Investigation of the relationship between Calcium Binding Proteins and Proapoptotic Proteins with Programmed Cell Death
Primary Faculty Mentor’s Name
C. Michele Davis McGibony
Proposal Track
Student
Session Format
Poster
Abstract
Calcium plays a number of roles in the control of important vital cell functions, including the triggering of mitotic cell division and the regulation of apoptosis. Although the mechanism is still unclear, there is building evidence that calcium and the concentration in which it presents itself, has a definite involvement in apoptosis. Apoptosis is the success of an ordered, sequential cascade of cellular events. The different proteins that bind calcium play a major role in the turning on or off of apoptosis. These proteins often contain various EF hand sites and bind calcium differently at each site, influencing the protein’s interaction with cysteine proteases, also referred to as caspases. Caspases are responsible for the intracellular substrate degradation that occurs in the cell death process. Previous data has shown that when calcium is present and calcium binding proteins, such as Calbindin D28K interact with the caspases, apoptosis can become inhibited. The overall goal of this project is to determine the specific involvement of calcium in apoptosis and how the interactions effect caspases, which are responsible for executing apoptosis. Determining this link could provide important insight into how cell death can be directly caused or prevented. There are a number of different proapoptotic proteins present in cells responsible for the undergoing of apoptosis, and there are a number of different calcium binding proteins that can potentially interact with them. These proteins will be studied to determine their relationship with calcium and programmed cellular death.
Keywords
Caspase, Calcium, Apoptosis
Location
Concourse and Atrium
Presentation Year
2015
Start Date
11-7-2015 10:10 AM
End Date
11-7-2015 11:20 AM
Publication Type and Release Option
Presentation (Open Access)
Recommended Citation
Smith, Brianna G. and Davis McGibony, C. Michele, "Investigation of the relationship between Calcium Binding Proteins and Proapoptotic Proteins with Programmed Cell Death" (2015). Georgia Undergraduate Research Conference (2014-2015). 19.
https://digitalcommons.georgiasouthern.edu/gurc/2015/2015/19
Investigation of the relationship between Calcium Binding Proteins and Proapoptotic Proteins with Programmed Cell Death
Concourse and Atrium
Calcium plays a number of roles in the control of important vital cell functions, including the triggering of mitotic cell division and the regulation of apoptosis. Although the mechanism is still unclear, there is building evidence that calcium and the concentration in which it presents itself, has a definite involvement in apoptosis. Apoptosis is the success of an ordered, sequential cascade of cellular events. The different proteins that bind calcium play a major role in the turning on or off of apoptosis. These proteins often contain various EF hand sites and bind calcium differently at each site, influencing the protein’s interaction with cysteine proteases, also referred to as caspases. Caspases are responsible for the intracellular substrate degradation that occurs in the cell death process. Previous data has shown that when calcium is present and calcium binding proteins, such as Calbindin D28K interact with the caspases, apoptosis can become inhibited. The overall goal of this project is to determine the specific involvement of calcium in apoptosis and how the interactions effect caspases, which are responsible for executing apoptosis. Determining this link could provide important insight into how cell death can be directly caused or prevented. There are a number of different proapoptotic proteins present in cells responsible for the undergoing of apoptosis, and there are a number of different calcium binding proteins that can potentially interact with them. These proteins will be studied to determine their relationship with calcium and programmed cellular death.
