Student Work

Studies in Cell Signaling

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Phospholipase Cβ1 (PLCβ1) plays a vital role in intracellular signaling by catalyzing the formation of inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG) from phosphatidylinositol 4,5-bisphosphate (PIP2) in response to extracellular signals. The activation of PLCβ is controlled by G-protein alpha subunits, particularly Gαq, which initiate downstream signaling cascades that are important for various cellular processes. Additionally, PLCβ1 expression also has other diverse physiological functions, including neuronal differentiation, and has been implicated in cancer and neurological disorders. PC12 cells, derived from adrenal medulla’s pheochromocytoma in rats, are used to research neuronal differentiation and neurotoxicity when monitoring the expression of PLCβ1. Differentiation of PC12 cells induces PLCβ1 expression, which we propose influences the localization of Ago2, TRBP, and Egr-1 proteins. This study aimed to investigate the relocalization of Ago2 and TRBP proteins upon PLCβ1 expression modulation. The methods followed for this research involved cell culture, differentiation, transfection for PLCβ1 silencing, fixation, immunostaining, and TIRF-cell imaging. Understanding the interaction between PLCβ1 and the associated proteins in differentiated and transfected PC12 cells opens doors to potential therapeutic targets for neurological disorders and cancer.

  • This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.
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Identifier
  • 121568
  • E-project-042424-174155
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Year
  • 2024
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Date created
  • 2024-04-24
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Major
Source
  • E-project-042424-174155
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