociation (ETD) is a method of fragmenting multiply-charged gaseous macromolecules in a mass spectrometer between the stages of tandem mass spectrometry (MS/MS). Similar to electron-capture dissociation, ETD induces fragmentation of large, multiply-charged cations by transferring electrons to them. ETD is used extensively with polymers and biological molecules such as proteins and peptides for sequence analysis. Transferring an electron causes peptide backbone cleavage into c- and z-ions while leaving labile post translational modifications (PTM) intact. The technique only works well for higher charge state peptide or polymer ions (z>2). However, relative to collision-induced dissociation (CID), ETD is advantageous for the fragmentation of longer peptides or even entire proteins. This makes the technique important for top-down proteomics. The method was developed by Hunt and coworkers at the University of Virginia.

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<span class="mw-page-title-main">Top-down proteomics</span>

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<span class="mw-page-title-main">Laser spray ionization</span>

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References

  1. ↑ "Catalogus Professorum: Prof.dr. A.J.R. Heck". UU. Retrieved 29 November 2019.
  2. ↑ "Hoogleraren" (in Dutch). Volkskrant. 5 September 2012. Retrieved 21 May 2014.
  3. ↑ "Albert Heck appointed Distinguished Professor of the Faculty of Science". 1 November 2017. Retrieved 7 January 2020.
  4. ↑ "Awards – 2013 Recipients". HUPO. Retrieved 21 May 2014.
  5. ↑ Leney, Aneika C.; Heck, Albert J. R. (2017). "Native Mass Spectrometry: What is in the Name?". Journal of the American Society for Mass Spectrometry. 28 (1): 5–13. Bibcode:2017JASMS..28....5L. doi:10.1007/s13361-016-1545-3. PMC   5174146 . PMID   27909974.
  6. ↑ "Grote complexen intact de MS in" (in Dutch). Chemisch2Weekblad (C2W). 7 June 2013.
  7. ↑ Snijder, Joost; Van De Waterbeemd, Michiel; Damoc, Eugen; Denisov, Eduard; Grinfeld, Dmitry; Bennett, Antonette; Agbandje-Mckenna, Mavis; Makarov, Alexander; Heck, Albert J. R. (2014). "Defining the Stoichiometry and Cargo Load of Viral and Bacterial Nanoparticles by Orbitrap Mass Spectrometry". Journal of the American Chemical Society. 136 (20): 7295–7299. doi:10.1021/ja502616y. PMC   4046769 . PMID   24787140.
  8. ↑ Uetrecht, Charlotte; Heck, Albert J. R. (2011). "Modern Biomolecular Mass Spectrometry and its Role in Studying Virus Structure, Dynamics, and Assembly". Angewandte Chemie International Edition. 50 (36): 8248–8262. doi:10.1002/anie.201008120. PMC   7159578 . PMID   21793131.
  9. ↑ Van De Waterbeemd, Michiel; Tamara, Sem; Fort, Kyle L.; Damoc, Eugen; Franc, Vojtech; Bieri, Philipp; Itten, Martin; Makarov, Alexander; Ban, Nenad; Heck, Albert J. R. (2018). "Dissecting ribosomal particles throughout the kingdoms of life using advanced hybrid mass spectrometry methods". Nature Communications. 9 (1): 2493. Bibcode:2018NatCo...9.2493V. doi:10.1038/s41467-018-04853-x. PMC   6021402 . PMID   29950687.
  10. ↑ Rosati, Sara; Rose, Rebecca J.; Thompson, Natalie J.; Van Duijn, Esther; Damoc, Eugen; Denisov, Eduard; Makarov, Alexander; Heck, Albert J. R. (2012). "Exploring an Orbitrap Analyzer for the Characterization of Intact Antibodies by Native Mass Spectrometry". Angewandte Chemie International Edition. 51 (52): 12992–12996. doi: 10.1002/anie.201206745 . PMID   23172610.
  11. ↑ Wang, Guanbo; De Jong, Rob N.; Van Den Bremer, Ewald T.J.; Beurskens, Frank J.; Labrijn, Aran F.; Ugurlar, Deniz; Gros, Piet; Schuurman, Janine; Parren, Paul W.H.I.; Heck, Albert J.R. (2016). "Molecular Basis of Assembly and Activation of Complement Component C1 in Complex with Immunoglobulin G1 and Antigen". Molecular Cell. 63 (1): 135–145. doi: 10.1016/j.molcel.2016.05.016 . PMID   27320199.
