A healthy proteome in cells is not only crucial for functionality of cells, but also essential for preventing damage (protein aggregates) that lead to a cascade of toxic events that threaten cellular health span. To ensure a proper protein homeostasis, an intricate protein quality control (PQC) network exists in cells in which Heat Shock Proteins (HSP), the central research topic in my group, play a central role.
Head Department; Principal Investigator
Regulation of Function of Heat Shock Proteins
|2007||Rujano Maldonado,M.A. (Maria)|
|2006||Vries,H.I. de (Hilda)|
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.
See dissertations supervised by Harm H. Kampinga (promotor or assessor)
Turcan, I. (2018). Cold cases in epidermolysis bullosa: not the usual suspects[Groningen]: Rijksuniversiteit Groningen. (assessment cee)
Meister, M. (2017). On protein quality control, myofibrillar myopathies, and neurodegeneration [Groningen]: University of Groningen
van Zomeren, K. C. (2017). α-Synuclein pathology and mitochondrial dysfunction: Studies in cell models for Parkinson’s disease [Groningen]: Rijksuniversiteit Groningen. (assessment cee)
Wang, C. (2016). Biomimetic drug nanocarriers to overcome biological barriers: Inspiration from pathogen invasion [Groningen]: University of Groningen
Wiersma, M. (2016). Implications of the cardiomyocyte stress response on protein homeostasis in atrial fibrillation [Groningen]: Rijksuniversiteit Groningen. (assessment cee)
Liu, W. (2016). Orphan nuclear receptor TR4 and fibroblast growth factor 1 in metabolism [Groningen]: University of Groningen. (assessment cee)
Holmberg, M. (2015). Genetic factors and analysis of protein misfolding in vivo[Groningen]: University of Groningen. (assessment cee)
Munoz Llancao, P. A. (2015). Role of EPAC in axon determination [Groningen]: University of Groningen. (assessment cee)
Popken, P. (2015). Selectivity of the yeast nuclear pore complex – probing transport in vivo [Groningen]: University of Groningen. (assessment cee)
Bispo de Jesus, M. (2015). Solid lipid nanoparticles for cancer therapy: an in vitro study in prostate cancer cells [Groningen]: University of Groningen. (assessment cee)
Minoia, M. (2014). Chaperones, protein homeostasis & protein aggregation diseases[S.l.]: s.n.
Kakkar, V. (2014). DNAJ proteins: more than just “co-chaperones”: Implicaties voor eiwit-aggregatie ziektes [S.l.]: [S.n.]
Regeling, A. (2014). Gene-environment interactions in Inflammatory Bowel Disease: Emphasis on smoking and autophagy ([S.l.] ed.) [S.n.] (assessment cee)
Meijering, R. (2014). Loss of proteostasis as a substrate for atrial fibrillation: Defining novel targets for therapy [S.l.]: s.n. (assessment cee)
Wiegman, E. M. (2014). Prediction and prevention of radiation induced lung toxicityGroningen: s.n.
Jezierska, J. (2013). Genetic and molecular mechanisms underlying spinocerebellar ataxias Groningen: s.n.
Yang, J. (2012). Autophagy, FOXO1 and proteostasis: implications for human diseases Groningen: s.n.
Ke, L. (2012). Molecular remodeling in atrial fibrillation: protective roles of small HSPs Groningen: s.n.
Seidel, K. (2011). Neurogenerative diseases and the Protein quality control system[S.n.]
Zijlstra, M. P. (2011). The role of heat shock proteins in polyQ disorders Groningen: s.n.
Vos, M. (2009). Small heat shock proteins: Implications for neurodegeneration & longevity s.n.
Bosveld, F. (2008). Physiological implications of impaired de novo Coenzyme A Biosynthesis in Drosophila melanogaster s.n.
Lombaert, I. M. A. (2008). Regeneration of irradiated salivary glands by stem cell therapy Groningen: s.n.
Hageman, J. (2008). The human HSP70/HSP40 chaperone family: a study on its capacity to combat proteotoxic stress Groningen: s.n.
Rujano Maldonado, M. A. (2007). Protein quality control pathways in polyglutamine diseasesGroningen: [S.n.]
Yi, X. (2007). The impact of impaired DNA damage responses on cells, tissues and organismsGroningen: s.n.
Vries, H. I. D. (2006). Grapes- and stonewall-related DNA damage responses in Drosophila melanogaster [S.n.]
Wachters, F. M. (2006). Therapeutic strategies in advanced non-small-cell lung cancer [S.n.]
Hut, H. M. J. (2005). Centrosomes and cellular stress responses s.n.
Stege, G. J. J. (1995). Hyperthermia and protein aggregation: role of heat shock proteins Groningen: s.n.
Disturbed protein homeostasis is a key event during cellular aging. Genetic mutations in proteins that increase the risk of protein aggregation or that impede on the protein quality control (PQC) mechanism that maintains normal protein homeostasis lead to accelerated aging or early onset of age-associated diseases.
HSP assist in protein folding as well as protein degradation (proteasomal and autophagosomal). The central aim of my group is understand how the 100 different human HSPs are regulated to recognise their targets and steer them towards folding or degradation and how this knowledge can be exploited to combat diseases in which this protein homeostasis is disturbed.
The main focus of my research is: what regulates the input and output of protein substrates into the so-called HSP70 machines, the central hub in the cellular PQC system?
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