Study on the role of heat shock protein 90 ( HSP90 ) gene in chicken preadipocytes proliferation and differentiation.
Xincheng KangChenglin ZhongXiaxia DuFelix Kwame AmevorAli Mujtaba ShahQing ZhuYaofu TianGang ShuYan WangXiaoling ZhaoPublished in: Animal biotechnology (2022)
In this study, we examined the effects of Heat Shock Protein 90 ( HSP90 ) on adipocyte proliferation and differentiation in chickens. To achieve this, we constructed RNA interference (RNAi) vectors to target HSP90 and transfected the vectors into primary adipocytes. After transfection, oil red O staining was performed to determine the status of triglyceride accumulation in the cells, whereas the CCK-8 cell kit and 5-Ethynyl-2'-Deoxyuridine (EdU) assays were used to determine cell proliferation. Thereafter, the mRNA and protein expression levels of PPARγ , FAS , SREBP-1c, and HSP90 were determined, and the results showed that after the interference of HSP90 , the mRNA and protein expression levels of HSP90 in the chicken adipocytes decreased significantly compared to the control and blank groups ( p < 0.05 ). The decreased mRNA and protein expression of PPARγ , FAS , and SREBP-1c was related to adipocyte differentiation ( p < 0.05 ). However, HSP90 interference had no effect on adipocyte proliferation ( p > 0.05 ). Taken together, the results of this study showed that HSP90 influenced the expression of PPARγ and adipose-differentiation-related genes, thereby regulating triglyceride accumulation and adipocyte differentiation in chickens.
Keyphrases
- heat shock protein
- heat shock
- adipose tissue
- insulin resistance
- heat stress
- fatty acid
- cell proliferation
- stem cells
- induced apoptosis
- binding protein
- skeletal muscle
- wastewater treatment
- gene expression
- mesenchymal stem cells
- metabolic syndrome
- cell death
- high throughput
- dna methylation
- bone marrow
- cell cycle
- cell therapy