Potential Co-prevalence of Plasmid-Mediated Quinolone Resistance Determinant qepA and 16S rRNA Methylase rmtB among E.coli Clinical Isolates from Alexandria- Egypt.

Background: Fluoroquinolone-resistant Gram-negative pathogens have been increasingly reported from most regions of the world over the last decade. A new plasmid-mediated fluoroquinolone efflux pump gene (qepA) is known to be associated with the 16S rRNA methylase gene (rmtB) that confers resistance to aminoglycosides.

Aim: To investigate the potential co-prevalence of qepA and rmtB genes in Escherichia coli (E.

Hepatitis C virus core protein triggers hepatic angiogenesis by a mechanism including multiple pathways.

Chronic hepatitis C virus (HCV) infection is associated with the production of serum cytokines, including transforming growth factor (TGF)-beta2. Despite the occurrence of hepatic angiogenesis in liver conditions, the role of HCV proteins in this context is currently unknown. We demonstrated that the development of hepatic neoangiogenesis in patients infected with HCV is associated with the expression of TGF-beta2 and vascular endothelial growth factor (VEGF) and with activation of endothelial cells, as evidenced by CD34 expression.

Induction of high-molecular-weight (HMW) tumor necrosis factor(TNF) alpha by hepatitis C virus (HCV) non-structural protein 3 (NS3) in liver cells is AP-1 and NF-kappaB-dependent activation.

Chronic infection of hepatitis C virus (HCV)-infected patients is associated with the production of serum and interhepatic inflammatory cytokines including tumor necrosis factor alpha (TNF-alpha). In this study, we delineated part of the mechanism whereby HCV induces the synthesis of TNF-alpha in human liver cell lines HepG2 and Huh7. HepG2 transiently transfected with the full-length HCV cDNA expressed high-molecular-weight (HMW) TNF-alpha mRNAs, which were absent in the control cells.

Activation of c-Jun NH2-terminal kinase (JNK) signaling pathway is essential for the stimulation of hepatitis C virus (HCV) non-structural protein 3 (NS3)-mediated cell growth.

Hepatitis C virus (HCV) non-structural protein 3 (NS3) has been shown to affect cellular functions and is thought to contribute to the development of HCV-related hepatocarcinogenesis. In this study, we delineated part of the mechanisms whereby NS3 protein stimulates cell growth in liver (HepG2) and non-liver (HeLa) cells. The expression of NS3 protein enhanced cell growth, c-jun NH(2)-terminal kinase (JNK) activation, DNA binding activities of the transcription factors AP-1 and ATF-2, and c-jun expression, but not the activation of extracellular signal-regulated kinase (ERK) or p38(MAPK).

Activation of RB/E2F signaling pathway is required for the modulation of hepatitis C virus core protein-induced cell growth in liver and non-liver cells.

Hepatitis C virus (HCV) core protein is a multifunctional protein that affects transcription and cell growth in vitro and in vivo. Here, we confirm the proliferative activities of core protein in liver and non-liver cells and delineate part of the mechanism whereby core protein promotes cell growth. We show that core protein suppresses the expression of tumor suppressor protein p53 and cyclin-dependent kinase (CDK) inhibitor p21 and enhances the activation of cyclin-dependent kinase 2 (CDK2), the phosphorylation of retinoblastoma (Rb), the activation of the transcription factor E2F-1, and the expression of E2F-1 and S phase kinase-interacting protein 2 (SKP2) genes.