Academic Journal
Lactate Dehydrogenase-B Oxidation and Inhibition by Singlet Oxygen and Hypochlorous Acid
| العنوان: | Lactate Dehydrogenase-B Oxidation and Inhibition by Singlet Oxygen and Hypochlorous Acid |
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| المؤلفون: | Lisa M. Landino, Emily E. Lessard |
| المصدر: | Oxygen, Vol 4, Iss 4, Pp 432-448 (2024) |
| بيانات النشر: | MDPI AG, 2024. |
| سنة النشر: | 2024 |
| المجموعة: | LCC:Analytical chemistry LCC:Inorganic chemistry |
| مصطلحات موضوعية: | lactate dehydrogenase, singlet oxygen, hypochlorous acid, cysteine oxidation, reactive oxygen species, disulfide, Analytical chemistry, QD71-142, Inorganic chemistry, QD146-197 |
| الوصف: | Alterations in cellular energy metabolism are a hallmark of cancer and lactate dehydrogenase (LDH) enzymes are overexpressed in many cancers regardless of sufficient oxygen and functional mitochondria. Further, L-lactate plays signaling roles in multiple cell types. We evaluated the effect of singlet oxygen and hypochlorous acid (HOCl) on pig heart LDH-B, which shares 97% homology with human LDH-B. Singlet oxygen was generated photochemically using methylene blue or the chlorophyll metabolites, pheophorbide A and chlorin e6. Singlet oxygen induced protein crosslinks observed by SDS-PAGE under reducing conditions and inhibited LDH-B activity. Ascorbate, hydrocaffeic acid, glutathione and sodium azide were employed as singlet oxygen scavengers and shown to protect LDH-B. Using fluorescein-modified maleimide, no changes in cysteine availability as a result of singlet oxygen damage were observed. This was in contrast to HOCl, which induced the formation of disulfides between LDH-B subunits, thereby decreasing LDH-B labeling with fluorescein. HOCl oxidation inhibited LDH-B activity; however, disulfide reduction did not restore it. LDH-B cysteines were resistant to millimolar H2O2, chloramines and Angeli’s salt. In the absence of pyruvate, LDH-B enhanced NADH oxidation in a chain reaction initiated by singlet oxygen that resulted in H2O2 formation. Once damaged by either singlet oxygen or HOCl, NADH oxidation by LDH-B was impaired. |
| نوع الوثيقة: | article |
| وصف الملف: | electronic resource |
| اللغة: | English |
| تدمد: | 2673-9801 |
| Relation: | https://www.mdpi.com/2673-9801/4/4/27; https://doaj.org/toc/2673-9801 |
| DOI: | 10.3390/oxygen4040027 |
| URL الوصول: | https://doaj.org/article/4541f173edc74de2abf0a4e1867011a3 |
| رقم الانضمام: | edsdoj.4541f173edc74de2abf0a4e1867011a3 |
| قاعدة البيانات: | Directory of Open Access Journals |
| تدمد: | 26739801 |
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| DOI: | 10.3390/oxygen4040027 |