Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.7.48 (transcriptase)
 9,479 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The association of an RNA-dependent RNA polymerase activity with virions of pike fry rhabdovirus has been demonstrated by both in vitro and in vivo studies. The temperature optimum for the in vitro assay is around 20 C, although enzyme activity can be observed at 4 C. Preparations of pike fry virus possess a glycoprotein, a membrane protein, a nucleoprotein, an L protein, and a phosphoprotein, as well as an RNA of about 3.8 times 10-6 mol wt. A protein kinase activity has been found associated with virus preparations. In vitro RNA product analyses indicate that the virus-associated enzyme functions principally as a transcriptase synthesizing viral-complementary, heteropolymeric RNA.
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PMID:RNA polymerase associated with virions of pike fry rhabdovirus. 116 3

A procedure has been developed for the sequential removal and purification of the glycoprotein and membrane protein of vesicular stomatitis virus (VSV). Neither of these proteins exhibited transcriptase activity. All of the activity was recovered in the ribonucleic acid (RNA)-ribonucleoprotein complex of VSV, which also has four other minor proteins associated with it. During transcription of 41% of the RNA of a virus preparation, no dissociation of the ribonucleoprotein from the viral RNA was observed.
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PMID:Dissociation of vesicular stomatitis virus and relation of the virion proteins to the viral transcriptase. 434 41

Earlier we reported a reduction to 1/30th-1/100th of the original number of infectious particles in the infectious vesicular stomatitis virus (VSV) released from L cells treated with 10 or 30 reference units of interferon per ml. However, in these cultures virus particle production, as measured by VSV particle-associated viral RNA, virus nucleocapsid protein, and viral transcriptase, was inhibited by less than 10%. Data reported in this paper show that there was a significant reduction in glycoprotein and membrane protein of VSV particles released from interferon-treated cells. Evidence supporting the deficiency of glycoprotein in VSV released from interferon-treated cells was derived from electron microscopic studies. Under conditions where glycoprotein spikes or projections were clearly detectable on the surface of VSV released from cells not treated with interferon, very few spikes were observed on VSV released from interferon-treated cells. These results suggested that interferon-treated cells produced VSV particles with low infectivity and that this low infectivity may be related to the reduced amount of glycoprotein and membrane protein incorporated into such particles.
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PMID:Interferon-treated cells release vesicular stomatitis virus particles lacking glycoprotein spikes: correlation with biochemical data. 615 48

Earlier, we reported a 30-200-fold reduction in the yield of infectious vesicular stomatitis virus (VSV) released from L cells treated with 10-30 reference units ml-1 of interferon (IFN); however, in these cultures virus particle production, as measured by VSV particle-associated viral RNA, virus nucleocapsid protein and viral transcriptase, was inhibited less than 10-fold. There was biochemical and morphological evidence of a significant reduction in glycoprotein (G) and membrane protein (M) of VSV particles released from IFN-treated cells. We compare here the effects of tunicamycin (TM) and IFN in L cells. Treatment with TM or IFN reduced the production of infectious VSV particles, decreased the amount of G and M proteins in VSV released from treated cells, and inhibited an early step in the formation of asparagine-linked oligosaccharide chains, the incorporation by membrane preparations from treated cells of N-acetylglucosamine into glycolipids with the properties of dolichol derivatives.
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PMID:Interferon treatment inhibits glycosylation of a viral protein. 615 39

A 200-fold inhibition in the titer of infectious vesicular stomatitis virus (VSV) was produced in cultures of Ly cells treated with 30 reference units of interferon per milliliter. Virus particle production, as measured by VSV particle-associated transcriptase, or nucleocapsid protein was inhibited by a maximum of tenfold. The glycoprotein and membrane protein content was reduced in VSV derived from interferon-treated cells. Thus interferon-treated cells may have produced VSV particles with low infectivity, which may be related to the reduced amount of glycoprotein incorporated into such particles. These findings resemble those reported in interferon-treated cells infected with murine leukemia viruses.
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PMID:Selective inhibition of glycoprotein and membrane protein of vesicular stomatitis virus from interferon-treated cells. 624 16

