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Our work has identified a cancer-specific, cell surface and growth-related quinol oxidase with both NADH oxidase and protein
disulfide-thiol interchange activities, a member of the ECTO-NOX protein family designated tNOX. We provide evidence for tNOX
as an alternative drug target to COX-2 to explain the anticancer activity of COX inhibitors. Non-steroidal anti-inflammatory
drugs (NSAIDS), piroxicam, aspirin, ibuprofen, naproxen and celecoxib all specifically inhibited tNOX activity of HeLa (human
cervical carcinoma) and BT-20 (human mammary carcinoma) cells (IC50 in the nanomolar range) without effect on ECTO-NOX activities of non-cancer MCF-10A mammary epithelial cells. With cancer
cells, rofecoxib was less effective and two NSAIDS selective for COX-1 were without effect in inhibiting NOX activity. The
IC50 for inhibition of tNOX activity of HeLa cells and the IC50 for inhibition of growth of HeLa cells in culture were closely correlated. The findings provide evidence for a new drug target
to account for anticancer effects of NSAIDS that occur independent of COX-2. 相似文献
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Burri L Vascotto K Fredersdorf S Tiedt R Hall MN Lithgow T 《The Journal of biological chemistry》2004,279(48):50243-50249
Translocation of precursor proteins across the mitochondrial membranes requires the coordinated action of multisubunit translocases in the outer and inner membrane, and the driving force for translocation across the inner membrane is provided by the matrix-located heat shock protein 70 (mtHsp70). The central components of the protein import machinery are essential. Here we describe Zim17, an essential protein with a zinc finger motif involved in protein import into mitochondria. Comparative genomics suggested a correction to the open reading frame of YNL310c, the gene encoding Zim17 in Saccharomyces cerevisiae. The revised open reading frame codes for a classic mitochondrial targeting signal, which is processed from Zim17 in the mitochondrial matrix. Loss of Zim17 selectively diminishes import of proteins into the matrix of mitochondria, but this loss of Zim17 is partially suppressed by overexpression of the J-protein Pam18/Tim14. We propose that Zim17 functions as an example of a "fractured" J-protein, where a protein like Zim17 contributes a zinc finger domain to Type III J-proteins, in toto providing for substrate loading onto Hsp70. 相似文献
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Histone acetyltransferase activity of p300 is required for transcriptional repression by the promyelocytic leukemia zinc finger protein 下载免费PDF全文
Guidez F Howell L Isalan M Cebrat M Alani RM Ivins S Hormaeche I McConnell MJ Pierce S Cole PA Licht J Zelent A 《Molecular and cellular biology》2005,25(13):5552-5566
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