  12. ↑ "Een moleculaire rattenkoning slaat groot immuunalarm" (in Dutch). NRC Handelsblad. 15 March 2014.
  13. ↑ Krijgsveld, Jeroen; Ketting, René F.; Mahmoudi, Tokameh; Johansen, Janik; Artal-Sanz, Marta; Verrijzer, C. Peter; Plasterk, Ronald H. A.; Heck, Albert J. R. (2003). "Metabolic labeling of C. Elegans and D. Melanogaster for quantitative proteomics". Nature Biotechnology. 21 (8): 927–931. doi:10.1038/nbt848. PMID   12858183. S2CID   2641430.
  14. ↑ Boersema, Paul J.; Raijmakers, Reinout; Lemeer, Simone; Mohammed, Shabaz; Heck, Albert J. R. (2009). "Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics". Nature Protocols. 4 (4): 484–494. doi:10.1038/nprot.2009.21. PMID   19300442. S2CID   5498505.
  15. ↑ Liu, Fan; Lössl, Philip; Rabbitts, Beverley M.; Balaban, Robert S.; Heck, Albert J. R. (2018). "The interactome of intact mitochondria by cross-linking mass spectrometry provides evidence for coexisting respiratory supercomplexes". Molecular & Cellular Proteomics. 17 (2): 216–232. doi: 10.1074/mcp.RA117.000470 . PMC   5795388 . PMID   29222160.
  16. ↑ "Moeilijk te vangen fosforgroepen" (in Dutch). Chemisch2Weekblad (C2W) Life Sciences. 23 June 2012.
  17. ↑ Yang, Yang; Franc, Vojtech; Heck, Albert J.R. (2017). "Glycoproteomics: A Balance between High-Throughput and In-Depth Analysis". Trends in Biotechnology. 35 (7): 598–609. doi:10.1016/j.tibtech.2017.04.010. hdl:1874/351003. PMID   28527536.
  18. ↑ Pinkse, Martijn W. H.; Uitto, Pauliina M.; Hilhorst, Martijn J.; Ooms, Bert; Heck, Albert J. R. (2004). "Selective Isolation at the Femtomole Level of Phosphopeptides from Proteolytic Digests Using 2D-NanoLC-ESI-MS/MS and Titanium Oxide Precolumns". Analytical Chemistry. 76 (14): 3935–3943. doi:10.1021/ac0498617. PMID   15253627.
  19. ↑ Schmidlin, Thierry; Debets, Donna O.; Van Gelder, Charlotte A.G.H.; Stecker, Kelly E.; Rontogianni, Stamatia; Van Den Eshof, Bart L.; Kemper, Kristel; Lips, Esther H.; Van Den Biggelaar, Maartje; Peeper, Daniel S.; Heck, Albert J.R.; Altelaar, Maarten (2019). "High-Throughput Assessment of Kinome-wide Activation States". Cell Systems. 9 (4): 366–374.e5. doi:10.1016/j.cels.2019.08.005. PMC   6838672 . PMID   31521607.
  20. ↑ Van Hoof, Dennis; Muñoz, Javier; Braam, Stefan R.; Pinkse, Martijn W.H.; Linding, Rune; Heck, Albert J.R.; Mummery, Christine L.; Krijgsveld, Jeroen (2009). "Phosphorylation Dynamics during Early Differentiation of Human Embryonic Stem Cells". Cell Stem Cell. 5 (2): 214–226. doi: 10.1016/j.stem.2009.05.021 . PMID   19664995.
  21. ↑ Giansanti, Piero; Tsiatsiani, Liana; Low, Teck Yew; Heck, Albert J. R. (2016). "Six alternative proteases for mass spectrometry–based proteomics beyond trypsin". Nature Protocols. 11 (5): 993–1006. doi:10.1038/nprot.2016.057. hdl:1874/333986. PMID   27123950. S2CID   2597839.
  22. ↑ Tsiatsiani, Liana; Heck, Albert J. R. (2015). "Proteomics beyond trypsin". FEBS Journal. 282 (14): 2612–2626. doi: 10.1111/febs.13287 . PMID   25823410. S2CID   24903856.
  23. ↑ Frese, Christian K.; Altelaar, A. F. Maarten; Van Den Toorn, Henk; Nolting, Dirk; Griep-Raming, Jens; Heck, Albert J. R.; Mohammed, Shabaz (2012). "Toward Full Peptide Sequence Coverage by Dual Fragmentation Combining Electron-Transfer and Higher-Energy Collision Dissociation Tandem Mass Spectrometry". Analytical Chemistry. 84 (22): 9668–9673. doi:10.1021/ac3025366. PMID   23106539.
