Head of the Department
Position Head Department; Principal Investigator
Research fields Regulation of Function of Heat Shock Proteins
  • Research Profile
  • Selected Publications
  • Harm Kampinga graduated in Biology at the University of Groningen in 1984 and received my PhD in 1989 in Groningen. After being assistant – and associated professor in Radiation Oncology, he became full professor in the Department of Cell Biology in 2001 and became head of this Department in 2015.

    The central theme of his research has always been related to the consequences of protein un- or misfolding on cellular functions. Initially, his work was centered around the biological effects of heat shock on cells in relation to the use of hyperthermia in combination with radiation or/and chemotherapy in cancer treatments. During these studies, Kampinga became interested in Heat Shock Proteins (HSP) that could protect cells from the cell biological effects of heat shock and focused my research on the functional regulation and diversity HSPs.

    Kampinga’ s lab was the first to clone a majority of all human and Drosophila HSPs and subsequently screened them for activity in several (age-related) cell and drosophila models for neurodegenerative diseases (in particular CAG repeat expansion diseases) and cardiac diseases. Major discoveries from his lab include the asymmetric segregation of protein damage in stem cells, the functional diversity of HSPs and their role in dealing with different disease-associated protein aggregation diseases, and the discovery of set of specific DNAJ family protein members (DNAJB6 and DNAJB8) with an exquisitely high potency to delay amyloidogenesis.

      • Selected Publications:
      1. Rujano MA, Bosveld A, Salomons FA, Dijk F, van Waarde MAWH, van der Want JJL, de Vos RAI, Brunt ER, Sibon OCM, Kampinga HH. 2006. Polarized asymmetric inheritance of accumulated protein damage in higher eukaryotes. PloS Biology 4, 2325-2335. (pdf)
      2. Hageman J, Rujano MA, van Waarde MAWH, Kakkar V, Dirks D, Govorukhina N, Oosterveld-Hut HJM, Lubsen NH, Kampinga HH. 2010. A DNAJB Chaperone Subfamily with HDAC-dependent Activities Suppresses Toxic Protein Aggregation. Molecular Cell 37, 355-369. (pdf)
      3. Kampinga HH, Craig EA. 2010 The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nature Reviews Mol. Cell. Biol. 11, 579-592. (pdf)
      4. Vos MJ, Zijlstra MP, Kanon B, van Waarde-Verhagen MAWH, Brunt ERP, Oosterveld-Hut HMJ, Carra S, Sibon OCM, Kampinga HH. 2010. HSPB7 is the most potent polyQ aggregation suppressor within the HSPB family of molecular chaperones. Human Molecular Genetics 19, 4677-4693. (pdf)
      5. Carra S, Boncoraglio A, Bart Kanon, Brunsting JF, Minoia M, Rana A, Vos MJ, Seidel K, Sibon OCM, Kampinga HH. 2010. Identification of the Drosophila ortholog of HSPB8: implication of HSPB8 loss of function in protein folding diseases. J Biol Chem. 285, 37811-37822. (pdf)
      6. Minoia M, Boncoraglio A, Vinet J, Morelli F, Brunsting JF, Poletti A, Krom S, Reits E, Kampinga HH, Carra S‡. 2014. BAG3 induces the sequestration of proteasomal clients into cytoplasmic puncta: implication for a proteasome-to-autophagy switch. Autophagy, 10, 1603-1621 (‡ = shared last authors). (pdf)
      7. Mansson C, Arosio P, Hussein R, Kampinga HH, Hashem RM, Boelens WC, Dobson CM, Knowles TPJ, Linse S, Emanuelsson C. 2014. Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation. Biol. Chem. 289, 31066-31076. (pdf)
      8. Vos MJ, Carra S, Kanon B, Bosveld F, Klauke K, Sibon OCM* and Kampinga HH* 2016. Specific protein homeostatic functions of small heat shock proteins increase lifespan. Ageing Cell 15, 217-226. (*shared last authors). (pdf)
      9. Kakkar V, Månsson C, de Mattos EP, Bergink S, van der Zwaag M, van Waarde MAWH, Kloosterhuis NJ, Melki R, van Cruchten R, Al-Karadaghi S, Arosio P, Dobson CM, Knowles TPJ, Bates GP, van Deursen J, Linse S, van de Sluis AJ, Emanuelsson C*, and Kampinga HH*. 2016. The S/T-rich motif in the DNAJB6 chaperone delays polyglutamine aggregation and the onset of disease in a mouse model. Molecular Cell 62, 1-12. (*shared last authors). (pdf)
      10. Kampinga HH, Bergink S. 2016. Heat shock proteins as potential targets for protective strategies in neurodegeneration. Lancet Neurology, doi: 10.1016/S1474-4422(16)00099-5. (pdf)
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