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herpes simplex/phosphatase

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Stranica 1 iz 164 rezultatima

A conserved domain of herpes simplex virus ICP34.5 regulates protein phosphatase complex in mammalian cells.

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ICP34.5, encoded by herpes simplex virus 1, is a protein phosphatase 1 (PP1) regulatory subunit that mediates dephosphorylation of the alpha subunit of translation initiation factor 2 (eIF2alpha). However, the mechanism of its action remains poorly understood. Here, we show that amino acid
Plasma membrane extracts from Herpes simplex virus type 1 transformed hamster embryo fibroblasts were chromatographed on Lens culinaris lectin coupled to Sepharose (LcH-Sepharose) and analysed by dodecyl sulphate polyacrylamide gel electrophoresis. Coomassie blue-staining revealed two major protein
Enhanced afferent excitability is considered to be an important pathophysiological basis of interstitial cystitis/bladder pain syndrome (IC/BPS). In addition, transient receptor potential vanilloid-1 (TRPV1) receptors are known to be involved in afferent sensitization. Animals with hydrogen peroxide
The ICP34.5 protein facilitates herpes simplex virus replication by binding and activating protein phosphatase 1 (PP1) by means of a very conserved C-terminal GADD34-like region. Natural variants of the ICP34.5 differing in the number of arginines in an Arg-rich cluster at the N terminus and the

Reversible decrease of fluoride resistant acid phosphatase-positive neurons after herpes simplex virus infection.

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Herpes simplex virus (HSV) frequently infects human sensory ganglion neurons, and similar infections have been reported in experimental animals. Reported here is an investigation of in vivo neuronal function after HSV infection. It was observed that the proportion of fluoride resistant acid
Earlier studies have shown that ICP22 and the U(L)13 protein kinase but not the U(S)3 kinase are required for optimal expression of a subset of late (gamma(2)) genes exemplified by U(L)38, U(L)41, and U(S)11. In primate cells, ICP22 mediates the disappearance of inactive isoforms of cdc2 and
We studied the effect of herpes simplex virus (HSV) vectors-based gene transfer of protein phosphatase 1α (PP1α) on bladder hypersensitivity in rats.Using adult female Sprague-Dawley rats, non-replicating HSV vectors carrying PP1α or green fluorescent

Role of cellular phosphatase cdc25C in herpes simplex virus 1 replication.

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Earlier studies have shown that in herpes simplex virus 1-infected cells, ICP22 upregulates the accumulation of a subset of gamma(2) proteins exemplified by the products of the U(L)38, U(L)41, and U(S)11 genes. The ICP22-dependent process involves degradation of cyclins A and B1, the stabilization

The inactivation of herpes simplex virus by phosphatase enzymes.

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Tissue phosphatases which are present in virus suspensions were found to contribute in considerable measure to the inactivation of herpes simplex virus. Phosphatase inhibitors and phosphatase substrates have been found to prolong the survival of the virus. Exogenous phosphatases, both acid and
Treatment of VERO cells with 2,4,6-triamino-pyridimyl-5-azobenzene (10 gamma/ml) one hour after inoculation of herpes simplex virus type 1 limits the influence of the virus infection, consisting in the enchancement of the activities of alkaline phosphatase, acid phosphatase and LDH (especially of
The carboxyl-terminal domain of the gamma134.5 protein of the herpes simplex virus 1 binds to protein phosphatase 1alpha (PP1) and is required to prevent the shut-off of protein synthesis resulting from phosphorylation of the alpha subunit of eIF-2 by the double-stranded RNA-activated protein
Prostate cancer is one of the most prevalent cancers in men. Replication-competent oncolytic herpes simplex virus (oHSV) vectors are a powerful antitumor therapy that can exert at least two effects: direct cytocidal activity that selectively kills cancer cells and induction of antitumor immunity. In
The ICP34.5 protein of herpes simplex virus type 1 is a neurovirulence factor that plays critical roles in viral replication and anti-host responses. One of its functions is to recruit protein phosphatase 1 (PP1) that leads to the dephosphorylation of the α subunit of translation initiation factor
In human cells infected with herpes simplex virus 1 the double-stranded RNA-dependent protein kinase (PKR) is activated but phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2) and total shutoff of protein synthesis is observed only in cells infected with
Addition of BrdUrd in combination with prednisolone to HSV1-transformed hamster embryo cells induces an alkaline phosphatase (AP). FdURd enhances, dThd reduces the inducing capacity of BrdUrd and prednisolone. Induction is prevented by addition of cycloheximide or of cytosine arabinoside. BrdUrd
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