Hsp60 (human, recombinant)

Heat shock protein 60 (Hsp60), also known as heat shock protein family D member 1 (HspD1), is an approximately 60 kDa protein that functions as a molecular chaperone.¹ It belongs to the type I subclass of chaperonins and is found in eubacteria, mitochondria, and chloroplasts where its expression is induced by stress. Hsp60 primarily exists as a heptameric ring that it is converted to a tetradecameric double-ring structure in the presence of ATP.² Within mitochondria, it associates with its co-chaperone, Hsp10, to form a barrel-like structure and refold proteins that have been shuttled to the mitochondria in an ATP-dependent manner.^2,3 Hsp60 also has extramitochondrial functions such as the production of proinflammatory cytokines in human leukocytes and activation of innate immune receptors.^4,5 Hsp60 expression is increased in the serum and saliva of patients with type 2 diabetes mellitus and mutations in HSPD1 lead to neurodegenerative diseases.^5,6

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1. Levy-Rimler, G., Bell, R.E., Ben-Tal, N., et al. Type I chaperonins: Not all are created equal. FEBES Lett. 529(1), 1-5 (2002).

2. Okamoto, T., Yamamoto, H., Kudo, I., et al. HSP60 possesses a GTPase activity and mediates protein folding with HSP10. Sci. Rep. 7(1), 16931 (2017).

3. Nisemblat, S., Parnas, A., Azem, A., et al. Crystallization and structure determination of a symmetrical “football” complex of the mammalian mitochondrial Hsp60-Hsp10 chaperonins. Acta Crystallogr. F Struct. Biol. Commun. 70(Pt 1), 116-119 (2013).

4. Osterloh, A., Meier-Stiegen, F., Veit, A., et al. Lipopolysaccharide-free heat shock protein 60 activates T cells. The Journal of Biological Chemisty 279(46), 47906-47911 (2004).

5. Juwono, J., and Martinus, R.D. Does Hsp60 Provide a Link between Mitochondrial Stress and Inflammation in Diabetes Mellitus? J. Diabetes Res. 2016:8017571, (2016).

6. Bross, P., and Fernandez-Guerra, P. Disease-associated mutations in the HSPD1 gene encoding the large subunit of the mitochondrial HSP60/HSP10 chaperonin complex. Front. Mol. Biosci. 3(49), 1-7 (2016).