scholarly journals Mass Spectrometry-Based Methodology for Identification of Native Histone Variant Modifications From Mammalian Tissues and Solid Tumors

2017 ◽  
pp. 275-290 ◽  
Author(s):  
A.G. Nuccio ◽  
M. Bui ◽  
Y. Dalal ◽  
A. Nita-Lazar
Keyword(s):  
Mass Spectrometry ◽  
Solid Tumors ◽  
Histone Variant ◽  
Mammalian Tissues

Imaging mass spectrometry: challenges in visualization of drug distribution in solid tumors

2013 ◽  
Vol 13 (5) ◽  
pp. 807-812 ◽  
Author(s):  
Lavinia Morosi ◽  
Massimo Zucchetti ◽  
Maurizio D’Incalci ◽  
Enrico Davoli
Keyword(s):  
Mass Spectrometry ◽  
Solid Tumors ◽  
Imaging Mass Spectrometry ◽  
Drug Distribution

Mass spectrometry-based phosphoproteomics of tumor needle biopsies from patients (pts) with advanced solid tumors during treatment with protein kinase inhibitors.

2016 ◽  
Vol 34 (15_suppl) ◽  
pp. 11609-11609
Author(s):  
Mariette Labots ◽  
Robin Beekhof ◽  
Jaco C. Knol ◽  
Maarten Neerincx ◽  
Richard R. de Haas ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Protein Kinase ◽  
Solid Tumors ◽  
Kinase Inhibitors ◽  
Protein Kinase Inhibitors ◽  
Advanced Solid Tumors

Imaging mass spectrometry: A new technology for the analysis of protein expression in mammalian tissues

10.1038/86573 ◽  
2001 ◽  
Vol 7 (4) ◽  
pp. 493-496 ◽  
Author(s):  
Markus Stoeckli ◽  
Pierre Chaurand ◽  
Dennis E. Hallahan ◽  
Richard M. Caprioli
Keyword(s):  
Mass Spectrometry ◽  
Protein Expression ◽  
New Technology ◽  
Imaging Mass Spectrometry ◽  
Mammalian Tissues

scholarly journals Mapping post‐translational modifications of the histone variant macroH2A1 using tandem mass spectrometry

2006 ◽  
Vol 20 (4) ◽  
Author(s):  
Feixia Chu ◽  
Dmitri A Nusinow ◽  
Robert J Chalkley ◽  
Kathrin Plath ◽  
Barbara Panning ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Tandem Mass Spectrometry ◽  
Histone Variant ◽  
Tandem Mass ◽  
Post Translational Modifications

scholarly journals Mapping Post-translational Modifications of the Histone Variant MacroH2A1 Using Tandem Mass Spectrometry

2005 ◽  
Vol 5 (1) ◽  
pp. 194-203 ◽  
Author(s):  
Feixia Chu ◽  
Dmitri A. Nusinow ◽  
Robert J. Chalkley ◽  
Kathrin Plath ◽  
Barbara Panning ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Tandem Mass Spectrometry ◽  
Histone Variant ◽  
Tandem Mass ◽  
Post Translational Modifications

scholarly journals The Mammalian Cytosolic Type 2 (R)-β-hydroxybutyrate Dehydrogenase (BDH2) is 4-oxo-L-proline Reductase (EC 1.1.1.104)

2021 ◽  
Author(s):  
Sebastian P. Kwiatkowski ◽  
Maria Bozko ◽  
Michal Zarod ◽  
Apolonia Witecka ◽  
Adam K. Jagielski ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Biochemical Characterization ◽  
Mass Spectrometry Analysis ◽  
Protein Preparation ◽  
Spectrometry Analysis ◽  
E Coli ◽  
Mammalian Tissues ◽  
Reversible Reduction

