Key role of heat shock protein 90 in leptin-induced STAT3 activation and feeding regulation.

ABSTRACT:

Background and purpose

Leptin, an important regulator of the energy balance, acts on the brain to inhibit feeding. However, the mechanisms involved in leptin signalling have not yet been fully elucidated. Heat shock protein 90 (HSP90) is a molecular chaperone that is involved in regulating cellular homeostasis. In the present study, we investigated the possible involvement of HSP90 in leptin signal transduction.

Experimental approach

HEK293 and SH-SY5Y cell lines stably transfected with the Ob-Rb leptin receptor (HEK293 Ob-Rb, SH-SY5Y Ob-Rb) were used in the present study. Phosphorylation of JAK2 and STAT3 was analysed by western blotting. An HSP90 inhibitor was administered i.c.v. into rats and their food intake was analysed.

Key results

The knock-down of HSP90 in th

SUBMITTER: Hosoi T 

PROVIDER: S-EPMC4945768 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature