Molecular Mechanism and Role of Translational Values of Heat Shock Protein (HSP27) in Various Disease

Abstract

HSP27, also known as HSPB1, was first discovered with a molecular weight 27kDa belonging to the four member gene family. Elevated levels of HSP27 are seen when different unfavorable conditions prevail such as increase in temperature and oxidative stress or exposure to heavy metals or organic solvents. They possess ATP-independent chaperone like activity which helps in maintaining protein homeostasis. It can also form large oligomers (300-600 kDa) containing different numbers of subunits. It is composed of total 205 amino acids. HSP27 undergoes post-translational modifications i.e. phosphorylation thereby converting large oligomers into dimers. It can act as an anti-apoptotic and antioxidant molecule during oxidative stress. The elevated form of HSP27 is also seen in some cancer belongs to breast, ovary, prostate, brain, colorectal, hepatocellular carcinoma, lung, liver, and cervical regions. Keeping in view of molecular roles of HSP27 signaling in various pathways, we have proposed their translational values in different diseases. In addition, we have also reported the existing scientific data on the HSP27 as the potential cancer biomarker and their therapeutic targets for improved prognosis and treatment in different diseases.

Assessment of Serum Levels of Oxidative Stress Markers and Heat Shock Proteins in Myocardial Infraction Patients

“…The distinction between cognate members or constitutively expressed members (e.g., Hsc70 and HSP90β) of HSP family and their isoforms are subjective due to cell tissue-restricted expression. The small HSP family comprises of HSP27 (15-42kDa), p 20, HSP-B3, MKBP/HSP-A crystalline and 𝛼-B-Crystalline [8]. All these HSPs play an essential role in protein folding, protein unfolding and cell survival from damage in response to environmental, physical and chemical stress stimuli.…”