Glycosylation and localization of clusterin in esophageal squamous cell carcinoma / 第二军医大学学报

ABSTRACT

Objective:To study the glycosylation of different clusterin isoforms and the alterations of their intracellular localizations in esophageal squamous cell carcinoma(ESCC),so as to better understand the potential mechanisms of clusterin in tumorigenesis of ESCC.Methods: The glycosylation of clusterin proteins was studied after treated with PGNase-F by Western blot analysis in 23 ESCC specimens and their corresponding adjacent tissues.Immunohistochemical staining was used to visualize the intracellular localization of clusterin proteins.Results: Mature clusterin,a 40 000 glycosylated protein in SDS-PAGE gel,(usually) presents in the connective tissues of the lamina propria of esophageal epithelial mucosa,and is secreted by esophageal glands onto the esophageal mucosa and in plasm.The glycosylation of clusterin proteins was abnormal in the 23 ESCC specimens,with the premature clusterin and nuclear clusterin aggregated in the cells and the mature clusterin decreased or disappeared in the stromal layer of esophagus.Conclusion: The deglycosylation and localization alterations of clusterin in ESSC may be closely associated with the tumorigenesis of ESCC.