Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0019163 (hepatitis B)
 38,309 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The hepatitis B virus X protein induces transcriptional activation of a wide variety of viral and cellular genes. In addition to its ability to interact directly with many nuclear transcription factors, several reports indicate that the X protein stimulates different cytoplasmic kinase signal cascades. Using the yeast two-hybrid screen, we have isolated a clone designated X-associated protein 3 (XAP3) that encodes a human homolog of the rat protein kinase C-binding protein. One of the activation domains of X (amino acids 90-122) is required for binding to XAP3, while the NH2-terminal part of XAP3 is necessary for binding to X. Both X and XAP3 bound specifically to the eta PKC isoenzyme synthesized in rabbit reticulocyte lysates. Overexpression of XAP3 enhanced X transactivation activity. These results support earlier findings that one of the mechanisms of transactivation by X is through involvement with the cellular protein kinase C pathway.
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PMID:The hepatitis B virus X-associated protein, XAP3, is a protein kinase C-binding protein. 919 57

The ability of the hepatitis B virus (HBV)-encoded X protein (HBx) to coactivate transcription of viral and cellular genes has been implicated in the development of HBV-related liver cancer. To dissect the transformation and the transcription activation properties of HBx, we generated REV2 cell lines expressing the wild-type and different truncated versions of the protein. Full-length HBx-expressing REV-2 cells display an altered morphology and form large colonies in soft agar. A similar transformation efficiency has been obtained with a truncated version of HBx, which contains only the first 50 NH2-terminal amino acids (HBx 1-50). In contrast, HBx mutants that lack the NH2-terminal segment but retain most of the transactivating function, as compared to the full length HBx, were unable to alter the growth characteristic of REV-2 cells. Furthermore, abrogation of full-length HBx transcriptional activation by the insertion of two amino acids (Arg-Pro) at position 68 did not affect REV-2 cells transformation. These results demonstrate that the transactivation activity of HBx is neither essential nor sufficient for tumor promotion.
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PMID:Hepatitis B virus X protein transcription activation domains are neither required nor sufficient for cell transformation. 972 62

Agmatinase, which hydrolyzes agmatine to putrescine and urea, not only represents a potentially important mechanism for regulating the biological effects of agmatine in mammalian cells but also represents an alternative to ornithine decarboxylase for polyamine biosynthesis. We have isolated a full-length cDNA encoding human agmatinase whose function was confirmed by complementation in yeast. The single-copy human agmatinase gene located on chromosome 1 encodes a 352-residue protein with a putative mitochondrial targeting sequence at the NH(3)-terminus. Human agmatinase has about 30% identity to bacterial agmatinases and <20% identity to mammalian arginases. Residues required for binding of Mn(2+) at the active site in bacterial agmatinase and other members of the arginase superfamily are fully conserved in human agmatinase. Agmatinase mRNA is most abundant in human liver and kidney but also is expressed in several other tissues, including skeletal muscle and brain. Its expression in human liver is induced during hepatitis B virus infection, suggesting that agmatinase may play a role in the pathophysiology of this disease.
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PMID:Cloning of human agmatinase. An alternate path for polyamine synthesis induced in liver by hepatitis B virus. 1180 60

The preS1 surface protein of the hepatitis B virus (HBV) is a key factor involved in initial viral entry into hepatocytes. It has been long postulated that an anti-HBV effect should be achievable using peptide fragments of the preS1. Recent reports demonstrated that several preS1-derived lipo-peptides in genotype D HBV exhibit nano to picomolar inhibitory activity against HBV infection. In this study, an acylated analog of a preS1 fragment, a 21-residue lipo-peptide (named 7524 BVS7) with a sequence of palmitoyl-GMGTNLSVPNPLGFFPDHQLDC-NH2, from genotype C HBV was produced base upon a previous structural study and was shown potently inhibits HBV infection with an IC(50) of approximately 20 nM.
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PMID:An anti-viral peptide derived from the preS1 surface protein of hepatitis B virus. 1882 87

A new method of electrochemical probe has been proposed for the determination of Herring Sperm DNA (DNA) based on its interaction with Basic Brown G (BBG). The electrochemical behavior of interaction of BBG with DNA was investigated on Hg electrode. In 0.1molL(-1) NH(3)-NH(4)Cl buffer solution (pH 8.0), BBG can be reduced on Hg electrode with a well-defined voltammetric peak at -0.67V (versus SCE). In the presence of DNA, the reduction peak current of BBG decreases and the peak potential shifts to a more positive potential without the appearance of new peak. The study shows that a new BBG-DNA complex is formed by linear sweep voltammetry (LSV) and spectrophotometry. The decrease of the second order derivative of reductive peak current (Delta i(")(p)) of BBG is proportional to the concentration of DNA in the range of 0.10-36microg mL(-1). Limit of detection of DNA is 0.04microg mL(-1). DNA of Hepatitis B Virus in serum samples was determined satisfactorily. Additionally, the binding mechanism was preliminarily discussed. The mode of interaction between BBG and DNA was found to be intercalation binding.
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PMID:Electrochemical studies of the interaction of Basic Brown G with DNA and determination of DNA. 1907 Dec 77

