[7] Its functions contribute to biological processes including signal transduction, apoptosis, protein homeostasis, and cell growth and differentiation.

Though the exact mechanism still remains unclear, there are at least two alternative modes of action: kinetic partitioning and local unfolding.

[7] Furthermore, this protein enhances antigen-specific tumor immunity by facilitating more efficient antigen presentation to cytotoxic T cells.

[5] Finally, Hsp72 can protect against disrupted metabolic homeostasis by inducing production of pro-inflammatory cytokines, tumor necrosis factor-α, interleukin 1β, and interleukin-6 in immune cells, thereby reducing inflammation and improving skeletal muscle oxidation.

In later stages of apoptosis the entire cell becomes fragmented, forming a number of plasma membrane-bounded apoptotic bodies which contain nuclear and or cytoplasmic elements.

The ultrastructural appearance of necrosis is quite different, the main features being mitochondrial swelling, plasma membrane breakdown and cellular disintegration.

Hsp70 member proteins, including Hsp72, inhibit apoptosis by acting on the caspase-dependent pathway and against apoptosis-inducing agents such as tumor necrosis factor-α (TNFα), staurosporine, and doxorubicin.

[6][8] As a result, tumor vaccine strategies for Hsp70s have been highly successful in animal models and progressed to clinical trials.

Though early speculation considered that Hsp72 expression might be affecting insulin sensitivity through a direct interaction with GLUT4, studies were unable to verify this link.

[9] Additionally, Hsp72 has been associated with another inflammatory condition, rheumatoid arthritis, and could be implemented to help diagnose and monitor disease activity in patients.