A NOVEL REVIEW OF HEAT SHOCK PROTEIN 110 KDA: A BASIS FOR RESEARCH AND CONTINUED EXPERIMENTATION THROUGH BIOCHEMICAL ANALYSIS

Author

Crist W. Cuffee, Virginia Commonwealth UniversityFollow

DOI

https://doi.org/10.25772/7ZV2-6528

Defense Date

2021

Document Type

Thesis

Degree Name

Master of Science

Department

Biochemistry

First Advisor

Dr. Qinglian Liu

Second Advisor

Dr. Carmen Sato-Bigbee

Third Advisor

Dr. Can Senkal

Abstract

Heat shock protein 110 kDa, Hsp110, is a distinct cellular protector, different in form and function from Hsp70, a close relative of Hsp110. Functioning primarily as a holdase or in tandem with other molecular chaperones, a review of current accomplishments elucidates the uniqueness of this protein and the continued mysteries that surrounds it. Found only in eukaryotes, Hsp110 has been linked to many diseases, ranging from parasitic infection to neurodegenerative disorders. While still lacking, studies of this protein have provided much in the realm of speculation on the mechanisms behind Hsp110s’ contribution to different pathologies. This review will serve as an introduction to present thinking and provide preliminary data investigating the form and function of this chaperone.

Rights

© The Author

Is Part Of

VCU University Archives

Is Part Of

VCU Theses and Dissertations

Date of Submission

7-6-2021