cDNA species encoding either the long or the short isoforms of the rat thyrotropin-releasing-hormone (TRH) receptor were expressed stably in Rat 1 fibroblasts, and clones expressing specific binding of [3H]TRH were detected and expanded. Clones expressing each of these receptors at levels up to 1 pmol/mg of membrane protein were selected for analysis. Reverse-transcriptase PCR on RNA isolated from these clones confirmed that each clone expressed only mRNA corresponding to the expected splice variant. Both receptor splice variants bound [3H]TRH with a Kd of some 80 nM when binding assays were performed in the presence of guanosine 5'-[beta gamma-imido]-triphosphate. In the presence of TRH, both receptor subtypes were able to cause stimulation of inositol phosphate generation in a pertussis-toxin-insensitive manner with similar EC50 values and to stimulate the mobilization of intracellular Ca2+, but, despite reports that TRH receptors can also interact with the G-proteins Gs and Gi2, neither receptor splice variant was able to modulate adenylate cyclase activity in either a positive or a negative manner. These data indicate that the long and short isoforms of the rat TRH receptor have similar affinities for TRH and display similar abilities to interact with the Gq-like G-proteins, but show no ability to regulate adenylate cyclase, at least when expressed in this genetic background.
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PMID:Comparison of the signalling properties of the long and short isoforms of the rat thyrotropin-releasing-hormone receptor following expression in rat 1 fibroblasts. 764 58

Epstein-Barr virus (EBV) is frequently found in Hodgkin and Reed-Sternberg cells in Hodgkin's disease. Epstein-Barr virus has transforming properties in vitro and might be involved in the pathogenesis of certain types of Hodgkin's disease. One of the possible mechanisms is the upregulation of the human proto-oncogene bcl-2 by the latent membrane protein 1 of EBV in vitro. Another possibility might be the expression of the viral 'bcl-2 homologue' BHRF-1. In the present study of 64 cases of Hodgkin's disease we investigated the expression of bcl-2 at the protein level in relation to the presence of EBV. Moreover, in 10 EBV positive cases we investigated, the expression of the bcl-2 homologue, BHRF-1, by reverse-transcriptase PCR. bcl-2 was detected in 14 of 22 (64%) EBV positive and in 37 of 42 (88%) EBV negative cases. In 17 of 22 (77%) EBV positive cases Reed-Sternberg cells were negative (n = 8) or expressed the bcl-2 protein in a very low percentage ( < 5%) of cells (n = 9), whereas in 20 of 42 (43%) of the EBV negative cases the majority ( > 50%) of the neoplastic cells were bcl-2 positive. Using the reverse-transcriptase PCR with primers amplifying transcripts of BHRF-1 we were able to detect BHRF-1 transcripts in only one of the 10 tested cases of EBV positive Hodgkin's disease. Our data indicate that in EBV positive Hodgkin's disease growth advantage of Reed-Sternberg cells is not obtained by upregulation of bcl-2 or by the EBV homologue BHRF-1.
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PMID:Expression of bcl-2 protein and transcription of the Epstein-Barr virus bcl-2 homologue BHRF-1 in Hodgkin's disease: implications for different pathogenic mechanisms. 884 76

Recent evidence suggests that a number of non-phagocytic cell types may contain a superoxide generating NADPH oxidase. Studies to data on cultured human fibroblasts have primarily concerned the identification of cytochrome b558, whilst expression of other NADPH oxidase components have not been addressed. In this study we have investigated the expression of NADPH oxidase with particular reference to the cytosolic factors p47-phox and p67-phox. Reverse transcriptase-polymerase chain reaction (RT-PCR) showed that human fibroblasts express mRNA for p47-phox, p67-phox and p22-phox. Expression of the gp91-phox transcript was not detected, indicating that human fibroblasts may possess an NADPH oxidase isoenzyme. Western blot analysis of human fibroblast cytosol, using an anti-p47-phox antibody (JW-1), identified a 47 kDa protein. Cell-free reconstitution assays showed that fibroblast cytosol could initiate superoxide generation when mixed with either human fibroblast membranes (0.16 nmol superoxide/min/microgram membrane protein), or resting human neutrophil membranes (0.20 nmol superoxide/min/microgram membrane protein). These data indicate that the expression of p47-phox and p67-phox by human fibroblasts may contribute to the cells' generation of superoxide.
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PMID:The functional expression of p47-phox and p67-phox may contribute to the generation of superoxide by an NADPH oxidase-like system in human fibroblasts. 798 96

