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.
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http://dx.doi.org/10.1016/j.archoralbio.2017.04.010 | DOI Listing |
Sci Rep
December 2024
Clinical Department of Anesthesiology and Intensive Therapy, Wroclaw Medical University, Borowska 213, 50-556, Wroclaw, Poland.
Coronary artery bypass grafting (CABG) with cardiopulmonary bypass (CPB) is associated with the transient activation of a systemic inflammatory response. Fibronectin (FN), an endogenous inflammatory mediator, is a key component of the extracellular matrix. This study aimed to detect changes in cellular and plasma FN levels, as well as its potential fragmentation or FN-fibrin complex formation, in 40 patients undergoing CABG with CPB.
View Article and Find Full Text PDFbioRxiv
September 2024
Department of Bioengineering, Temple University, Pennsylvania.
Fibronectin (Fn) is an extracellular matrix glycoprotein with mechanosensitive structure-function. EDA Fn, a Fn isoform, is not present in adult tissue but is required for tissue repair. Curiously, EDA Fn is linked to both regenerative and fibrotic tissue repair.
View Article and Find Full Text PDFInvest Ophthalmol Vis Sci
October 2024
University of Wisconsin-Madison, Madison, Wisconsin, United States.
Genes Dis
November 2024
Department of Oncology, Southwest Hospital, Third Military Medical University (Army Medical University), Chongqing 400038, China.
Biochem Biophys Res Commun
November 2024
Center for Regenerative Medicine, Medical Research and Education Institute, Lomonosov Moscow State University, 119192, Moscow, Russia.
Establishing the molecular and cellular mechanisms of fibrosis requires the development of validated and reproducible models. The complexity of in vivo models challenges the monitoring of an individual cell fate, in some cases making it impossible. However, the set of factors affecting cells in vitro culture systems differ significantly from in vivo conditions, insufficiently reproducing living systems.
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