dr. J.W.M. (Jo ) HoppenerAssociate Professor
- Group Burgering, section Molecular Cancer Research
Jo Höppener graduated (cum laude) in 1981 in Biology at Utrecht University. He did his Ph.D. (cum laude) in 1988 with Prof. Lips and Prof. Jansz (financed by NWO and Ciba Geigy). Part of the Ph.D. study was performed at the Johns Hopkins Hospital (Baltimore, USA). He was research fellow at Utrecht University until 1989 (financed by STW), when he was awarded a 5-year fellowship from the Royal Netherlands Academy of Arts and Sciences (KNAW). He was appointed senior research scientist in the Faculty of Medicine (presently UMC Utrecht) at the Division of Internal Medicine in 1994. He was appointed Associate Professor at the Division of Biomedical Genetics at UMC Utrecht in 2005 and his research was incorporated in the Laboratory of Translational Immunology in 2013. The major research theme of his group is the role of IAPP and islet amyloid in islet ß-cell dysfunction in Type 2 diabetes mellitus (DM2). To this end they have generated a transgenic mouse model, in which the amyloidogenic human IAPP is expressed in the islet ß-cells. This unique animal model is used for pioneering research on the pathogenesis, diagnosis and therapy of DM2.
Fellowship and Awards
Jo Höppener has been co-promotor of 5 Ph.D. students and is author on more than 100 peer-reviewed papers in international journals. His research has been supported by KNAW (personal 5-year fellowship), Dutch Cancer Society (NKB/KWF), Dutch Diabetes Research Fund, European Union and industry.
Research Output (71)
Lips C.J.M., Höppener J.W.M. 2012, In: Nature Reviews. Endocrinology. 8 , p. 575-576 2 p.
Variable clinical expression in patients with a germline MEN1 disease gene mutation: clues to a genotype-phenotype correlation.
Lips C.J.M., Dreijerink K.M.A., Hoppener J.W.M. 2012, In: Clinics (São Paulo, Brazil). 67 , p. 49-56 8 p.
The role of the disulfide bond in the interaction of islet amyloid polypeptide with membranes
Khemtemourian L.P., Engel M.F.M., Kruijtzer J.A.W., Hoppener J.W.M., Liskamp R.M.J., Killian J.A. 2010, In: European Biophysics Journal. 39 , p. 1359-1364 6 p.
The N-terminal fragment of human islet amyloid polypeptide is non-fibrillogenic in the presence of membranes and does not cause leakage of bilayers of physiologically relevant lipid composition
Khemtemourian L.P., Engel M.F.M., Liskamp R.M.J., Höppener J.W.M., Killian J.A. 2010, In: Biochimica et Biophysica Acta-Biomembranes. 1798 , p. 1805-1811 7 p.
A combinatorial approach for the design of complementarity-determining region-derived peptidomimetics with in vitro anti-tumoral activity
Timmerman P., Barderas R., Desmet J., Altschuh D., Shochat S., Hollestelle M.J., Hoppener J.W.M., Monasterio A., Casal J.I., Meloen R.H. 2009, In: Journal of Biological Chemistry. 284 , p. 34126-34134 9 p.
The multiple endocrine neoplasia type 1 (MEN1) tumor suppressor regulates peroxisome proliferator-activated receptor gamma-dependent adipocyte differentiation.
Dreijerink K.M.A., Varier R.A., van Beekum O., Jeninga E.H., Hoppener J.W.M., Lips C.J.M., Kummer J.A., Kalkhoven E., Timmers H.T.M. 2009, In: Molecular and Cellular Biology. 29 , p. 5060-5069 10 p.
van Veelen W., de Groot J.W.B., Acton D.S., Hofstra R.M., Hoppener J.W.M., Links T.P., Lips C.J.M. 2009, In: Journal of Internal Medicine. 266 , p. 126-140 15 p.
P18 is a tumor suppressor gene involved in human medullary thyroid carcinoma and pheochromocytoma development.
van Veelen W., Klompmaker R., Gloerich M., van Gasteren C.J.R., Kalkhoven E., Berger R., Lips C.J.M., Medema R.H., Höppener J.W.M., Acton D.S. 2009, In: International Journal of Cancer. 124 , p. 339-345 6 p.
Gracanin A., Dreijerink K.M.A., van der Luijt R.B., Lips C.J.M., Hoppener J.W.M. 2009, In: Cancer Research. 69 , p. 6371-6374 4 p.
Impaired processing of human pro-islet amyloid polypeptide is not a causative factor for fibril formation or membrane damage in vitro
Khemtémourian L.P., Lahoz Casarramona G., Suylen D.P., Hackeng T.M., Meeldijk J.D., de Kruijff B., Hoppener J.W.M., Killian J.A. 2009, In: Biochemistry. 48 , p. 10918-10925 8 p.