Human interleukin-10 (h-IL-10) is a pleiotropic cytokine with stimulatory activity on B-lymphocytes. Recent evidence indicates that infection with Epstein-Barr virus (EBV) induces h-IL-10 production in B-cells and that this cytokine may contribute to EBV-induced B-cell transformation. It is not known whether h-IL-10 induction by EBV correlates with distinct phenotypic features of the infected cells or with the expression of particular viral genes. We have approached these questions by investigating the expression of h-IL-10 mRNA in a panel of B-cell lines including: in vitro EBV-transformed lymphoblastoid cell lines (LCLs), EBV-carrying Burkitt lymphoma (BL) lines, EBV-negative BL lines and their sublines infected with different EBV strains, or transfected with the transformation-associated viral gene. h-IL-10 mRNA was detected by reverse-transcriptase-assisted (RT)-PCR in a subset of EBV-negative BLs and in all EBV-positive BL lines and LCLs investigated except Daudi. This cell line carries an EBV nuclear antigen (EBNA)-2 gene-defective virus strain. h-IL-10 mRNA was induced by conversion of 3 EBV-negative and h-IL-10-negative BL lines (BL41, BL47 and BL49) with the transforming, B95.8-derived EBV strain. P3HR-I virus convertants that do not express the viral EBNA-2 and the EBV latent membrane protein (LMP)-1, and fail to progress towards a LCL-like cell phenotype, showed no evidence of h-IL-10 up-regulation. Expression of LMP1 was sufficient to induce h-IL-10 mRNA in transfected sublines of the EBV-negative DG75 and BL41 cell lines, whereas expression of EBNA1, 2, 5, or 6 had no effect. h-IL-10 was detected in the culture supernatants of the LMP1 transfectants by specific ELISA assays. The present findings confirm the role of LMP1 in the transactivation of a wide variety of cellular genes which may be involved in EBV-induced B-cell transformation.
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PMID:The Epstein-Barr virus latent membrane protein-1 (LMP1) induces interleukin-10 production in Burkitt lymphoma lines. 815 62

The peritrophic membrane is a semi-permeable chitinous matrix lining the gut of most insects and is thought to have important roles in the maintenance of insect gut structure, facilitation of digestion, and protection from invasion by microrganisms and parasites. Proteins are integral components of this matrix, although the structures and functions of these proteins have not been characterized in any detail. The peritrophic membrane from the larvae of the fly Lucilia cuprina, the primary agent of cutaneous myiasis in sheep, was shown to contain six major integral peritrophic membrane proteins. Two of these proteins, a 44-kDa glycoprotein (peritrophin-44) and a 48-kDa protein (peritrophin-48) together represent >70% of the total mass of the integral peritrophic membrane proteins. Peritrophin-44 was purified and its complete amino acid sequence was determined by cloning and sequencing the DNA complementary to its mRNA. The deduced amino acid sequence codes for a protein of 356 amino acids containing an amino-terminal signal sequence followed by five similar but nonidentical domains, each of approximately 70 amino acids and characterized by a specific register of 6 cysteines. One of these domains was also present in the noncatalytic regions of chitinases from Brugia malayi, Manduca sexta, and Chelonus. Peritrophin-44 has a uniform distribution throughout the larval peritrophic membrane. Reverse transcriptase-polymerase chain reaction detected the expression of peritrophin-44 in all three larval instars but only trace levels in adult L. cuprina. The protein binds specifically to tri-N-acetyl chitotriose and reacetylated chitosan in vitro. It is concluded that the multiple cysteine-rich domains in peritrophin-44 are responsible for binding to chitin, the major constituent of peritrophic membrane. Peritrophin-44 probably has roles in the maintenance of peritrophic membrane structure and in the determination of the porosity of the peritrophic membrane. This report represents the first characterization of an insect peritrophic membrane protein.
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PMID:Characterization of a major peritrophic membrane protein, peritrophin-44, from the larvae of Lucilia cuprina. cDNA and deduced amino acid sequences. 862 36


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