Radiosynthesis and preclinical evaluation of [¹¹C]SNX-ab as an Hsp90α,β isoform-selective PET probe for in vivo brain and tumour imaging.

ABSTRACT:

Background

The molecular chaperone, Hsp90, is a key player in the protein quality control system that maintains homeostasis under cellular stress conditions. It is a homodimer with ATP-dependent activity, and is a prominent member of the chaperone machinery that stabilizes, matures and (re)folds an extensive list of client proteins. Hsp90 occurs as four isoforms, cytosolic Hsp90α and Hsp90β, mitochondrial TRAP1 and Grp94 present in the endoplasmic reticulum. An aberrant role of Hsp90 has been attributed to several cancers and neurodegenerative disorders. Consequently, Hsp90 has emerged as an attractive therapeutic target. However, pan-Hsp90 inhibition often leads to detrimental dose-limiting toxicities. Novel strategies for Hsp90-targeted therapy intend to avoid this by using isofo

SUBMITTER: Cools R 

PROVIDER: S-EPMC9886718 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature