94 percent of recent graduates from UE's Department of Biology are either in graduate or professional schools or employed in STEM- (Science, Technology, Engineering, and Math) related fields!

Michael Cullen

Faculty Photo

Contact Information


  • Cell Biology
  • Neurobiology


  • A.B. - Western Reserve University
  • Ph.D. - Case Western Reserve University
  • Postdoctoral - National Institutes of Health

Research Interests

My research focuses on the associations that initiate, direct, and maintain the unique and highly specialized cells in the nervous system. Early work studied the role synaptic input plays in the formation and maintenance of specialized neurons and local regions on the neuronal surface. Later work focused on the role neurons play in the formation and maintenance of the specialized cells that differentiate large amounts of a specialized membrane, the myelin sheath. From that work has developed a series of studies on the cell-cell and cell-matrix interactions that influence the determination of the myelin-forming Schwann cells from neural crest cells, a population of cells with many potential cell fates. Finally, work with Drs. Zoltan Tökés, Giselle Lim, and Jon Backstrom has described a class of enzymes, metalloproteinases, that are inactive in neurodegenerative diseases and may play a role in the pathogenesis of conditions such as Alzheimer's disease and amyotrophic lateral sclerosis.

Selected Publications

Lim, G.P., M.J. Russell, M.J. Cullen and Z.A. Tökés. 1997. Matrix metalloproteinases in dog brains exhibiting Alzheimer-like characteristics. Journal of Neurochemistry. 68:1606-1611.

Lim, G.P., J.R. Backstrom, M.J. Cullen, C.A. Miller, R.D. Atkinson, and Z.A. Tökés. 1996. Matrix metalloproteinases in the neocortex and spinal cord of amyotrophic lateral sclerosis (ALS) patients. Journal of Neurochemistry 67:251-259.

Backstrom, J.R., G.P. Lim, M.J. Cullen and Z.A. Tökés. 1996. Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-ß peptide (1-40). Journal of Neuroscience. 16:7910-7919.