ROLE OF CHAPERONES AND ENDOPLASMIC RETICULUM STRESS IN PROTEIN COMPLEXITY ASSOCIATED WITH DYSLIPIDEMIA: A FUTURE PERSPECTIVE TO NOVEL THERAPEUTICS (REVIEW)

Abstract

Protein structure is extraordinarily complex and consists of various folding processes, namely, primary, secondary, tertiary and quaternary. Currently, researchers are eager to acquire knowledge and elucidate the mechanisms involved in these processes. Over the past decade, several studies have indicated that the endoplasmic reticulum stress (ERS) response assists in the protein response via intracellular signaling. ERS plays a key role in protein folding and unfolding. An increase in ERS promotes the unwinding of the folded protein. The present review specifically discusses the protein complexity involved in dyslipidemia (the condition of elevated cholesterol levels in the blood) with the ERS response and unfolded protein response. ERS in dyslipidemia is achieved by several pathological conditions, including oxidative stress, calcium imbalance and high levels of cholesterol in the blood. Therefore, in the present review, the ERS response in dyslipidemia is specifically highlighted as regards protein complexity, which indicates that considering oxidative stress, calcium imbalance and high levels of cholesterol would be a great benefit to reducing the ERS. The present literature review was performed using the search engines of the web‑based databases (Google Scholar and ScienceDirect) with keywords such as ‘Role of chaperones in dyslipidemia’ and ‘Protein complexity’ or ‘Protein involved in dyslipidemia’. Furthermore, the role of chaperones associated with ER in finding novel therapeutics for disease prevention is also discussed.