Date of Graduation

5-2021

Document Type

Thesis

Degree Name

Bachelor of Science in Chemistry

Degree Level

Undergraduate

Department

Chemistry & Biochemistry

Advisor/Mentor

Kumar, Suresh

Committee Member/Reader

Adams, Paul

Committee Member/Second Reader

Ceballos, Ruben Michael

Committee Member/Third Reader

Strauss, Kim

Abstract

The Interleukin 1 family is a unique collection of cytokines in that they are primarily associated with both acute and chronic inflammation, which is associated with many diseases. In classical protein secretion, a protein, typically with an N-terminal signal peptide, is synthesized on a ribosome of a cell either in the cytoplasm or on the rough endoplasmic reticulum, transported to and merges with the Golgi apparatus, and is then sent to bind with either a lysosome or the cell membrane or is released from the cell via exocytosis. Thus, a non-classical secretion mechanism is any mechanism that differs from this. The classical mechanism usually applies to proteins with cell surface receptors, but not always. Additionally, many proteins undergo non-classical mechanisms because they lack a cell surface receptor, such as the N- terminal signal sequence, which is true of interleukin 1 alpha (IL-la). This project specifically focuses on coming to a better understanding of the non-classical release mechanism of IL-la. Current research shows that IL-la binds to a protein known as S100A13, a calcium binding protein, which is induced by divalent copper ions and then is released from the cell. This project largely desires to determine whether other divalent metal ions can be used to induce the IL-la release complex. More broadly, it is necessary to study and come to a better understanding of the non-classical release mechanism of IL-la from cells because this will improve treatment of inflammation induced diseases.

Keywords

IL-1a; Martin; Kumar; Biochemistry; Chemistry

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