Title:Role of Hsp70 in Cancer Growth and Survival
Volume: 19
Issue: 6
Author(s): Marcus P.D. Hatfield and Sandor Lovas
Affiliation:
Keywords:
Heat shock protein, Hsp70, structure, cancer, inhibition, housekeeping functions, apoptosis, substrate binding domain, cancer cells, nucleotide-binding domain (NBD), DnaK, ATPase, ATP-induced high-to-low affinity, phospholipases
Abstract: Hsp70 is a highly conserved protein that refolds misfolded proteins and has numerous housekeeping
functions which regulate apoptosis and other cell activities. Hsp70 consists of a nucleotide binding
domain which binds ATP and a substrate binding domain that binds misfolded proteins. The substrate binding
domain contains a peptide binding pocket which is covered by a helical lid. In humans, there are three
major cytosolic Hsp70 isotypes, Hsp70-8, Hsp70-1 and Hsp70-2. Leukemic and numerous other cancer
cells have a greater amount of Hsp70-1 and -2, which help the cancer cells inhibit apoptosis in response to
stress. This review summarizes the structure and role of Hsp70 proteins in cancer survival.
