Summary of Study ST001665
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 PR001070. The data can be accessed directly via it's Project DOI: 10.21228/M8D12Q This work is supported by NIH grant, U2C- DK119886.
See: https://www.metabolomicsworkbench.org/about/howtocite.php
Study ID | ST001665 |
Study Title | Branched-chain alpha-ketoacids are preferentially reaminated and activate protein synthesis in the rat heart |
Study Summary | Branched-chain amino acids (BCAA) and their cognate α-ketoacids (BCKA) are elevated in an array of cardiometabolic diseases. Here we demonstrate that the major metabolic fate of uniformly-13C-labeled α-ketoisovalerate ([U-13C]KIV) in the heart is reamination to valine. Activation of cardiac branched-chain α-ketoacid dehydrogenase (BCKDH) by treatment with the BCKDH kinase inhibitor, BT2, does not impede the strong flux of [U-13C]KIV to valine. |
Institute | Duke University |
Last Name | Walejko |
First Name | Jacquelyn |
Address | 300 N Duke St |
jacquelyn.walejko@duke.edu | |
Phone | 9194792304 |
Submit Date | 2021-01-26 |
Analysis Type Detail | GC-MS |
Release Date | 2021-02-17 |
Release Version | 1 |
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Factors:
Subject type: Mammal; Subject species: Rattus norvegicus (Factor headings shown in green)
mb_sample_id | local_sample_id | Treatment |
---|---|---|
SA152214 | 206 | BT-2 |
SA152215 | 217 | BT-2 |
SA152216 | 205 | BT-2 |
SA152217 | 216 | BT-2 |
SA152218 | 215 | Control |
SA152219 | 200 | Control |
SA152220 | 207 | Control |
SA152221 | 208 | Control |
SA152222 | 199 | Control |
SA152223 | 218 | LY |
SA152224 | 214 | LY |
SA152225 | 211 | LY |
SA152226 | 210 | LY |
SA152227 | 212 | LY |
SA152228 | 213 | LY |
Showing results 1 to 15 of 15 |