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

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Sameer Chaudhary
Sapana Sameer Chaudhary
Sakshi Rawat
Savneet Kaur
Bogireddy Devi
Malik M. Ahmad
Zia Arshad
M. Mustafa
Manie M. Al Jedaie
Pravej Alam


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.

Heat shock protein, chaperone, phosphorylation, apoptosis, cancer, biomarker.

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How to Cite
Chaudhary, S., Chaudhary, S. S., Rawat, S., Kaur, S., Devi, B., Ahmad, M. M., Arshad, Z., Mustafa, M., Jedaie, M. M. A., & Alam, P. (2020). Molecular Mechanism and Role of Translational Values of Heat Shock Protein (HSP27) in Various Disease. Journal of Pharmaceutical Research International, 32(24), 110-118.
Review Article


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