Honors College Thesis

 

Comparing 26S Proteasome Efficiency Between Long-Living and Short-Living Rodents 公开 Deposited

可下载的内容

下载PDF文件
https://ir.library.oregonstate.edu/concern/honors_college_theses/vd66w2133

Descriptions

Attribute NameValues
Creator
Abstract
  • Many people die yearly worldwide due to diseases associated with aging, and if the process of aging in humans was more understood, the health of these patients could be improved. While many biochemical actions are involved with the aging process, loss of proteostasis has been called one of the most important causes of aging. When proteostasis is lost, proteins in the cells cannot be properly checked for quality, and build-up of toxic protein can occur. The 26S proteasome is a mechanism of proteostasis, degrading improperly folded proteins before they become toxic to the cell. While the exact mechanisms are known for how the 26S proteasome affects aging in short-living mammals, it is not well-known how it affects aging in long-living mammals. A comparative biology approach was used for this project, where a traceable 26S proteasome cellular signal was used to compare the efficiencies of the proteasome between naked mole rats, a long-living species, and mice, a short-living species. It was hypothesized that naked mole rats have a higher 26S proteasome efficiency than mice, and the aim of this study was to quantify that difference. Problems with methods and mouse cell lines made it so final comparative efficiencies could not be made between naked mole rats and mice, but protocols were refined and optimized. The end result of this project is a proposed protocol that is likely to gain data relevant to the project’s aim. Key Words: aging, proteostasis, 26S proteasome, ubiquitin, fusion proteins, naked mole rat, fluorescent quantification
License
Resource Type
Date Available
Date Issued
Degree Level
Degree Name
Degree Field
Degree Grantor
Commencement Year
Advisor
Non-Academic Affiliation
权利声明
Funding Statement (additional comments about funding)
  • Biochemistry and Biophysics department, KARE and CURE awards
Publisher
Peer Reviewed
Language
Replaces

关联

Parents:

This work has no parents.

属于 Collection:

单件