دورية أكاديمية
Quantitative Analysis of Acetyl-CoA, Malonyl-CoA, and Succinyl-CoA in Myocytes.
| العنوان: | Quantitative Analysis of Acetyl-CoA, Malonyl-CoA, and Succinyl-CoA in Myocytes. |
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| المؤلفون: | Tan L; Metabolomics Core Facility, Department of Bioinformatics and Computational Biology, The University of Texas MD Anderson Cancer Center, Houston, Texas 77054, United States., Martinez SA; Metabolomics Core Facility, Department of Bioinformatics and Computational Biology, The University of Texas MD Anderson Cancer Center, Houston, Texas 77054, United States., Lorenzi PL; Metabolomics Core Facility, Department of Bioinformatics and Computational Biology, The University of Texas MD Anderson Cancer Center, Houston, Texas 77054, United States., Karlstaedt A; Department of Cardiology, Smidt Heart Institute, Los Angeles, California 90048, United States. |
| المصدر: | Journal of the American Society for Mass Spectrometry [J Am Soc Mass Spectrom] 2023 Nov 01; Vol. 34 (11), pp. 2567-2574. Date of Electronic Publication: 2023 Oct 09. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: ACS Publications Country of Publication: United States NLM ID: 9010412 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-1123 (Electronic) Linking ISSN: 10440305 NLM ISO Abbreviation: J Am Soc Mass Spectrom Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 2020- : Washington, DC : ACS Publications Original Publication: New York, NY : Elsevier, c1990- |
| مواضيع طبية MeSH: | Malonyl Coenzyme A*/metabolism , Acyl Coenzyme A*/chemistry , Acyl Coenzyme A*/metabolism, Humans ; Acetyl Coenzyme A/metabolism ; Muscle Cells/chemistry ; Muscle Cells/metabolism |
| مستخلص: | Several analytical challenges make it difficult to accurately measure coenzyme A (CoA) metaboforms, including insufficient stability and a lack of available metabolite standards. Consequently, our understanding of CoA biology and the modulation of human diseases may be nascent. CoA's serve as lipid precursors, energy intermediates, and mediators of post-translational modifications of proteins. Here, we present a liquid chromatography-mass spectrometry (LC-MS) approach to measure malonyl-CoA, acetyl-CoA, and succinyl-CoA in complex biological samples. Additionally, we evaluated workflows to increase sample stability. We used reference standards to optimize CoA assay sensitivity and test CoA metabolite stability as a function of the reconstitution solvent. We show that using glass instead of plastic sample vials decreases CoA signal loss and improves the sample stability. We identify additives that improve CoA stability and facilitate accurate analysis of CoA species across large sample sets. We apply our optimized workflow to biological samples of skeletal muscle cells cultured under hypoxic and normoxia conditions. Together, our workflow improves the detection and identification of CoA species through targeted analysis in complex biological samples. |
| المشرفين على المادة: | BSI27HW5EQ (succinyl-coenzyme A) 524-14-1 (Malonyl Coenzyme A) 72-89-9 (Acetyl Coenzyme A) 0 (Acyl Coenzyme A) |
| تواريخ الأحداث: | Date Created: 20231009 Date Completed: 20231102 Latest Revision: 20231102 |
| رمز التحديث: | 20231102 |
| DOI: | 10.1021/jasms.3c00278 |
| PMID: | 37812744 |
| قاعدة البيانات: | MEDLINE |
Find this article in full text from Springer Verlag. 
Find this issue from the American Chemical Society | تدمد: | 1879-1123 |
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| DOI: | 10.1021/jasms.3c00278 |