AbstractThe early studies on chicken embryos revealed that exposition to 4-oxo-L-proline resulted in the explicit increase in 4-hydroxy-L-proline content in their tissues. In 1962, 4-oxo-L-proline reductase, an enzyme responsible for the reduction of 4-oxo-L-proline, was partially purified from rabbit kidneys and characterized biochemically, but only recently the molecular identity of the enzyme has been unveiled in our laboratory. The present investigation reports the purification, identification as well as biochemical characterization of 4-oxo-L-proline reductase. The enzyme was purified from rat kidneys about 280-fold. Following mass spectrometry analysis of the purified protein preparation, the mammalian cytosolic type 2 (R)-β-hydroxybutyrate dehydrogenase (BDH2) emerged as the only meaningful candidate for the reductase. Rat and human BDH2 were expressed in E. coli, purified, and shown to catalyze the reversible reduction of 4-oxo-L-proline to cis-4-hydroxy-L-proline, as confirmed by chromatographic and mass spectrometry analysis. Specificity studies carried out on both enzymes showed that 4-oxo-L-proline was the best substrate, particularly the human enzyme acted with 9400-fold higher catalytic efficiencies on 4-oxo-L-proline than on (R)-β-hydroxybutyrate. Finally, HEK293T cells efficiently metabolized 4-oxo-L-proline to cis-4-hydroxy-L-proline and simultaneously accumulated trans-4-hydroxy-L-proline in the culture medium, suggesting that 4-oxo-L-proline is most likely an inhibitor of trans-4-hydroxy-L-proline metabolism in human cells. We conclude that BDH2 is mammalian 4-oxo-L-proline reductase that converts 4-oxo-L-proline to cis-4-hydroxy-L-proline, and not to trans-4-hydroxy-L-proline as currently thought, and hypothesize that the enzyme may be considered as a potential source of cis-4-hydroxy-L-proline in mammalian tissues.

scholarly journals Plk1 regulates the kinesin-13 protein Kif2b to promote faithful chromosome segregation

2012 ◽  
Vol 23 (12) ◽  
pp. 2264-2274 ◽  
Author(s):  
Emily A. Hood ◽  
Arminja N. Kettenbach ◽  
Scott A. Gerber ◽  
Duane A. Compton
Keyword(s):  
Mass Spectrometry ◽  
Solid Tumors ◽  
Chromosome Segregation ◽  
Chromosomal Instability ◽  
Phosphorylation Sites ◽  
Common Cause ◽  
Chromosome Missegregation

Solid tumors are frequently aneuploid, and many display high rates of ongoing chromosome missegregation in a phenomenon called chromosomal instability (CIN). The most common cause of CIN is the persistence of aberrant kinetochore-microtubule (k-MT) attachments, which manifest as lagging chromosomes in anaphase. k-MT attachment errors form during prometaphase due to stochastic interactions between kinetochores and microtubules. The kinesin-13 protein Kif2b promotes the correction of k-MT attachment errors in prometaphase, but the mechanism restricting this activity to prometaphase remains unknown. Using mass spectrometry, we identified multiple phosphorylation sites on Kif2b, some of which are acutely sensitive to inhibition of Polo-like kinase 1 (Plk1). We show that Plk1 directly phosphorylates Kif2b at threonine 125 (T125) and serine 204 (S204), and that these two sites differentially regulate Kif2b function. Phosphorylation of S204 is required for the kinetochore localization and activity of Kif2b in prometaphase, and phosphorylation of T125 is required for Kif2b activity in the correction of k-MT attachment errors. These data demonstrate that Plk1 regulates both the localization and activity of Kif2b during mitosis to promote the correction of k-MT attachment errors to ensure mitotic fidelity.

Recent Studies on a Murine Leukemia Virus Grown in Tissue Culture

1967 ◽  
Vol 25 ◽  
pp. 106-107
Author(s):  
L. Z. de Tkaczevski ◽  
E. de Harven ◽  
C. Friend
Keyword(s):  
Tissue Culture ◽  
Solid Tumors ◽  
Murine Leukemia Virus ◽  
Leukemia Virus ◽  
Supernatant Fluid ◽  
Virus Particles ◽  
Friend Leukemia ◽  
Type C ◽  
Leukemia Viruses ◽  
Murine Leukemia

Despite extensive studies, the correlation between the morphology and pathogenicity of murine leukemia viruses (MLV) has not yet been clarified. The virus particles found in the plasma of leukemic mice belong to 2 distinct groups, 1 or 2% of them being enveloped A particles and the vast majority being of type C. It is generally believed that these 2 types of particles represent different phases in the development of the same virus. Particles of type A have been thought to be an earlier form of type C particles. One of the tissue culture lines established from Friend leukemia solid tumors has provided the material for the present study. The supernatant fluid of the line designated C-1A contains an almost pure population of A particles as illustrated in Figure 1. The ratio is, therefore, the reverse of what is unvariably observed in the plasma of leukemic mice where C particles predominate.

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