Summary of Study ST000165

This data is available at the NIH Common Fund's National Metabolomics Data Repository (NMDR) website, the Metabolomics Workbench, https://www.metabolomicsworkbench.org, where it has been assigned Project ID PR000143. The data can be accessed directly via it's Project DOI: 10.21228/M8GP4N This work is supported by NIH grant, U2C- DK119886.

See: https://www.metabolomicsworkbench.org/about/howtocite.php

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Download additional data:  the amino acids were measured under negative ion chemical ionisation conditions using isobutane as reactant gas

Study ID	ST000165
Study Title	Sparing of muscle mass and function by passive loading in an experimental intensive care unit model
Study Type	time course + intervention
Study Summary	A unique experimental rat ICU model has been used allowing long-term (weeks) time-resolved analyses of the effects of standardized unilateral passive mechanical loading on skeletal muscle size and function and underlying mechanisms. Results show that passive mechanical loading alleviated the muscle wasting and the loss of force-generation associated with the ICU intervention, resulting in a doubling of the functional capacity of the loaded versus the unloaded muscles after a 2-week ICU intervention.
Institute	Uppsala University
Department	Department of Neuroscience
Last Name	Larsson
First Name	Lars
Email	Lars.larsson@neuro.uu.se
Submit Date	2015-05-14
Num Groups	2
Total Subjects	13
Raw Data Available	No
Analysis Type Detail	IR-MS
Release Date	2015-05-10
Release Version	1

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Sample Preparation:

Sampleprep ID:	SP000184
Sampleprep Summary:	An i.v. bolus dose of [ring-13C6]phenylalanine (15 ?g g?1 body weight) was given 15 min prior to the animals being killed. Immediately after death, the gastrocnemius muscle was removed from the left and right hindlimb and split into a medial and lateral deep red and superficial white portion and frozen in liquid propane chilled by liquid nitrogen. Tissue fluid and mixed gastrocnemius muscle proteins were isolated according to the method of Ljungqvist et al. (1997). The mixed muscle protein precipitate from the isolation was hydrolysed by heating with 6 m HCl overnight at 110°C. Both tissue fluid and hydrolysed mixed gastrocnemius muscle amino acids were purified using a BioRad AG-50 × 8 ion exchange resin prior to mass spectrometry analysis. Tissue fluid The level of enrichment of [ring-13C6]phenylalanine in tissue fluid was analysed using ThermoFisher Quantum gas chromatography tandem mass spectrometry (GC/MS/MS) (San Jose, CA, USA). The heptafluorobutyryl isobutyl ester derivative was prepared as described by Ford et al. (1985) and the amino acids were measured under negative ion chemical ionisation conditions using isobutane as reactant gas. The [M-HF]? fragments reflecting the m0 and m+6 species were monitored (m/z transitions 397?377 and 403?383, respectively) and the enrichment of the label was measured against a calibration curve prepared from known amounts of labelled and unlabelled phenylalanine (range 030%).

Sampleprep ID:

SP000184

Sampleprep Summary:

An i.v. bolus dose of [ring-13C6]phenylalanine (15 ?g g?1 body weight) was given 15 min prior to the animals being killed. Immediately after death, the gastrocnemius muscle was removed from the left and right hindlimb and split into a medial and lateral deep red and superficial white portion and frozen in liquid propane chilled by liquid nitrogen. Tissue fluid and mixed gastrocnemius muscle proteins were isolated according to the method of Ljungqvist et al. (1997). The mixed muscle protein precipitate from the isolation was hydrolysed by heating with 6 m HCl overnight at 110°C. Both tissue fluid and hydrolysed mixed gastrocnemius muscle amino acids were purified using a BioRad AG-50 × 8 ion exchange resin prior to mass spectrometry analysis.
Tissue fluid
The level of enrichment of [ring-13C6]phenylalanine in tissue fluid was analysed using ThermoFisher Quantum gas chromatography tandem mass spectrometry (GC/MS/MS) (San Jose, CA, USA). The heptafluorobutyryl isobutyl ester derivative was prepared as described by Ford et al. (1985) and the amino acids were measured under negative ion chemical ionisation conditions using isobutane as reactant gas. The [M-HF]? fragments reflecting the m0 and m+6 species were monitored (m/z transitions 397?377 and 403?383, respectively) and the enrichment of the label was measured against a calibration curve prepared from known amounts of labelled and unlabelled phenylalanine (range 030%).