Mentor: Lucia Notterpeck
College of Medicine
"I applied to the Scholars program because I wanted the ability to plan my own research project and see it to completion. During my project, I hope to learn common lab techniques that I can carry through my scientific education. Also, I hope to elucidate some of the unknown in regards to PMP22's effect on cell structure."
- Preprofessional Service Organization
- UF Intramural basketball
- Shands Radiology Center
- Westwood Middle mentoring
- Bethesda Memorial Hospital escort
- Mission trip to Huancayo, Peru
Hobbies and Interests
- Pursuing a career in medicine
Investigating the Potential Involvement of PMP22 in modulating the Actin Network
Myelin is an ensheathing membrane around axons. In the peripheral nervous system, Schwann cells (SC) are responsible for the creation and wrapping of myelin. Peripheral Myelin Protein 22 (PMP22) is a tetraspan glycoprotein mostly found in SCs. Diseases linked to PMP22 lead to various neuropathies including Charcot-Marie-Tooth Disease type 1A (CMT1A) and Hereditary Neuropathies with Liability to Pressure Palsies (HNPP). To date, it is unclear how the miss-expression of PMP22 leads to the neuropathic phenotype of these diseases. It is hypothesized that the main function of PMP22 is to participate in the formation of compact myelin by interacting with membrane adhesion proteins (Amici et al, 2007). However, additional functions of PMP22 are likely, as PMP22 is also present in other cell types including fibroblasts, endothelia and polarized epithelia. Transgenic mice with genetic deletion of PMP22 (PMP22-KO) are available and useful to study the role PMP22. These mice have severe dysmyelination and demyelination due to the lack of PMP22. Mechanistically, previous work in PMP22-KO SCs indicates that the absence of PMP22 increases proliferation, alters adhesion, and slows migration as compared to wild type SCs (Amici et al, unpublished). The changes in motility and cell adhesion without PMP22 may be caused by disruption in the cytoskeletal architecture of actin since reorganization of the actin network is critical for mediating cell motility. Moreover, the lamellipodia, normally actin-enriched areas, are collapsed in the PMP22-KO SCs. Thus to investigate the role of PMP22 in regulating cell shape and motility, we hypothesize that the absence of PMP22 alters the cytoskeletal actin network. Our interest in actin is further based on the known function and localization of actin in myelination. The effect PMP22 on modulating the actin network has not been studied, thus illuminating the link between PMP22 and actin may elucidate novel functions of PMP22.