Hepatocellular carcinoma (HCC) is one of the most prevalent and lethal cancers worldwide. The main HCC-associated diseases are chronic infections with hepatitis B virus (HBV) and hepatitis C virus (HCV), and HBV-associated HCC is still prevalent in Asia. Many studies have suggested that HBV X protein (HBX), which is the most common ORF integrated into the host genome, plays a crucial role in hepatocarcinogenesis. However, the accumulated evidence regarding HBX-mediated signaling pathways is not concordant, and it is difficult to understand the mechanistic nature of HBX-associated hepatocarcinogenesis. For example, HBX was reported to inactivate the early responses to DNA damage via p53-dependent and -independent pathways by interacting with several DNA damage-binding proteins and was also reported to sensitize cells to p53-mediated apoptosis via ataxia-telangiectasia and Rad3-related (ATR)-dependent signaling. HBX also interferes with the centrosome replication process, resulting in rearrangement of chromosomes with micronuclei. Moreover, HBX was found to sensitize protein kinases such as Ras/Raf/mitogen-activated protein kinase (MAPK), extracellular signal-regulated kinase (ERK), stress-activated protein kinase/NH2-terminal-Jun kinase (SAPK/JNK), protein kinase B (PKB/Akt), and Janus kinase/STAT (JAK/STAT), indicating that a variety of signaling pathways may be activated by HBX. In this review, we focus on the roles of HBX in DNA damage repair during HCC development, with a view to achieving a better understanding of the significance of HBX in the early steps of hepatocarcinogenesis.
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PMID:Impact of hepatitis B virus X protein on the DNA damage response during hepatocarcinogenesis. 1978 39

A novel fluorescent resonant energy transfer (FRET) biosensor was fabricated for the detection of hepatitis B virus (HBV) DNA using poly(ethylenimine) (PEI) modified upconversion nanoparticles (NH2-UCNPs) as energy donor and gold nanoparticles (Au NPs) as acceptor. The PEI modified upconversion nanoparticles were prepared directly with a simple one-pot hydrothermal method, which provides high quality amino-group functionalized UCNPs with uniform morphology and strong upconversion luminescence. Two single-stranded DNA strands, which were partially complementary to each other, were then conjugated with NH2-UCNPs and Au NPs. When DNA conjugated NH2-UCNPs and Au NPs are mixed together, the hybridization between complementary DNA sequences on UCNPs and Au NPs will lead to the quenching of the upconversion luminescence due to the FRET process. Meanwhile, upon the addition of target DNA, Au NPs will leave the surface of the UCNPs and the upconversion luminescence can be restored because of the formation of the more stable double-stranded DNA on the UCNPs. The sensor we fabricated here for target DNA detection shows good sensitivity and high selectivity, which has the potential for clinical applications in the analysis of HBV and other DNA sequences.
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PMID:An upconversion fluorescent resonant energy transfer biosensor for hepatitis B virus (HBV) DNA hybridization detection. 2642 23

Nitrogen (N) and sulfur (S) codoped reduced graphene oxide (N,S-rGO) was synthesized through a facile solvothermal process. The introduction of N and S heteroatoms into GO effectively activated the sp(2)-hybridized carbon lattice and made the material an ideal electron/energy acceptor. Such unique properties enable this material to perform as a general platform for rapid and sensitive detection of various biological species through simple fluorescence quenching and recovering. When quantum dot (QD)-labeled HBV (human being disease-related gene hepatitis B virus DNA) and HIV (human being disease-related gene human immunodeficiency virus DNA) molecular beacon probes were mixed with N,S-rGO, QD fluorescence was quenched; when target HBV and HIV DNA were added, QD fluorescence was recovered. By the recovered fluorescence intensity, the target virus DNA detection limits were reduced to 2.4 nM for HBV and 3.0 nM for HIV with detection time of less than 5 min. It must be stressed out that different viruses in the same homogeneous aqueous media could be discriminated and quantified simultaneously through choosing diverse QD probes with different colors. Moreover, even one mismatched target DNA could be distinguished using this method. When altering the molecular beacon loop domain to protein aptamers, this sensing strategy was also able to detect thrombin and IgE in 5 min with detection limits of 0.17 ng mL(-1) and 0.19 ng mL(-1), respectively, which was far more rapid and sensitive than bare GO-based fluorescence detection strategy.
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PMID:Nitrogen and Sulfur Codoped Reduced Graphene Oxide as a General Platform for Rapid and Sensitive Fluorescent Detection of Biological Species. 2708 22

