Faculty & Staff Directory

John Capodilupo

Email
capodilj@gvsu.edu

Title
Professor

Office
232 Henry Hall

Phone
616-331-3019

Fax
616-331-2090

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 250 - Anatomy and Physiology I Laboratory
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 Alzheimers 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 Alzheimers 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.

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