Effect of Regulating the Expression of HSP47 on Collagen Metabolism in Scleral Fibroblasts. (4th March 2021)

• Record Type: Journal Article
• Authors: Guo, Qingge; Tian, Qingshan; Tian, Xiang; Liu, Taixiang
• Is Part Of: Current eye research. Volume 46:Number 3(2021)
• Page Start: 408
• Page End: 416
• Publication Date: 2021-03-04
• Subjects: HSP 47 -- collagen -- scleral fibroblasts -- α-SMA; Ophthalmology -- Periodicals; Eye -- Diseases -- Periodicals; Ophthalmology -- Periodicals; 573.88
• DOI: 10.1080/02713683.2020.1805471
• Languages: English
• ISSNs: 0271-3683

Abstract

ABSTRACT: Purpose: To explore the effect of heat shock protein 47 (HSP 47) on collagen (types I, III, and V) metabolism in scleral fibroblasts. Methods: Scleral fibroblasts with over- or low-expression of HSP 47 were constructed by plasmid transfection. The mRNA and intracellular proteins expression of HSP 47, collagen (types I, III, and V) and α-smooth muscle actin (α-SMA) were detected by quantitative real-time polymerase chain reaction and western blot. The proteins expression of collagen (types I, III, and V), matrix metalloproteinase 2 (MMP-2), and tissue inhibitor of matrix metalloproteinases 1 and 2 (TIMP-1 and −2) in extracellular matrix (ECM) were detected by ELISA. The migration and proliferation activities of cells were detected by scratch-wound assay and MTS. The internal structure of scleral fibroblasts was observed by transmission electron microscopy (TEM). Results: The results obtained demonstrated significant increases in the expression of the mRNA and protein expression of collagen I in HSP47 up-regulated cells. Overexpression of HSP 47 promotes the expression of α-SMA and cell migration. Down-regulated expression of HSP 47 results in decreased mRNA and protein expression of collagen. Low expression of HSP 47 significantly inhibits cell migration and proliferation, and affects the internal structure of cells. Conclusion: HSP 47 affects collagen metabolism in scleral fibroblasts. It appears to promote the synthesis and secretion of collagen I as well as inhibit degradation.