Connections Between Protein Misfolding and Monobenzone-Induced Vitiligo
Date of Award
6-2017
Degree Type
Thesis
Degree Name
Master of Science in Biochemistry & Molecular Biology
Department
Biology
Chief Instructor
Jillian Richmond
Second Reader
Noel D. Lazo
Third Reader
Denis Larochelle
Keywords
Molecular biology, Biochemistry, Immunology
Abstract
Vitiligo, an autoimmune disease affecting melanocytes, causes areas of skin to completely lose pigment. These colorless lesions can spread, eventually leading to the complete absence of skin and hair pigment in some patients. Exposure to monobenzyl ether of hydroquinone (MBEH), or monobenzone, is an environmental trigger of this disfiguring disease. In this study, we aimed to elucidate the mechanism of this phenomenon by studying monobenzone's inhibition of tyrosinase, a melanocyte enzyme that plays a key role in melanin production. As tyrosinase is an oxidizing enzyme, we hypothesized that when inhibited by monobenzone, resulting elevated levels of reactive oxygen species (ROS) lead to tyrosinase misfolding and initiate the unfolded protein response, thus creating a link between a person's levels of active tyrosinase and their sensitivity to depigmentation by monobenzone. To test this hypothesis, studies of the effects of monobenzone on tyrosinase in simple solutions of tyrosinase and monobenzone, cell lines, primary cells and samples of human skin were conducted.
Recommended Citation
Carty, Senegal, "Connections Between Protein Misfolding and Monobenzone-Induced Vitiligo" (2017). Biology. 22.
https://commons.clarku.edu/biology_masters_papers/22