Prokaryotic and eukaryotic organisms respond to heat shock or other environmental stress by inducing the synthesis of proteins collectively known as heat-shock proteins (hsp).

An immunophilin of M r 59K is known to associate with two heat-shock proteins (Hsp90 and Hsp70) and the glucocorticoid receptor.

It combines the antigens with a heat-shock protein, which plays a role in presenting them to the immune system.

Plants protect themselves from frost and dehydration stress with antifreeze proteins, heat-shock proteins and sugars (sucrose is common).

In the E2 classical pathway or estrogen classical pathway, 17β estradiol (E2) enters the cytoplasm, where it causes dissociation of heat-shock protein (HSP).

In the receptors' quiescent state, they are covered by substances, called heat-shock proteins, that keep them in a state of readiness to bind to estrogen.

Gene expression studies revealed changes in expression of genes for heat-shock proteins, catalase, β-1,3-glucanase and genes involved in photosynthesis.

This discovery eventually led to the identification of the heat-shock proteins (HSP) or stress proteins whose expression these puffs represented.

Extracellular and membrane bound heat-shock proteins, especially Hsp70 are involved in binding antigens and presenting them to the immune system.

Most cMVs contain the so-called "heat-shock proteins" hsp70 and hsp90, which can facilitate interactions with cells of the immune system.