Wan-Qi Lv1, Jing Peng2, Hai-Cheng Wang3, De-Ping Chen2, Yue Yang4, Yang Zhao2, Xiao-Yan Qiu5, Jiu-Hui Jiang6, Cui-Ying Li7. 1. Central Laboratory, Peking University School and Hospital of Stomatology, 22 South Zhongguancun Avenue, Haidian District, Beijing 100081, China. 2. Department of Beijing Citident Stomatology Hospital, 109 North Xidan Avenue, Xicheng District, Beijing 100032,China. 3. Department of Oral Pathology, School and Hospital of Stomatology, Tongji University Shanghai Engineering Research Center of Tooth Restoration and Regeneration, Shanghai 200072, China. 4. Department of Dentistry Capital Medical University Xuanwu Hospital, 45 Changchun Street, Xicheng District, Beijing 100053, China. 5. Department of Immunology, Key Laboratory of Medical Immunology, Ministry of Health, School of Basic Medical Sciences, Peking University, Beijing 100191, China. Electronic address: qiuxy@bjmu.edu.cn. 6. Department of Orthodontics, Peking University School and Hospital of Stomatology, 22 South Zhongguancun Avenue, Haidian District, Beijing 100081, China. Electronic address: drjiangw@gmail.com. 7. Central Laboratory, Peking University School and Hospital of Stomatology, 22 South Zhongguancun Avenue, Haidian District, Beijing 100081, China. Electronic address: licuiying_67@163.com.
Abstract
OBJECTIVE: Cancer-IgG is a newly-discovered molecule, mainly derived from epithelial carcinoma cells and is significantly correlated with differentiation, metastasis, local invasion, and poor prognosis of many cancers. In our previous study we detected IgG expression in oral epithelial carcinoma, including salivary adenoid cystic carcinoma (SACC), using an IgG-specific commercial antibody. Here, we explored the correlation between cancer-IgG and clinicopathological features of SACC. DESIGN: A total of 68 human SACC tissue specimens and 2 siRNAs were used to analyze the correlation between cancer-IgG and extra domain A (EDA+)-containing fibronectin using the cancer-IgG-specific monoclonal antibody, RP215. RESULTS: We found an unexpected correlation between cancer-IgG and EDA+ fibronectin, both of which showed aberrant expression in SACC tissue samples. Both were highly expressed in SACC with nerve invasion. In our previous study, EDA+ fibronectin overexpression in SACC cells decreased N-cadherin expression. In the present study, we used SACC-83 cells, wherein EDA+ fibronectin is overexpressed and cancer-IgG is knocked down. EDA+ fibronectin expression was reduced with cancer-IgG knockdown, while cancer-IgG expression did not affect EDA+ fibronectin overexpression. Furthermore, knockdown of non-B cell-derived IgG in SACC cells decreased cellular motility (P<0.05) as well as increased E-cadherin and alpha-smooth muscle actin levels. CONCLUSION: The results suggest that cancer IgG potentially regulates EDA+ fibronectin expression, thereby suggesting possible new therapeutic approaches for SACC.
OBJECTIVE:Cancer-IgG is a newly-discovered molecule, mainly derived from epithelial carcinoma cells and is significantly correlated with differentiation, metastasis, local invasion, and poor prognosis of many cancers. In our previous study we detected IgG expression in oral epithelial carcinoma, including salivary adenoid cystic carcinoma (SACC), using an IgG-specific commercial antibody. Here, we explored the correlation between cancer-IgG and clinicopathological features of SACC. DESIGN: A total of 68 human SACC tissue specimens and 2 siRNAs were used to analyze the correlation between cancer-IgG and extra domain A (EDA+)-containing fibronectin using the cancer-IgG-specific monoclonal antibody, RP215. RESULTS: We found an unexpected correlation between cancer-IgG and EDA+ fibronectin, both of which showed aberrant expression in SACC tissue samples. Both were highly expressed in SACC with nerve invasion. In our previous study, EDA+ fibronectin overexpression in SACC cells decreased N-cadherin expression. In the present study, we used SACC-83 cells, wherein EDA+ fibronectin is overexpressed and cancer-IgG is knocked down. EDA+ fibronectin expression was reduced with cancer-IgG knockdown, while cancer-IgG expression did not affect EDA+ fibronectin overexpression. Furthermore, knockdown of non-B cell-derived IgG in SACC cells decreased cellular motility (P<0.05) as well as increased E-cadherin and alpha-smooth muscle actin levels. CONCLUSION: The results suggest that cancer IgG potentially regulates EDA+ fibronectin expression, thereby suggesting possible new therapeutic approaches for SACC.