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IMAGING

Imaging

One research line within the Microscopic Imaging Centre (MIC) is the molecular organization of protein complexes involved in intracellular energy metabolism. Individual reactions contributing to the generation and utilization of energy are spatially highly organized on a subcellular and molecular level. Both, the organization of proteins inside the mitochondrion as well as the targeting of enzymes that generate energy in the cell periphery for processes such as motion and phagocytosis are areas of intense research within the MIC. Within the NCMD we study more specifically the relationship between cellular energy metabolism and cell surface and mitochondrial morphology and physiological function in life cells. “Energy stress” (induced via metabolic conditions or defects in the oxidative phosphorylation system) is reflected in adaptive changes of cells, often resulting in dynamic remodeling of the actin-myosin cytoskeletal network and in semi-permanent changes in mitochondrial morphology. We use advanced imaging microscopy to study the question whether high resolution still pictures of cell surface structure and mitochondria will reflect these changes. In addition we will address the question if new technology, both at the light and electron (wet-SEM) microscopical level, can be used to obtain ultrastructural data on mitochondria in living cells, and whether this information can be used as a highly sensitive indicator of altered energy status.

Contact
Jack A.M. Fransen, PhD,
NCMLS, Radboud University Nijmegen Medical Centre
283 Department of Cell Biology an Microscopisc Imaging Centre
P.O. Box 9101
6500 HB Nijmegen
The Netherlands
Phone: +31.24.3614284
Fax: +31.24.3615317
E-mail: J.Fransen@ncmls.ru.nl
Website: http://www.ncmls.nl/celbio/

Members
Helma Pluk
Huib Croes
Mietske Wijers

Key publications

Kuiper, J.W., R. van Horssen, F. Oerlemans, W. Peters, M.M. van Dommelen, M.M. Te Lindert, T.L. Ten Hagen, E. Janssen, J.A. Fransen, and B. Wieringa. 2009. Local ATP Generation by Brain-Type Creatine Kinase (CK-B) Facilitates Cell Motility. PLoS ONE. 4:e5030.
 
Pluk, H., D.J. Stokes, B. Lich, B. Wieringa, and J. Fransen. 2009. Advantages of indium-tin oxide-coated glass slides in correlative scanning electron microscopy applications of uncoated cultured cells. J Microsc. 233:353-363.
 
van Horssen, R., E. Janssen, W. Peters, L. van de Pasch, M.M. Lindert, M.M. van Dommelen, P.C. Linssen, T.L. Hagen, J.A. Fransen, and B. Wieringa. 2009. Modulation of Cell Motility by Spatial Repositioning of Enzymatic ATP/ADP Exchange Capacity. J Biol Chem. 284:1620-1627.
 
Kuiper, J.W., F.T. Oerlemans, J.A. Fransen, and B. Wieringa. 2008. Creatine kinase B deficient neurons exhibit an increased fraction of motile mitochondria. BMC Neurosci. 9:73.
 
Kuiper, J.W., H. Pluk, F. Oerlemans, F.N. van Leeuwen, F. de Lange, J. Fransen, and B. Wieringa. 2008. Creatine kinase-mediated ATP supply fuels actin-based events in phagocytosis. PLoS Biol. 6:e51.
 
Willemse, M., E. Janssen, F. de Lange, B. Wieringa, and J. Fransen. 2007. ATP and FRET - a cautionary note. Nat. Biotechnol. 25:170-172.
 
van Herpen, R.E.M.A., R.J.A. Oude Ophuis, M. Wijers, M.B. Bennink, F.A.J. van de Loo, J. Fransen, B. Wieringa, and D.G. Wansink. 2005. Divergent Mitochondrial and Endoplasmic Reticulum Association of DMPK Splice Isoforms Depends on Unique Sequence Arrangements in Tail Anchors. Mol. Cell. Biol. 25:1402-1414.

 

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