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Johannes Nimpf
ao.Univ. Prof Johannes Nimpf

Center for Medical Biochemistry (Division of Molecular Genetics)
Position: Associate Professor

T +43 1 4277 61808

Further Information


Chickens; Developmental Biology; Granulosa Cells; LDL-Receptor Related Proteins; Neurons; Neurosciences; Oocytes; Ovarian Follicle; Vitellogenins

Research interests

We study the biology of LDL receptor related proteins (VLDL receptor and ApoER2), a group of cell surface receptors which mediate transport of macromolecules across cell membranes and play important roles in signal transduction. The biological systems we are working with are the chicken oocyte and the mammalian brain. These two systems reflect the functional dichotomy of the receptors which function in endocytosis (follicles) and signal transduction (brain development). The best characterized function of VLDLR in follicles of egg laying species is endocytosis of yolk precursors into the growing oocyte. These yolk precursors (VLDL and Vitellogenin) are synthesized in the liver and rapidly taken up by the growing oocyte. Recently we have started to elucidate cell signalling functions of VLDLR and ApoER2 in granulosa cells which support the maturation of oocytes within the follicle. In respect to brain development both receptors act as Reelin-signal transducers. The Reelin signal orchestrates the correct positioning of newly generated neurons within laminated structures of the brain.

Selected publications

  1. Cuchillo-Ibanez, I. et al., 2016. The β-amyloid peptide compromises Reelin signaling in Alzheimer�s disease. Scientific Reports, 6(1). Available at:
  2. Eresheim, C. et al., 2014. Signaling by the Extracellular Matrix Protein Reelin Promotes Granulosa Cell Proliferation in the Chicken Follicle. Journal of Biological Chemistry, 289(14), pp.10182-10191. Available at:
  3. Leeb, C., Eresheim, C. & Nimpf, J., 2013. Clusterin Is a Ligand for Apolipoprotein E Receptor 2 (ApoER2) and Very Low Density Lipoprotein Receptor (VLDLR) and Signals via the Reelin-signaling Pathway. Journal of Biological Chemistry, 289(7), pp.4161-4172. Available at:
  4. Balmaceda, V. et al., 2013. ApoER2 processing by presenilin-1 modulates reelin expression. The FASEB Journal, 28(4), pp.1543-1554. Available at:
  5. Duit, S. et al., 2009. Differential Functions of ApoER2 and Very Low Density Lipoprotein Receptor in Reelin Signaling Depend on Differential Sorting of the Receptors. Journal of Biological Chemistry, 285(7), pp.4896-4908. Available at: