Poly(ADP-ribose) degradation by post-nuclear extracts from human cells

Biochimie ◽  
2002 ◽  
Vol 84 (12) ◽  
pp. 1227-1233 ◽  
Author(s):  
L Rossi
Keyword(s):  
Human Cells ◽  
Nuclear Extracts ◽  
Ribose Degradation

scholarly journals Deoxyinosine repair in nuclear extracts of human cells

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Chia-Chia Lee ◽  
Ya-Chien Yang ◽  
Steven D. Goodman ◽  
Shi Chen ◽  
Teng-Yung Huang ◽  
...  
Keyword(s):  
Human Cells ◽  
Nuclear Extracts

scholarly journals Expression and regulation by interferon of a double-stranded-RNA-specific adenosine deaminase from human cells: evidence for two forms of the deaminase.

1995 ◽  
Vol 15 (10) ◽  
pp. 5376-5388 ◽  
Author(s):  
J B Patterson ◽  
C E Samuel
Keyword(s):  
Adenosine Deaminase ◽  
Fusion Proteins ◽  
Immunoblot Analysis ◽  
Binding Activity ◽  
Human Cells ◽  
Cell Fractionation ◽  
Double Stranded Rna ◽  
Nuclear Extracts ◽  
Dsrna Binding ◽  
Ifn Treatment

A 6,474-nucleotide human cDNA clone designated K88, which encodes double-stranded RNA (dsRNA)-specific adenosine deaminase, was isolated in a screen for interferon (IFN)-regulated cDNAs. Northern (RNA) blot analysis revealed that the K88 cDNA hybridized to a single major transcript of approximately 6.7 kb in human cells which was increased about fivefold by IFN treatment. Polyclonal antisera prepared against K88 cDNA products expressed in Escherichia coli as glutathione S-transferase (GST) fusion proteins recognized two proteins by Western (immunoblot) analysis. An IFN-induced 150-kDa protein and a constitutively expressed 110-kDa protein whose level was not altered by IFN treatment were detected in human amnion U and neuroblastoma SH-SY5Y cell lines. Only the 150-kDa protein was detected in mouse fibroblasts with antiserum raised against the recombinant human protein; the mouse 150-kDa protein was IFN inducible. Immunofluorescence microscopy and cell fractionation analyses showed that the 110-kDa protein was exclusively nuclear, whereas the 150-kDa protein was present in both the cytoplasm and nucleus of human cells. The amino acid sequence deduced from the K88 cDNA includes three copies of the highly conserved R motif commonly found in dsRNA-binding proteins. Both the 150-kDa and the 110-kDa proteins prepared from human nuclear extracts bound to double-stranded but not to single-stranded RNA affinity columns. Furthermore, E. coli-expressed GST-K88 fusion proteins that included the R motif possessed dsRNA-binding activity. Extracts prepared either from K88 cDNA-transfected cells or from IFN-treated cells contained increased dsRNA-specific adenosine deaminase enzyme activity. These results establish that K88 encodes an IFN-inducible dsRNA-specific adenosine deaminase and suggest that at least two forms of dsRNA-specific adenosine deaminase occur in human cells.

Design and chemoproteomic functional characterization of a chemical probe targeted to bromodomains of BET family proteins

MedChemComm ◽  
2014 ◽  
Vol 5 (12) ◽  
pp. 1871-1878 ◽  
Author(s):  
Jiang Wu ◽  
Julia Shin ◽  
Cara M. M. Williams ◽  
Kieran F. Geoghegan ◽  
Stephen W. Wright ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Human Cells ◽  
Chemical Probe ◽  
Affinity Capture ◽  
Nuclear Extracts

Selectivity of a PFI-1 based BET bromodomain probe was demonstrated using affinity capture in nuclear extracts from human cells.

scholarly journals Identification of a nuclear-localized nuclease from wheat cells undergoing programmed cell death that is able to trigger DNA fragmentation and apoptotic morphology on nuclei from human cells

