The Effects of Different Compounds on PLCβ-1 Activity in HL-1 Cells

Session Number

C33

Advisor(s)

Gary Aistrup, Northwestern University
William Marszalec, Northwestern University
J. Andrew Wasserstrom, Northwestern University

Location

B-110

Start Date

28-4-2016 8:25 AM

End Date

28-4-2016 8:50 AM

Abstract

In hearts, the T-tubules allow calcium ions to enter the organ, which will then initiate a pathway that allows the heart to contract. Studies have shown that over time, T-tubules will lose their structure, leading to less efficient contraction and eventual heart failure. One protein that causes this is phospholipase Cβ-1 (PLCβ-1), which, when activated, cleaves and deactivates phosphatidylinositol 4,5-bisphosphate (PIP2), a protein that supports the stability of T-tubules. Eighteen different chemical compounds were previously determined to be able to theoretically prevent PLCβ-1 from binding to its receptor, protecting T-tubules from remodeling. Our investigation treated HL-1 cells, a type of tumor cell isolated from mouse hearts, with the compounds in order to see which ones were able to lower the activity of PLCβ-1.


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Apr 28th, 8:25 AM Apr 28th, 8:50 AM

The Effects of Different Compounds on PLCβ-1 Activity in HL-1 Cells

B-110

In hearts, the T-tubules allow calcium ions to enter the organ, which will then initiate a pathway that allows the heart to contract. Studies have shown that over time, T-tubules will lose their structure, leading to less efficient contraction and eventual heart failure. One protein that causes this is phospholipase Cβ-1 (PLCβ-1), which, when activated, cleaves and deactivates phosphatidylinositol 4,5-bisphosphate (PIP2), a protein that supports the stability of T-tubules. Eighteen different chemical compounds were previously determined to be able to theoretically prevent PLCβ-1 from binding to its receptor, protecting T-tubules from remodeling. Our investigation treated HL-1 cells, a type of tumor cell isolated from mouse hearts, with the compounds in order to see which ones were able to lower the activity of PLCβ-1.