Autophagy is closely associated with the regulation of hepatitis B virus (HBV) replication. HBV X protein (HBx), a multifunctional regulator in HBV-associated biological processes, has been demonstrated to be crucial for autophagy induction by HBV. However, the molecular mechanisms of autophagy induction by HBx, especially the signaling pathways involved, remain elusive. In the present investigation, we demonstrated that HBx induced autophagosome formation independently of the class I phosphatidylinositol 3-kinase (PI3K)/AKT/mTOR signaling pathway. In contrast, the class III PI3K(VPS34)/beclin-1 pathway was revealed to be critical for HBx-induced autophagosome formation. Further study showed that HBx did not affect the level of VPS34 and beclin-1 expression but inhibited beclin-1/Bcl-2 association, and c-Jun NH2-terminal kinase (JNK) signaling was found to be important for this process. Moreover, it was found that HBx treatment led to the generation of reactive oxygen species (ROS), and inhibition of ROS activity abrogated both JNK activation and autophagosome formation. Of importance, ROS-JNK signaling was also revealed to play an important role in HBV-induced autophagosome formation and subsequent HBV replication. These data may provide deeper insight into the mechanisms of autophagy induction by HBx and help in the design of new therapeutic strategies against HBV infection.IMPORTANCE HBx plays a key role in diverse HBV-associated biological processes, including autophagy induction. However, the molecular mechanisms of autophagy induction by HBx, especially the signaling pathways involved, remain elusive. In the present investigation, we found that HBx induced autophagy independently of the class I PI3K/AKT/mTOR signaling pathway, while the class III PI3K(VPS34)/beclin-1 pathway was revealed to be crucial for this process. Further data showed that ROS-JNK activation by HBx resulted in the release of beclin-1 from its association with Bcl-2 to form a complex with VPS34, thus enhancing autophagosome formation. Of importance, ROS-JNK signaling was also demonstrated to be critical for HBV replication via regulation of autophagy induction. These data help to elucidate the molecular mechanisms of autophagy induction by HBx/HBV and might be useful for designing novel therapeutic approaches to HBV infection.
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PMID:Reactive Oxygen Species-Mediated c-Jun NH2-Terminal Kinase Activation Contributes to Hepatitis B Virus X Protein-Induced Autophagy via Regulation of the Beclin-1/Bcl-2 Interaction. 2851 4

A sensitive label-free electrochemical immunosensor was designed using a novel signal amplification system for quantitative detecting hepatitis B surface antigen (HBsAg). Nitrogen-doped graphene quantum dots (N-GQDs) supported surfactant-free AuPdCu ternary nanoparticles (AuPdCu/N-GQDs), which featured with good conductivity and excellent catalytic properties for the reduction of hydrogen peroxide (H2O2), was synthesized by a simple and benign hydrothermal procedure. At the same time, the electroactive polymer nanospheres (PS) was synthesized by infinite coordination polymers of ferrocenedicarboxylic acid, which could play as carrier and electronic mediator to load AuPdCu/N-GQDs. The PS not only improved the ability to load antibodies because of the good biocompatibility, but also accelerated electron transport of the electrode interface attribute to plentiful ferrocene unit. Thus, the prepared AuPdCu/N-GQDs@PS has abilities of good biocompatibility, catalytic activity and electrical conductivity to be applied as transducing materials to amplify electrochemical signal in detection of HBsAg. Under optimal conditions, the fabricated immunosensor exhibited high sensitivity and stability in the detection of HBsAg. A linear relationship between current signals and the concentrations of HBsAg was obtained in the range from 10fg/mL to 50ng/mL and the detection limit of HBsAg was 3.3fg/mL (signal-to-noise ratio of 3). Moreover, the designed immunosensor with excellent selectivity, reproducibility and stability shows excellent performance in detection of human serum samples. Furthermore, this label-free electrochemical immunosensor has promising application in clinical diagnosis of HBsAg.
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PMID:A label-free electrochemical immunosensor based on the novel signal amplification system of AuPdCu ternary nanoparticles functionalized polymer nanospheres. 2929 95


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