Targeting of Heat Shock Proteins by Natural Products in Cancer


ÖNAY UÇAR E., PEKMEZ M. , ARDA E. Ş. N.

in: Molecular Oncology: Underlying Mechanisms and Translational Advancements, Farooqi A.A., Ismail M., Editor, Springer-Verlag , Cham, pp.173-193, 2017

  • Publication Type: Book Chapter / Chapter Vocational Book
  • Publication Date: 2017
  • Publisher: Springer-Verlag
  • City: Cham
  • Page Numbers: pp.173-193
  • Editors: Farooqi A.A., Ismail M., Editor

Abstract

Initially discovered as a group of proteins showing significantly higher
expression in response to heat stress, Heat shock proteins (HSPs) have gained
considerable appreciation. Overwhelmingly increasing scientific evidence has
highlighted the role of these proteins as molecular chaperones which trigger protein
holding and folding thus facilitating freshly synthesized protein/s to achieve
mature and biologically active conformation. It is becoming progressively more
understandable that HSPs are involved in post-translational modification of proteins
of signaling cascades, modulation of apoptosis related proteins, assembly
and disassembly of transcriptional machinery. Recently emerging functional and
structural data has provided new insights related to biochemical regulation of
HSPs and the structural dynamics used by these proteins to act on a diverse client
repertoire.
Different strategies are currently being tested to effectively inhibit/downregulate
HSPs in cancer cells. Wide ranging natural products, particularly, antioxidant compounds,
prevent HSP expression and induce apoptosis in tumor cells. Besides, these
compounds help to reduce off-target effects of radio- or chemotherapies in many
types of cancers.
Plethora of information has considerably improved our understanding of the
molecular and cellular basis of HSP induced regulation of myriad of proteins and
these insights may lead to the development of efficient therapeutic agents. The
current chapter focuses on suppression of HSPs by using natural compounds in
cancer cells.