scholarly journals LILY-lipidome isotope labeling of yeast: in vivo synthesis of 13C labeled reference lipids for quantification by mass spectrometry

The Analyst ◽  
2017 ◽  
Vol 142 (11) ◽  
pp. 1891-1899 ◽  
Author(s):  
Evelyn Rampler ◽  
Cristina Coman ◽  
Gerrit Hermann ◽  
Albert Sickmann ◽  
Robert Ahrends ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Dynamic Range ◽  
Isotope Labeling ◽  
Chemical Diversity ◽  
In Vivo Synthesis

Quantification is an essential task in comprehensive lipidomics studies challenged by the high number of lipids, their chemical diversity and their dynamic range (up to 7 orders of magnitude) of the lipidome.

Urinary metabolites of thromboxane and prostacyclin in diabetes mellitus

1988 ◽  
Vol 118 (2) ◽  
pp. 301-305 ◽  
Author(s):  
K. Gréen ◽  
O. Vesterqvist ◽  
V. Grill
Keyword(s):  
Diabetes Mellitus ◽  
Mass Spectrometry ◽  
Gas Chromatography ◽  
Insulin Treatment ◽  
Artificial Pancreas ◽  
Urinary Metabolites ◽  
Gas Chromatography Mass Spectrometry ◽  
Diabetic State ◽  
In Vivo Synthesis

Abstract. The in vivo synthesis of thromboxane A2 and prostacyclin was estimated in 23 diabetics through measurements of the major urinary metabolites 2,3-dinor-thromboxane B2 and 2,3-dinor-6-keto-PGF1α utilizing gas chromatography-mass spectrometry. Mean excretion was similar to that in non-diabetic subjects. The possible influence of hyperglycemia on the excretion of 2,3-dinor-thromboxane B2 and 2,3-dinor-6-keto-PGF1α was evaluated in three ways: by measuring excretion before and during an acute 9-h normalization of hyperglycemia through an artificial pancreas (Biostator) as well as by comparing excretion before and 7–12 days or 40–180 days after the initiation of insulin treatment. Despite significant reducing effects on hyperglycemia or on levels of hemoglobin A1c, no effects on the excretion of the thromboxane and prostacyclin metabolites could be found. Abnormal formation of thromboxane or prostacyclin is not a generalized feature of the diabetic state.

scholarly journals Interrogation of Dystrophin and Dystroglycan Complex Protein Turnover After Exon Skipping Therapy

2021 ◽  
pp. 1-20
Author(s):  
James S. Novak ◽  
Rita Spathis ◽  
Utkarsh J. Dang ◽  
Alyson A. Fiorillo ◽  
Ravi Hindupur ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Protein Expression ◽  
Protein Turnover ◽  
Isotope Labeling ◽  
Exon Skipping ◽  
Mdx Mice ◽  
Wild Type ◽  
Gene Correction ◽  
Dystrophin Protein

Recently, the Food and Drug Administration granted accelerated approvals for four exon skipping therapies –Eteplirsen, Golodirsen, Viltolarsen, and Casimersen –for Duchenne Muscular Dystrophy (DMD). However, these treatments have only demonstrated variable and largely sub-therapeutic levels of restored dystrophin protein in DMD patients, limiting their clinical impact. To better understand variable protein expression and the behavior of truncated dystrophin protein in vivo, we assessed turnover dynamics of restored dystrophin and dystroglycan complex (DGC) proteins in mdx mice after exon skipping therapy, compared to those dynamics in wild type mice, using a targeted, highly-reproducible and sensitive, in vivo stable isotope labeling mass spectrometry approach in multiple muscle tissues. Through statistical modeling, we found that restored dystrophin protein exhibited altered stability and slower turnover in treated mdx muscle compared with that in wild type muscle (∼44 d vs. ∼24 d, respectively). Assessment of mRNA transcript stability (quantitative real-time PCR, droplet digital PCR) and dystrophin protein expression (capillary gel electrophoresis, immunofluorescence) support our dystrophin protein turnover measurements and modeling. Further, we assessed pathology-induced muscle fiber turnover through bromodeoxyuridine (BrdU) labeling to model dystrophin and DGC protein turnover in the context persistent fiber degeneration. Our findings reveal sequestration of restored dystrophin protein after exon skipping therapy in mdx muscle leading to a significant extension of its half-life compared to the dynamics of full-length dystrophin in normal muscle. In contrast, DGC proteins show constant turnover attributable to myofiber degeneration and dysregulation of the extracellular matrix (ECM) in dystrophic muscle. Based on our results, we demonstrate the use of targeted mass spectrometry to evaluate the suitability and functionality of restored dystrophin isoforms in the context of disease and propose its use to optimize alternative gene correction strategies in development for DMD.

P3-071: IN VIVO STABLE ISOTOPE LABELING AND QUANTITATIVE MASS SPECTROMETRY IMAGING OF Aβ PLAQUE DEPOSITION AND TAUOPATHY IN HUMAN AD BRAIN

2006 ◽  
Vol 14 (7S_Part_20) ◽  
pp. P1091-P1092
Author(s):  
Norelle C. Wildburger ◽  
Greg S. Day ◽  
Wendy Sigurdson ◽  
Melissa Sullivan ◽  
Amanda Peters ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Stable Isotope ◽  
Mass Spectrometry Imaging ◽  
Isotope Labeling ◽  
Stable Isotope Labeling ◽  
Quantitative Mass Spectrometry ◽  
Plaque Deposition

The analytical method to identify the nitrogen source for nitric oxide synthesis

2020 ◽  
Vol 85 (2) ◽  
pp. 211-214
Author(s):  
Ryo Nasuno ◽  
Yuki Yoshikawa ◽  
Hiroshi Takagi
Keyword(s):  
Nitric Oxide ◽  
Mass Spectrometry ◽  
Nitrogen Source ◽  
Analytical Method ◽  
Isotope Labeling ◽  
Nitrogen Sources ◽  
Tandem Mass ◽  
Nitric Oxide Synthesis

ABSTRACT Nitric oxide (NO) is a ubiquitous signaling molecule synthesized from various nitrogen sources. An analytical method to identify a nitrogen source for NO generation was developed using liquid chromatography with tandem mass spectrometry in combination with stable isotope labeling. Our method successfully detected the 15N-labeled NO-containing compound generated from 15N-labeled substrate nitrite in vitro and in vivo.

P2-143: Quantitation of in vivo amyloid-beta synthesis and clearance rates in humans using stable isotope labeling and mass spectrometry

2006 ◽  
Vol 2 ◽  
pp. S275-S275
Author(s):  
Randall J. Bateman ◽  
Ling Munsell ◽  
John C. Morris ◽  
Kevin Yarasheski ◽  
David M. Holtzman
Keyword(s):  
Mass Spectrometry ◽  
Stable Isotope ◽  
Amyloid Beta ◽  
Isotope Labeling ◽  
Stable Isotope Labeling ◽  
Clearance Rates

scholarly journals In Vivo Stable-Isotope Labeling and Mass-Spectrometry-Based Metabolic Profiling of a Potent Tobacco-Specific Carcinogen in Rats

2018 ◽  
Vol 90 (20) ◽  
pp. 11863-11872 ◽  
Author(s):  
Romel Dator ◽  
Linda B. von Weymarn ◽  
Peter W. Villalta ◽  
Cory J. Hooyman ◽  
Laura A. Maertens ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Stable Isotope ◽  
Metabolic Profiling ◽  
Isotope Labeling ◽  
Stable Isotope Labeling
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