The investigation of small heat shock protein expression under endoplasmic reticulum stress treated c2c12 myotubes
Year: 2024
Type: dissertation
Abstract: Skeletal muscle function declines with age and is associated with reduced health span. Dysregulated proteostasis is a key hallmark of ageing, characterised by an imbalance between protein synthesis, breakdown, and folding within the cell. To counteract this, chaperones are expressed to prevent the accumulation of misfolded protein species. The endoplasmic reticulum (ER) is crucial for maintaining protein and ensuring the newly synthesized proteins are folded correctly to achieve their functional form, which can be disrupted under stressful conditions. Research, including our lab preliminary data, revealed that ER stress-related and unfolded protein response (UPR) signaling pathways proteins are altered in aged mouse skeletal muscle. Furthermore, another group of proteins, small heat shock protein (sHSP), which performs holdase function under general protein aggregation, also recorded an increase in the data. We hypothesized that ER stresses stimulate the expression of sHSP to prevent the formation of protein aggregates. Herein, this thesis used two different pharmacological ER stress inducers, Tunicamycin and Thapsigargin, in C2C12 myotubes to investigate the regulation of sHSP under ER stress. Our results show that HSPB1 and HSPB6 decrease throughout ER stress whilst HSPB5 and HSPB7 remain unchanged. The results show that ER stress regulates sHSP expressions throughout two types of ER stress inducers. Altogether, this thesis improves the understanding of sHSP regulation under various types of unfolded protein responses in skeletal muscle.
Author: Ng, Jimi
Language: English
Topic: Heat shock proteins research
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W7134880373