VISNA VIRUS INDUCED FUSION OF NERVE CELLS IN VITRO

1978 ◽  
Vol 37 (5) ◽  
pp. 628
Author(s):  
E. Hooghe-Peters ◽  
M. Dubois-Dalcq ◽  
D. Schmechel
Keyword(s):  
Nerve Cells ◽  
Visna Virus

scholarly journals Anticancer activity of midostaurin in hormone refractory human prostate cancer DU145 cells

2016 ◽  
Vol 11 (2) ◽  
pp. 378
Author(s):  
Jin-Jun Sun ◽  
Shi-Feng Kan ◽  
Guan-Xing Sun
Keyword(s):  
Prostate Cancer ◽  
Kinase Inhibitor ◽  
Cancer Cell Line ◽  
Prostate Cancer Cell Line ◽  
Nerve Cells ◽  
Human Prostate ◽  
Human Prostate Cancer ◽  
Du145 Cells ◽  
Hormone Refractory

<p class="Abstract">We tried a new method of prostate cancer treatment by inducing<em> in vitro</em> differentiation which resulted in reduction of cancer cells growth. A protein kinase inhibitor, midostaurin's ability to trigger the human prostate cancer cell line, DU145 to segregate into nerve cells was studied. Midostaurin (100 nM) suppressed the growth of DU145 cells but without change in the number of dead cells. Midostaurin started to extend neurites on DU145 cells after 24 hours and differentiated into nerve cells by 72 hours. The microtubule was stabilized by tau protein and its mRNA expression showed time-dependent increase in midostaurin-treated DU145 cells. At the same time, the amount of acetylcholinesterase was also increased. The midostaurin-treated DU145 cells showed 40% less activity than control in the colony forming assay. The results suggests that midostaurin can induce differentiation of DU145 cells into nerve cells.</p><p> </p>

scholarly journals Implication of caspases during maedi–visna virus-induced apoptosis

2002 ◽  
Vol 83 (12) ◽  
pp. 3153-3161 ◽  
Author(s):  
R. Duval ◽  
V. Bellet ◽  
S. Delebassée ◽  
C. Bosgiraud
Keyword(s):  
Cell Death ◽  
Caspase 3 ◽  
Specific Cell ◽  
Caspase 9 ◽  
Virus Growth ◽  
Caspase Inhibitors ◽  
Visna Virus ◽  
Maedi Visna Virus ◽  
Cellular Lysis

Maedi–visna virus (MVV) causes encephalitis, pneumonia and arthritis in sheep. In vitro, MVV infection and replication lead to strong cytopathic effects characterized by syncytia formation and subsequent cellular lysis. It was demonstrated previously that MVV infection in vitro induces cell death of sheep choroid plexus cells (SCPC) by a mechanism that can be associated with apoptotic cell death. Here, the relative implication of several caspases during acute infection with MVV is investigated by employing diverse in vitro and in situ strategies. It was demonstrated using specific pairs of caspase substrates and inhibitors that, during in vitro infection of SCPC by MVV, the two major pathways of caspase activation (i.e. intrinsic and extrinsic pathways) were stimulated: significant caspase-9 and -8 activities, as well as caspase-3 activity, were detected. To study the role of caspases during MVV infection in vitro, specific, cell-permeable, caspase inhibitors were used. First, these results showed that both z-DEVD-FMK (a potent inhibitor of caspase-3-like activities) and z-VAD-FMK (a broad spectrum caspase inhibitor) inhibit caspase-9, -8 and -3 activities. Second, both irreversible caspase inhibitors, z-DEVD-FMK and z-VAD-FMK, delayed MVV-induced cellular lysis as well as virus growth. Third, during SCPC in vitro infection by MVV, cells were positively stained with FITC-VAD-FMK, a probe that specifically stains cells containing active caspases. In conclusion, these data suggest that MVV infection in vitro induces SCPC cell death by a mechanism that is strongly dependent on active caspases.

scholarly journals Maedi-visna virus Vif protein uses motifs distinct from HIV-1 Vif to bind zinc and cofactor required for A3 degradation

2020 ◽  
pp. jbc.RA120.015828
Author(s):  
Kirsten M. Knecht ◽  
Yingxia Hu ◽  
Diana Rubene ◽  
Matthew Cook ◽  
Samantha J Ziegler ◽  
...  
Keyword(s):  
Viral Infections ◽  
Zinc Ion ◽  
Binding Motif ◽  
Cytidine Deaminases ◽  
Visna Virus ◽  
Primate Lentiviruses ◽  
Maedi Visna Virus ◽  
Hiv 1