2006 ◽  
Vol 397 (3) ◽  
pp. 529-536 ◽  
Author(s):  
Fernando Domínguez ◽  
Francisco J. Cejudo
Keyword(s):  
Cell Death ◽  
Programmed Cell Death ◽  
Serine Protease ◽  
Dna Fragmentation ◽  
Plant Cells ◽  
Human Cells ◽  
Animal Cells ◽  
Free System ◽  
Nuclear Extracts ◽  
Apoptotic Morphology

PCD (programmed cell death) in plants presents important morphological and biochemical differences compared with apoptosis in animal cells. This raises the question of whether PCD arose independently or from a common ancestor in plants and animals. In the present study we describe a cell-free system, using wheat grain nucellar cells undergoing PCD, to analyse nucleus dismantling, the final stage of PCD. We have identified a Ca2+/Mg2+ nuclease and a serine protease localized to the nucleus of dying nucellar cells. Nuclear extracts from nucellar cells undergoing PCD triggered DNA fragmentation and other apoptotic morphology in nuclei from different plant tissues. Inhibition of the serine protease did not affect DNA laddering. Furthermore, we show that the nuclear extracts from plant cells triggered DNA fragmentation and apoptotic morphology in nuclei from human cells. The inhibition of the nucleolytic activity with Zn2+ or EDTA blocked the morphological changes of the nucleus. Moreover, nuclear extracts from apoptotic human cells triggered DNA fragmentation and apoptotic morphology in nuclei from plant cells. These results show that degradation of the nucleus is morphologically and biochemically similar in plant and animal cells. The implication of this finding on the origin of PCD in plants and animals is discussed.

In vitro correction of G o T mispairs to G o C pairs in nuclear extracts from human cells

Nature ◽  
1989 ◽  
Vol 339 (6221) ◽  
pp. 234-236 ◽  
Author(s):  
Karin Wiebauer ◽  
Josef Jiricny
Keyword(s):  
Human Cells ◽  
Nuclear Extracts

Alpha-Tocopherol Protects Cultured Human Cells from the Acute Lethal Cytotoxicity of Dioxin

2002 ◽  
Vol 72 (3) ◽  
pp. 147-153 ◽  
Author(s):  
Kei-Ichi Hirai ◽  
Jie-Hong Pan ◽  
Ying-Bo Shui ◽  
Eriko Simamura ◽  
Hiroki Shimada ◽  
...  
Keyword(s):  
Cell Death ◽  
Cell Damage ◽  
Smooth Endoplasmic Reticulum ◽  
Dehydroascorbic Acid ◽  
Human Cells ◽  
Alpha Tocopherol ◽  
Cervical Cancer Cells ◽  
Cultured Human Cells ◽  
Nuclear Damage ◽  
Conjunctival Epithelial Cells

The possible protection of cultured human cells from acute dioxin injury by antioxidants was investigated. The most potent dioxin, 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), caused vacuolization of the smooth endoplasmic reticulum and Golgi apparatus in cultured human conjunctival epithelial cells and cervical cancer cells. Subsequent nuclear damage included a deep irregular indentation resulting in cell death. A dosage of 30–40 ng/mL TCDD induced maximal intracellular production of H2O2 at 30 minutes and led to severe cell death (0–31% survival) at two hours. A dose of 1.7 mM alpha-tocopherol or 1 mM L-dehydroascorbic acid significantly protected human cells against acute TCDD injuries (78–97% survivals), but vitamin C did not provide this protection. These results indicate that accidental exposure to fatal doses of TCDD causes cytoplasmic free radical production within the smooth endoplasmic reticular systems, resulting in severe cytotoxicity, and that vitamin E and dehydroascorbic acid can protect against TCDD-induced cell damage.

Chromium oxidation state mapping in human cells

2003 ◽  
Vol 104 ◽  
pp. 289-292 ◽  
Author(s):  
R. Ortega ◽  
B. Fayard ◽  
M. Salomé ◽  
G. Devès ◽  
J. Susini
Keyword(s):  
Oxidation State ◽  
Human Cells ◽  
Chromium Oxidation
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