  24. ↑ Reiding, Karli R.; Bondt, Albert; Franc, Vojtech; Heck, Albert J.R. (2018). "The benefits of hybrid fragmentation methods for glycoproteomics". Trends in Analytical Chemistry. 108: 260–268. doi:10.1016/j.trac.2018.09.007. hdl:1874/373361. S2CID   105377340.
  25. ↑ Mommen, G. P. M.; Frese, C. K.; Meiring, H. D.; Van Gaans-Van Den Brink, J.; De Jong, A. P. J. M.; Van Els, C. A. C. M.; Heck, A. J. R. (2014). "Expanding the detectable HLA peptide repertoire using electron-transfer/Higher-energy collision dissociation (EThcD)". Proceedings of the National Academy of Sciences. 111 (12): 4507–4512. Bibcode:2014PNAS..111.4507M. doi: 10.1073/pnas.1321458111 . PMC   3970485 . PMID   24616531.
  26. ↑ Liepe, Juliane; Marino, Fabio; Sidney, John; Jeko, Anita; Bunting, Daniel E.; Sette, Alessandro; Kloetzel, Peter M.; Stumpf, Michael P. H.; Heck, Albert J. R.; Mishto, Michele (2016). "A large fraction of HLA class I ligands are proteasome-generated spliced peptides". Science. 354 (6310): 354–358. Bibcode:2016Sci...354..354L. doi:10.1126/science.aaf4384. hdl: 10044/1/42330 . PMID   27846572. S2CID   41095551.
  27. ↑ Liu, Fan; Rijkers, Dirk T. S.; Post, Harm; Heck, Albert J. R. (2015). "Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry". Nature Methods. 12 (12): 1179–1184. doi:10.1038/nmeth.3603. hdl: 1874/329447 . PMID   26414014. S2CID   6786537.
  28. ↑ Liu, Fan; Lössl, Philip; Scheltema, Richard; Viner, Rosa; Heck, Albert J. R. (2017). "Optimized fragmentation schemes and data analysis strategies for proteome-wide cross-link identification". Nature Communications. 8: 15473. Bibcode:2017NatCo...815473L. doi: 10.1038/ncomms15473 . PMC   5454533 . PMID   28524877.
  29. ↑ "Proteins At Work". The Analytical Scientist. 23 February 2014.
  30. ↑ Raijmakers, Reinout; Olsen, Jesper V.; Aebersold, Ruedi; Heck, Albert J. R. (2014). "PRIME-XS, a European infrastructure for proteomics". Molecular & Cellular Proteomics. 13 (8): 1901–1904. doi: 10.1074/mcp.E114.040162 . PMC   4125724 . PMID   24958170.
  31. ↑ "Proteomics Experts Unite for EPIC-XS". Technology Networks. 22 March 2019. Retrieved 29 November 2019.
  32. ↑ "Overzicht KNCV Gouden Medaille Winnaars" (in Dutch). KNCV . Retrieved 29 November 2019.
  33. ↑ "Descartes-Huygens Prize". KNAW. Archived from the original on 22 March 2019. Retrieved 29 November 2019.
  34. ↑ "Most important international proteomics award for Albert Heck". Netherlands Genomics Initiative. 2 October 2013. Retrieved 21 May 2014.
  35. ↑ "EMBO announces new members for 2013". EMBO. 21 May 2014. Retrieved 21 May 2014.
  36. ↑ "Albert Heck en Ineke Braakman verkozen tot EMBO leden" (in Dutch). Utrecht University. 19 May 2014. Retrieved 21 May 2014.
  37. ↑ "KNAW kiest zeventien nieuwe leden" (in Dutch). KNAW. 21 May 2014. Retrieved 21 May 2014.
  38. ↑ "Prestigious American Chemical Society awards for Albert Heck and Geert-Jan Boons". UU. 28 August 2015. Retrieved 28 November 2019.
  39. ↑ "NWO Spinoza Prizes awarded to Eveline Crone, Albert Heck, Michel Orrit and Alexander van Oudenaarde". NWO. 6 June 2017. Retrieved 28 November 2019.
  40. ↑ "Professor Albert Heck is to receive two international distinctions". UU. 3 July 2018. Retrieved 28 November 2019.
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