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Article citations


Du, Z.-X., Wang, H.Q., Zhang, H.Y. and Gao, D.X. (2007) Involvement of glyceraldehyde-3-phosphate de- hydrogenase in tumor necrosis factor-related apoptosis- inducing ligand-mediated death of thyroid cancer cells. Journal of endocrinology, 148, 4352. doi:10.1210/en.2006-1511

has been cited by the following article:

  • TITLE: Study of glyceraldehyde-3-phosphate dehydrogenase expression in the tumor process of: Breast, cervix and prostate cancers

    AUTHORS: Bouchra Elkhalfi, Nezha Senhaji, Hakima Benomar, Abdelaziz Soukri

    KEYWORDS: Cancer; GAPDH; Immunohistochemistry; Expression; Isoforms

    JOURNAL NAME: Advances in Biological Chemistry, Vol.2 No.4, November 21, 2012

    ABSTRACT: W Tumor proliferation of cancer cells requires a high intake of oxygen by angiogenesis. Deep cancer cells suffer from asphyxia and meet their energy needs through the enzymes of glycolysis. The anti-angio- genesis approach has been recognized for therapeutic purposes, but the deep cancers, difficult to reach by this therapy, could be targeted by inhibiting an enzyme of the glycolytic cycle. Our work focused on the study of the expression of GAPDH, a key enzyme of glycolysis, in cervix, breast and prostate tumors, for two approaches: Fundamental and targeted therapeutics. 60 samples, taken at the Anatomopathology laboratory of the Pasteur Institute of Morocco, were examined histologically and immunohistochemically, demonstrating the expression and cellular localization of GAPDH. The three organs have shown an overex-pression of GAPDH in tumor tissues. At the cellular level, the localization of GAPDH in cancer tissue is diffuse but mostly nuclear whereas it remains focused at the membrane and/or the cytoplasm in benign tumor tissues. From these results we could assume that GAPDH is involved in the cancer process and draws attention to a possible new nuclear role that could be either specific to one form or different isoforms of GAPDH enzyme.