Troy Rohn

Professor, Department of Biological Sciences
Year arrived at BSU: 2000
Mailing Address:

Department of Biology
Boise State University
Boise, ID 83725-1515

Office Location: Science Building, Room 228
Office Number: 208-426-2396
Lab Location:Science Building, Room 216


Troy Rohn graduated in 1990 from the University of California at Davis with a B.S. in Physiology. He received his Ph.D. in Pharmacology from the University of Washington , Seattle in 1994. His interests include the role of apoptosis in neurodegenerative diseases. Dr. Rohn had several Postdoctoral stints including two plus years living in Paris , France , one year at Montana State University in Bozeman , Montana , and two years at UC Irvine at the Institute of Brain Aging and Dementia under the direction of Dr. Carl Cotman. Dr. Rohn continues to collaborate extensively with UC Irvine and in addition with Dr. Eliezer Masliah at UC San Diego. He has obtained extramural funding continuously since his arrival at BSU including grants from NIH, AFAR and AHAF.


BIOL442/542: This is a molecular neurobiology course for undergraduate and graduate-students. Topics covered are all aspects of neuronal function at the molecular level. A discussion of several neurodegenerative diseases including Parkinson’s, Alzheimer’s, and Schizophrenia are a few of diseases covered.

BIOL 431/531: This is a general pharmacology course for undergraduate and graduate-students. Topics include the pharmacokinetics and pharmacodynamics. All major drug classes are covered in this course.

  • Both courses are taught in the fall semesters

BIOL 100: This is a non-majors course covering all aspects of biology. A two-hour weekly lab reinforces concepts taught in lecture. I also teach the electronic course for this class during spring semesters.

BIOL 301: A cell biology course that represents a core requirement for all biology majors.  This course will be team taught with Dr. Cheryl Jorcyk starting in the spring semester of 2012.


The primary focus of my laboratory is involved in the research involving neurodegenerative diseases including to a large extent, Alzheimer’s disease (AD). During the progression of Alzheimer’s disease, many neurons die particularly in the area of the hippocampus. Because the hippocampus is an area of the brain involved in memory, AD is primary a disease where afflicted individuals lose their capacity for memory.

Currently, we are investigating whether caspase-cleavage of APOE4 underlies its pathogenesis in AD. The APOE4 allele, if inherited greatly increases the risk of AD, but how it contributes to disease progression is not known. We believe this protein may be susceptible to proteolytic cleavage by proteases and this inactivates the ability of this protein to function properly in the brain. This could contribute to disease progression by allowing for the accumulation of the toxic protein, beta-amyloid, that is normally removed from the brain, in part by functional APOE4. My lab has recently been awarded an NIH grant to investigate this hypothesis.

Our lab also has an interest in other neurodegenerative diseases including Parkinson’s, Pick’s, frontal temporal dementia and vascular dementia.

RECENT PUBLICATIONS (selected from 46 total)

Rohn, T.T., Catlin, L.W. and Poon, W.W. (2013). Caspase-cleaved glial fibrillary acidic protein within cerebellar white matter of the Alzheimer’s disease brain. Int J Clin Exp Pathol. 6(1): 41-8. Epub 2012 Nov 20

Rohn, T.T. (2013). The Triggering Receptor Expressed on Myeloid Cells 2: “TREM-ming” the Inflammatory Component Associated with Alzheimer’s Disease. Oxidative Medicine and Cellular Longevity. Invited Review,

Rohn, T.T. (2013). Proteolytic cleavage of apolipoprotein E4 as the keystone for the heightened risk associated with Alzheimer’s disease. Int. J. Mol. Sci. 14(7): 14908-14922.

Rohn, T.T. (2012). Targeting alpha-synuclein for the treatment of Parkinson’s disease. CNS & Neurological Disorders-Drug Targets. Invited Review, 11(2):174-9.

Rohn, T.T., Catlin, L.W., Coonse, K.G. and Habig, J.W. (2012). Identification of an amino-terminal fragment of apolipoprotein E4 that localizes to neurofibrillary tangles of the Alzheimer’s disease brain. Brain Res. 1475:106-15

1. Rohn, T.T. and Catlin, L.W. (2011). Immunolocalization of Influenza A Virus and Markers of Inflammation in the Human Parkinson’s Disease Brain.  PLoS ONE,  31 May 2011 10.1371/journal.pone.0020495.

2. Masliah, E., Rockenstein, E., Mante, M., Crews, L., Spencer, B., Adame, A., Patrick, C., Trejo, M., Ubhi, K., Rohn, T.T., Mueller-Steiner, S., Seubert, P., Barbour, R., McConlogue, L., Buttini, M., Games, D. and Schenk, D. (2011). Passive immunization reduces behavioral and neuropathological deficits in an alpha-synuclein transgenic model of Lewy body disease. PLoS ONE, 10.1371/journal.pone.0019338.

3. Rohn, T.T., Wirawan, E., Brown, R.J., Harris, J.R., Masliah, E. and Vandenabeele, P.  (2011) Depletion of Beclin-1 due to proteolytic cleavage by caspases in the Alzheimer’s disease brain. Neurobiology of Disease 43: 68-78.

4. Kokoulina, P. and Rohn, T.T. (2010).  Caspase-cleaved TAR DNA-binding protein-43 in Parkinson’s disease and dementia with Lewy bodies. Neurodegenerative Diseases, 7(4): 243-250.

5. Rohn, T.T. (2010).  The Role of Caspases in Alzheimer’s Disease;  Potential Novel Therapeutic Opportunities.  Invited Review, Apoptosis Journal, 2010 Feb 3. [Epub ahead of print].

6. Rohn, T.T., Kokoulina, P., Eaton, C.R. and Poon, W.W. (2009).  Caspase Activation in Transgenic Mice with Alzheimer-like Pathology:  Results From a Pilot Study Utilizing The Caspase Inhibitor, Q-VD-OPh. Int J Clin Exp Med. 2009; 2(4): 300–308. Published online 2009 November 5.

7. Rohn, T.T. (2009).  Cytoplasmic Inclusions of TDP-43 in Neurodegenerative Diseases:  A Potential Role for Caspases.  Histology and Histopathology (Invited Review, 24(8):1081-1086).

8. Rohn, T.T. and Kokoulina, P. (2009). Caspase-cleaved TAR DNA-binding protein-43 in Pick’s disease. Int, J. Physio. Pathophysio. Pharmacol. 1(1):25-32.

9. Rohn, T.T., Hernandez-Estrada, T. and Head, E. (2009) Caspases as therapeutic targets in Alzheimer’s disease:  Is it time to “cut” to the chase? Int. J. Clin. Exp. Pathol. (Invited Review, 2, 108-118).

10. Rohn, T.T., Vyas, V., Hernandez-Estrada, T., Nichol, K.E., Christie, L-A and Head, E.  (2008).  Lack of pathology in a triple transgenic mouse model of Alzheimer’s disease after overexpression of the anti-apoptotic protein, Bcl-2. J. Neurosci, 28(12): 3051-59

11. Corsetti V., Amadoro G., Gentile A., Capsoni S., Ciotti M.T., Cencioni M.T., Atlante A., Canu N., Rohn T.T., Cattaneo A, Calissano P. (2008).  Identification of a caspase-derived N-terminal tau fragment in cellular and animal Alzheimer disease models.  Mol. Cell. Neurosci. 38(3):381-92. PMID: 18511295

12. Rohn, T.T. (2008). Caspase-cleaved TAR DNA-binding protein-43 is a major pathological finding in Alzheimer’s disease.  Brain Research, 1228(4): 189-198.