Noninvasive Imaging of Protein Metabolic Labeling in Single Human Cells Using Stable Isotopes and Raman Microscopy

2008 ◽  
Vol 80 (24) ◽  
pp. 9576-9582 ◽  
Author(s):  
Henk-Jan van Manen ◽  
Aufried Lenferink ◽  
Cees Otto
Keyword(s):  
Stable Isotopes ◽  
Noninvasive Imaging ◽  
Raman Microscopy ◽  
Human Cells ◽  
Metabolic Labeling

scholarly journals High-Resolution Mass Spectrometry for In Vivo Proteome Dynamics using Heavy Water Metabolic Labeling

2020 ◽  
Vol 21 (21) ◽  
pp. 7821
Author(s):  
Rovshan G. Sadygov
Keyword(s):  
Stable Isotopes ◽  
Heavy Water ◽  
Large Scale ◽  
High Resolution Mass Spectrometry ◽  
Mass Resolution ◽  
Mass Analyzer ◽  
Metabolic Labeling ◽  
Spectral Accuracy ◽  
Mass Spectrometers ◽  
Modern Mass

Cellular proteins are continuously degraded and synthesized. The turnover of proteins is essential to many cellular functions. Combined with metabolic labeling using stable isotopes, LC–MS estimates proteome dynamics in high-throughput and on a large scale. Modern mass spectrometers allow a range of instrumental settings to optimize experimental output for specific research goals. One such setting which affects the results for dynamic proteome studies is the mass resolution. The resolution is vital for distinguishing target species from co-eluting contaminants with close mass-to-charge ratios. However, for estimations of proteome dynamics from metabolic labeling with stable isotopes, the spectral accuracy is highly important. Studies examining the effects of increased mass resolutions (in modern mass spectrometers) on the proteome turnover output and accuracy have been lacking. Here, we use a publicly available heavy water labeling and mass spectral data sets of murine serum proteome (acquired on Orbitrap Fusion and Agilent 6530 QToF) to analyze the effect of mass resolution of the Orbitrap mass analyzer on the proteome dynamics estimation. Increased mass resolution affected the spectral accuracy and the number acquired tandem mass spectra.

Monitoring the Glutathione Redox Reaction in Living Human Cells by Combining Metabolic Labeling with Heteronuclear NMR

2016 ◽  
Vol 128 (28) ◽  
pp. 8071-8074 ◽  
Author(s):  
Xing Jin ◽  
Soeun Kang ◽  
Shinya Tanaka ◽  
Sunghyouk Park
Keyword(s):  
Redox Reaction ◽  
Heteronuclear Nmr ◽  
Human Cells ◽  
Metabolic Labeling ◽  
Glutathione Redox

scholarly journals Metabolic labeling of human cells with tritiated nucleosides results in activation of the ATM-dependent p53 signaling pathway and acceleration of DNA repair

Oncogene ◽  
2003 ◽  
Vol 22 (36) ◽  
pp. 5562-5571 ◽  
Author(s):  
Razmik Mirzayans ◽  
Scott Pollock ◽  
April Scott ◽  
Cindy Q Gao ◽  
David Murray
Keyword(s):  
Dna Repair ◽  
Signaling Pathway ◽  
Human Cells ◽  
Metabolic Labeling ◽  
P53 Signaling ◽  
P53 Signaling Pathway

Metabolic Labeling of Mammalian Organisms with Stable Isotopes for Quantitative Proteomic Analysis

2004 ◽  
Vol 76 (17) ◽  
pp. 4951-4959 ◽  
Author(s):  
Christine C. Wu ◽  
Michael J. MacCoss ◽  
Kathryn E. Howell ◽  
Dwight E. Matthews ◽  
John R. Yates
Keyword(s):  
Stable Isotopes ◽  
Proteomic Analysis ◽  
Metabolic Labeling ◽  
Quantitative Proteomic Analysis

SEM–Raman image cytometry of cells

The Analyst ◽  
2018 ◽  
Vol 143 (18) ◽  
pp. 4495-4502 ◽  
Author(s):  
A. Enciso-Martinez ◽  
F. J. Timmermans ◽  
A. Nanou ◽  
L. W. M. M. Terstappen ◽  
C. Otto
Keyword(s):  
Image Cytometry ◽  
Raman Microscopy ◽  
Human Cells ◽  
Raman Image ◽  
Individual Human

Hybrid SEM–Raman microscopy to distinguish individual human cells.

scholarly journals Characterization of the human c-fms gene product and its expression in cells of the monocyte-macrophage lineage.

1985 ◽  
Vol 5 (12) ◽  
pp. 3458-3466 ◽  
Author(s):  
J Woolford ◽  
V Rothwell ◽  
L Rohrschneider
Keyword(s):  
Rabbit Antiserum ◽  
Growth Factor Receptor ◽  
Protein Product ◽  
Human Cells ◽  
Cell Protein ◽  
Bewo Cell ◽  
Metabolic Labeling ◽  
Bewo Cells ◽  
Human Choriocarcinoma Cells

The McDonough strain of feline sarcoma virus contains an oncogene called v-fms whose ultimate protein product (gp140v-fms) resembles a cell surface growth factor receptor. To identify and characterize the protein product of the proto-oncogene c-fms, antisera were prepared to the viral fms sequences and used to detect specific cross-reacting sequences in human choriocarcinoma cells (BeWo) known to express c-fms mRNA. Both tumor-bearing rat sera and a rabbit antiserum prepared to a segment of v-fms expressed in Escherichia coli detected a 140-kilodalton (kDa) glycoprotein in the BeWo cells. Tryptic fingerprint analysis of [35S]methionine-labeled proteins indicated that the viral fms proteins and the 140-kDa BeWo cell protein were highly related. This 140-kDa glycoprotein contained an associated tyrosine kinase activity in vitro and was labeled principally on serine after 32Pi metabolic labeling. These results suggest that the 140-kDa protein in BeWo cells is the protein product of the human c-fms proto-oncogene. This conclusion is supported by the finding that a similar protein is detectable only in other human cells that express c-fms mRNA. These other human cells include adherent monocytes and the cell line ML-1, which can be induced to differentiate along the monocyte-macrophage pathway. This is in agreement with current thought that the c-fms proto-oncogene product functions as the CSF-1 receptor specific to this pathway.

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