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Heat shock protein 47 effects on hepatic stellate cell-associated receptors in hepatic fibrosis of Schistosoma japonicum-infected mice
- Source :
- Biological Chemistry. 398:1357-1366
- Publication Year :
- 2017
- Publisher :
- Walter de Gruyter GmbH, 2017.
-
Abstract
- The study aimed to explore the regulation of heat shock protein 47 (HSP47) on expressions of receptors associated with hepatic stellate cell (HSC) in liver fibrosis mouse models induced bySchistosoma japonicum(S. japonicum). Mouse fibroblasts (NIH/3T3) were transfected with HSP47 shRNA plasmid by lipofectamine transfection, and experimental fibrosis in HSCs was studied inS. japonicummouse models treated with HSP47 shRNAin vivo. HSP47 expression was assessed using Western blot and real-time PCR. Flow cytometry was adopted to determine the expression of cell membrane receptors. HSP47-shRNA could markedly down-regulate the expression of collagen (Col1a1 and Col3a1). The expressions of HSP47, endothelin receptor A (ETAR) and endothelin receptor B (ETBR) significantly increased in the liver tissue of infected mice. However, the expressions of ETAR and HSP47 and ETBR remarkably decreased after the administration of HSP47 shRNAin vitroandin vivo. ETAR and ETBR levels were found to be positively correlated with HSP47 expression. HSP47 might exert influence on liver fibrosis via the regulation of ETAR and ETBR.
- Subjects :
- Liver Cirrhosis
0301 basic medicine
animal structures
Clinical Biochemistry
Biochemistry
Schistosoma japonicum
Mice
03 medical and health sciences
Fibrosis
Hepatic Stellate Cells
medicine
Animals
Receptor
HSP47 Heat-Shock Proteins
Molecular Biology
Cells, Cultured
Heat shock protein 47
Mice, Inbred BALB C
biology
Chemistry
Receptor, Endothelin A
medicine.disease
biology.organism_classification
Receptor, Endothelin B
Molecular biology
Disease Models, Animal
030104 developmental biology
Lipofectamine
embryonic structures
NIH 3T3 Cells
biology.protein
Hepatic stellate cell
Female
Endothelin receptor
Hepatic fibrosis
Subjects
Details
- ISSN :
- 14374315 and 14316730
- Volume :
- 398
- Database :
- OpenAIRE
- Journal :
- Biological Chemistry
- Accession number :
- edsair.doi.dedup.....5c5f81c215bfc32bb28562da6bbde354
- Full Text :
- https://doi.org/10.1515/hsz-2017-0177