The mammalian apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3 (APOBEC3 or A3) family of cytidine deaminases restrict viral infections by mutating viral DNA and impeding reverse transcription. To overcome this antiviral activity, most lentiviruses express a viral accessory protein called Vif, which recruits A3 proteins to Cullin-RING E3 ubiquitin ligases such as Cul5 for ubiquitylation and subsequent proteasomal degradation. While Vif proteins from primate lentiviruses like HIV-1 utilize the transcription factor CBFβ as a non-canonical cofactor to stabilize the complex, maedi-visna virus (MVV) Vif hijacks cyclophilin A (CypA) instead. Since CBFβ and CypA are both highly conserved among mammals, the requirement for two different cellular cofactors suggests that these two A3-targeting Vif proteins have different biochemical and structural properties. To investigate this topic, we used a combination of in vitro biochemical assays and in vivo A3 degradation assays to study motifs required for MVV Vif to bind zinc ion, Cul5, and the cofactor CypA. Our results demonstrate that while some common motifs between HIV-1 Vif and MVV Vif are involved in recruiting Cul5, different determinants in MVV Vif are required for cofactor binding and stabilization of the E3 ligase complex, such as the zinc-binding motif and N- and C-terminal regions of the protein. Results from this study advance our understanding of the mechanism of MVV Vif recruitment of cellular factors and the evolution of lentiviral Vif proteins.

Radiation and Whole Light Effects on Molluscan Nerve Cells in Vitro

1967 ◽  
Vol 31 (3) ◽  
pp. 452 ◽  
Author(s):  
Makoto Sato ◽  
George Austin ◽  
Hideko Yai
Keyword(s):  
Nerve Cells ◽  
Light Effects

The preservation of nerve cells in rat neostriatal slices maintained in vitro: A morphological study

1980 ◽  
Vol 197 (2) ◽  
pp. 341-353 ◽  
Author(s):  
Il Jin Bak ◽  
Ulrich Misgeld ◽  
Molly Weiler ◽  
Ellen Morgan
Keyword(s):  
Morphological Study ◽  
Nerve Cells ◽  
Neostriatal Slices

scholarly journals Targeting of the Visna Virus Tat Protein to AP-1 Sites: Interactions with the bZIP Domains of Fos and Jun In Vitro and In Vivo

1999 ◽  
Vol 73 (1) ◽  
pp. 37-45 ◽  
Author(s):  
B. A. Morse ◽  
L. M. Carruth ◽  
J. E. Clements
Keyword(s):  
Transcription Factors ◽  
Protein Interactions ◽  
Tat Protein ◽  
Protein Protein Interactions ◽  
Viral Promoter ◽  
Visna Virus ◽  
Cellular Transcription ◽  
Virus Promoter

ABSTRACT The visna virus Tat protein is required for efficient viral transcription from the visna virus long terminal repeat (LTR). AP-1 sites within the visna virus LTR, which can be bound by the cellular transcription factors Fos and Jun, are also necessary for Tat-mediated transcriptional activation. A potential mechanism by which the visna virus Tat protein could target the viral promoter is by protein-protein interactions with Fos and/or Jun bound to AP-1 sites in the visna virus LTR. Once targeted to the visna virus promoter, the Tat protein could then interact with basal transcription factors to activate transcription. To examine protein-protein interactions with cellular proteins at the visna virus promoter, we used an in vitro protein affinity chromatography assay and electrophoretic mobility shift assay, in addition to an in vivo two-hybrid assay, to show that the visna virus Tat protein specifically interacts with the cellular transcription factors Fos and Jun and the basal transcription factor TBP (TATA binding protein). The Tat domain responsible for interactions with Fos and Jun was localized to an alpha-helical domain within amino acids 34 to 69 of the protein. The TBP binding domain was localized to amino acids 1 to 38 of Tat, a region previously described by our laboratory as the visna virus Tat activation domain. The bZIP domains of Fos and Jun were found to be important for the interactions with Tat. Mutations within the basic domains of Fos and Jun abrogated binding to Tat in the in vitro assays. The visna virus Tat protein was also able to interact with covalently cross-linked Fos and Jun dimers. Thus, the visna virus Tat protein appears to target AP-1 sites in the viral promoter in a mechanism similar to the interaction of human T-cell leukemia virus type 1 Tax with the cellular transcription factor CREB, by binding the basic domains of an intact bZIP dimer. The association between Tat, Fos, and Jun would position Tat proximal to the viral TATA box, where the visna virus Tat activation domain could contact TBP to activate viral transcription.

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