John Capodilupo

Associate Professor
Biomedical Science Department
234 Padnos Hall
Allendale, Michigan 49401
Phone:  616-331-3019
Fax:  616-331-2090
email:  capodilj@gvsu.edu

OFFICE HOURS:
See available times here, or by appointment
 
COURSES TAUGHT
BMS 202 - Human Anatomy and Physiology
BMS 202L - Laboratory in Human Anatomy and Physiology
BMS 208 - Human Anatomy
BMS 290 - Human Physiology
BMS 291 - Laboratory in Human Physiology
BMS 309 - Human Anatomy Cadaver Laboratory
BMS 310 - Basic Pathophysiology
BMS 365 - Exercise Physiology
BMS 375 - Biology of Human Aging
BMS 427 - Neuroanatomy
BMS 428 - Neuroscience
BMS 495 - Capstone

EDUCATION/TRAINING
Ph.D. (1994) Wayne State University School of Medicine
M.S.  (1991) Wayne State University School of Medicine
B.S.   (1987) Mercy College of Detroit

RESEARCH INTERESTS
We are examining a molecule called GAP-43 which is a brain protein that is expressed in a wide variety of species including humans and has been shown to become biochemically altered in the process of learning and memory.  Specifically, levels of phosphorylated forms of GAP-43 have been shown to increase following a controversial paradigm of learning and memory in several animals including rat, mouse and rabbit.  We are interested to see if any differences in the profile of GAP-43 are associated with dementing illnesses that severely disrupt memory and learning.  Since human brain tissue is difficult to obtain, we utilize brain tissue from a genetically altered mouse engineered to resemble Alzheimer’s disease, a human neurodegenerative disorder characterized by profound cognitive impairment.  Therefore, to test the hypothesis that the profile of  phosphorylated isoforms of GAP-43 are changed in the brains of a mouse used to model Alzheimer’s disease, GAP-43 will be examined by 1 and 2 dimensional SDS polyacrylamide gel electrophoresis.  Isoforms of mouse brain GAP-43 will be detected by immunocytochemistry and silver staining and, further, quantified by computerized densitometry.  Alterations in quantities of phosphorylated forms of GAP-43 might result from a pathological biochemical processes.  Revealing molecular defects generates potential targets for the development of possibly more effective drugs to combat dementia.

SELECTED PUBLICATIONS
Walker, P.D., Capodilupo, J.G., Wolf, W.A and Carlock, L.R. Preprotachykinin and preproenkephalin mRNA expression within striatal sub-regions in response to altered serotonin transmission. Brain Research, 732 (1996) 25-35.

Roher, A.E., Capodilupo, J.G., Wakade, A.R. and Ball, M.J. New biochemical insights to unravel the pathogenesis of Alzheimer’s lesions. Can. J. Neurol. Sci., 18 (1991) 408-410.

Page last modified September 10, 2009