Hsp70 (70 kDa heat shock protein) is a molecular chaperone that is involved in protein folding and the protection of proteins from damage during stress. The expression of Hsp70 is increased under conditions of thermal stress or in the presence of toxic chemicals such as heavy metals.
Hsp70 binds in an ATP-dependent manner to sequences of hydrophobic residues. These can be on nascent polypeptide chains emerging from the ribosome, or exposed on other proteins by stress conditions. Binding by Hsp70 promotes folding of newly synthesized or mis-folded proteins to their native state. Hsp70 also prevents non-native protein aggregation by binding along with co-chaperones of the J-domain protein (JDP) family to hydrophobic residues of substrate molecules shielding them from other intermolecular attractions.
Hsp70 interacts with numerous eukaryotic regulatory proteins including nuclear receptors, kinases (e.g. Raf-1) and transcription factors. Hsp70 also acts in concert with other chaperones (e.g. Hsp90) and is regulated by a number of co-chaperones/accessory proteins (e.g. p23, Cdc37).
Hsp70 also interacts with key regulatory proteins ('clients') of signal transduction pathways for the control of cell homeostasis, proliferation, differentiation and cell death. For example, Hsp70 is involved in the caspase pathway and acts as a general antiapoptotic agent (such as Bcl-2) that inhibits heat shock-induced apoptosis. Hsp70 prevents the activation of caspase-3, PARP cleavage, DNA laddering and therefore apoptotic cell death- but has no effect on cytochrome c release.
Hsp70 family members include the constitutively expressed chaperone Hsc70, which facilitates protein folding and GRP-78 (78kDa glucose-regulated protein) involved in the transportation of proteins to the endoplasmic reticulum.View all products for Hsp70 »
Literature for Hsp70
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