Small heterodimer partner-interacting XXXX zipper protein inhibits adipogenesis by regulating Peroxisome proliferator-activated receptor y activity.

@entity2426 @entity28 @entity368 @entity2425 @entity30206 @entity72059
AIMS: Adipocytes play a critical role in energy balance. Growth of fat tissue is achieved via an increase in adipocyte mass and the formation of newly differentiated adipocytes from precursor cells. Understanding the cellular and molecular mechanisms of adipocyte differentiation is crucial for the study of @entity28 - and fat-related diseases. The present study was designed to study whether small heterodimer partner-interacting @entity368 zipper protein ( @entity72059 ), a novel co-repressor, could regulate differentiation of adipocyte in 3T3-L1 cells. MATERIALS AND METHODS: Treatment of endoplasmic stress inducers, @entity2426 and @entity2425 , inhibited adipocyte differentiation, stimulated @entity72059 mRNA expression, and repressed the expression of adiponectin ( @entity30206 ) in 3T3-L1 pre-adipocyte. Overexpression of @entity72059 in 3T3-L1 cells decreased the expression of the mRNA encoding @entity30206 , a major marker of adipocytes, significantly. Furthermore, knockdown of @entity72059 recovered the @entity2426 -mediated repression of @entity30206 transcription. Co-immunoprecipitation experiments revealed that @entity72059 interacted physically with PPARy in 3T3-L1 cells. In addition, chromatin immunoprecipitation experiments revealed that @entity72059 suppressed the binding affinity of PPARy for the @entity30206 promoter. KEY FINDINGS: we demonstrate that @entity72059 controls adipocyte differentiation by regulating the transactivity of peroxisome proliferator-activated receptor y (PPARy). SIGNIFICANCE: These findings demonstrate that @entity72059 represses adipocyte differentiation by regulating PPARy transactivity; hence, @entity72059 is a potential regulator of PPARy-related diseases.
