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At least 181 records · Page 10Linked to original sources
PubMed1951

AMMIVIN.

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Ammi↗
PubMed2004

Real time PCR for monitoring regulation of host gene expression in herpes simplex virus type 1-infected human diploid cells.

Herpes simplex virus type 1 (HSV-1) induces prominent shifts in the rates of transcription of host cellular genes of relevance for the outcome of the viral infection. The quantitative analysis of transcription may be obscured by virus-induced alterations in the levels of RNA encoded by cellular housekeeping genes that are used commonly for normalisation of real time reverse transcription PCR (RT-qPCR). In the present study, we analysed beta-actin, GAPDH and 18S rRNA for their usefulness in normalisation of RT-qPCR analysis of the transcription of the HSV-1 gamma gB-1 gene and FUT5, a cellular gene induced by viral infection. The transcription of these genes was monitored in a TaqMan-based real time RT-PCR system over a 24h interval of virus infection of human embryonic lung fibroblasts. The levels of gB-1 and FUT5 RNA were normalised via difference in the threshold cycle (deltaC(t)) values relative to each and one of the housekeeping genes or calculated in relation to the number of infected cells without any further normalisation. The levels of RNA encoded by beta-actin or GAPDH were found to vary by several orders of magnitude during HSV-1 infection, introducing large errors in the estimation of the gB-1 and FUT5 RNA levels. In contrast, the variation of C(t) values for 18S rRNA was less than one cycle during 24h period of HSV-1 infection. The FUT5 and gB-1 RNA figures obtained by DeltaC(t) normalisation relative 18S rRNA were identical to those calculated in relation to the number of infected cells. These data recommend 18S rRNA for normalisation in HSV-1-infected human cells but discourage the use of beta-actin and GAPDH RNA for this purpose. By applying these procedures, it was shown that the transcription of FUT5 was increased by 50-fold 5-24h after HSV-1 infection and 200-fold by the inhibition of viral DNA replication in HSV-infected cells.

Actins↗
PubMed1997

Cellular and mitochondrial toxicity of zidovudine (AZT), didanosine (ddI) and zalcitabine (ddC) on cultured human muscle cells.

Zidovudine (AZT), didanosine (ddI) and zalcitabine (ddC) are the reference antiretroviral therapy in patients with AIDS. A toxic mitochondrial myopathy can be observed in patients treated with AZT, but not with ddI and ddC. All 3 compounds can inhibit mitochondrial (mt)DNA polymerase and cause termination of synthesis of growing mtDNA strands and mtDNA depletion. The propensity to injure particular target tissues is unexplained. In our work, cultured muscle cells prepared from human muscle biopsies, were exposed to various concentrations of AZT (4-5000 micromol/l), ddI (5-1000 micromol/l) and ddC (1-1000 micromol/l) for 10 days. We evaluated cell proliferation and differentiation and measured lipid droplet accumulation, lactate production and respiratory chain enzyme activities. All 3 compounds induced a dose-related decrease of cell proliferation and differentiation. AZT seemed to be the most potent inhibitor of cell proliferation. AZT, ddI and ddC induced cytoplasmic lipid droplet accumulations, increased lactate production and decreased activities of COX (complex IV) and SDH (part of complex II). NADHR (complex I) and citrate sinthase activities were unchanged. Zalcitabine (ddC) and, to a lesser extent, ddI, were the most potent inhibitors of mitochondrial function. In conclusion, AZT, ddI and ddC all exert cytotoxic effects on human muscle cells and induce functional alterations of mitochondria possibly due to mechanisms other than the sole mtDNA depletion. Our results provide only a partial explanation of the fact that AZT, but not ddI and ddC, can induce a myopathy in HIV-infected patients. AZT myopathy might not simply result from a direct mitochondrial toxic effect of crude AZT.

Anti-HIV Agents↗
PubMed2002

Cloning and sequencing of nineteen transcript isoforms of the human alpha2,3-sialyltransferase gene, ST3Gal III; its genomic organisation and expression in human tissues.

The recruitment of human peripheral blood leukocytes (PBL) to sites of infection and inflammation requires the surface expression of Sialyl Lewis x glycoconjugates (SLe(x)) on white blood cells and their interaction with E- and P-selectins on activated endothelial cells. E-selectin has additionally been shown to interact with the sialyl Lewis a (SLe(a)) epitope. Human ST3Gal III codes for an alpha2,3-sialyltransferase involved in the biosynthesis of both SLe(a) and SLe(x) epitopes, although the latter with a lower efficiency. We have cloned and sequenced human ST3Gal III gene transcripts from human peripheral blood leukocytes, covering the coding region of this gene. Within our clones we isolated 19 different transcripts with a wide variety of deletions from 45 to 896 nucleotides, and insertions of 26 to 173 nucleotides. Among the insertions we identified two new exons (E3, E6). In order to map and characterise the ST3Gal III gene we used the GenBank database and "computer-cloned" and characterised the genomic organisation of the ST3Gal III gene. The coding sequences of the ST3Gal III gene stretch over a gene sequence of approximately 223 Kb comprised of 15 exons. RT-PCR and laser-induced fluorescent capillary electrophoresis (LIF-CE) were used to examine the expression of this gene in twenty-one human tissues, which showed a highly specific tissue expression pattern. Neural and muscular tissues showed the most complex patterns and were distinctly different from all other tissues examined.

Alternative Splicing↗
PubMed2004

Identification of seven new alpha2,3-sialyltransferase III, ST3Gal III, transcripts from human foetal brain.

We have recently cloned and sequenced 19 human ST3Gal III gene isotranscripts from peripheral blood leukocytes and identified very complex patterns of isotranscripts of this gene in neuronal tissues. We have now cloned and sequenced additionally seven new isotranscripts from foetal brain. These novel isotranscripts showed losses of complete exons along the whole length of the coding sequence. None of the new isotranscripts coded for proteins with the two (L- and S-) sialylmotifs intact. One of the isotranscripts belonged to the isoform ST3Gal III -B, five to the ST3Gal III -C isoform and one to ST3Gal III -D isoform of isotranscripts, which lacks exon 3, exons 3 and 4 and exon 4 respectively. Two of the C series isotranscripts, ST3Gal III C4 and C11 had both lost exons 12 and 13 containing the S-motif but had otherwise the L- and the VS-motifs intact. Three isotranscripts, ST3Gal III C5, C12 and D5, were similar in the 3'-end coding for an identical amino acid sequence unrelated to the original enzyme. Isotranscripts ST3Gal III C9 and B10 were distinctly different from all other forms identified so far. The splice variants reported here are unlikely to express enzymatic activities but may other biological functions.

Alternative Splicing↗