原创力文档calcineurin inhibitor-induced and ras-mediated overexpression of vegf in renal cancer cells involves mtor through the regulation of pras40钙调磷酸酶inhibitor-induced和ras-mediated超表达的vegf在肾癌细胞包括mtor pras40的规定.pdfVIP
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calcineurin inhibitor-induced and ras-mediated overexpression of vegf in renal cancer cells involves mtor through the regulation of pras40钙调磷酸酶inhibitor-induced和ras-mediated超表达的vegf在肾癌细胞包括mtor pras40的规定
Calcineurin Inhibitor-Induced and Ras-Mediated
Overexpression of VEGF in Renal Cancer Cells Involves
mTOR through the Regulation of PRAS40
Aninda Basu1,2, Pallavi Banerjee1,2, Alan G. Contreras1,2, Evelyn Flynn1,2, Soumitro Pal1,2*
1 Division of Nephrology and Transplantation Research Center, Children’s Hospital, Boston, Massachusetts, United States of America, 2 Department of Pediatrics, Harvard
Medical School, Boston, Massachusetts, United States of America
Abstract
Malignancy is a major problem in patients treated with immunosuppressive agents. We have demonstrated that treatment
with calcineurin inhibitors (CNIs) can induce the activation of proto-oncogenic Ras, and may promote a rapid progression of
human renal cancer through the overexpression of vascular endothelial growth factor (VEGF). Interestingly, we found that
CNI-induced VEGF overexpression and cancer cell proliferation was inhibited by rapamycin treatment, indicating potential
involvement of the mammalian target of rapamycin (mTOR) pathway in this tumorigenic process. Here, we examined the
role of mTOR pathway in mediating CNI- and Ras-induced overexpression of VEGF in human renal cancer cells (786-0 and
Caki-1). We found that the knockdown of raptor (using siRNA) significantly decreased CNI-induced VEGF promoter activity
as observed by promoter-luciferase assay, suggesting the role of mTOR complex1 (mTORC1) in CNI-induced VEGF
transcription. It is known that mTOR becomes activated following phosphorylation of its negative regulator PRAS40, which
is a part of mTORC1. We observed that CNI treatment and activation of H-Ras (through transfection of an active H-Ras
plasmid) markedly increased the phosphorylation of PRAS40, and the transfection of cells using a dominant-negative
plasmid of Ras, significantly decreased PRAS40 phosphorylation. Prot
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