Rasheed 2018 Arch Pathol Lab Med
| Rasheed MRHA, Tarjan G (2018) Succinate dehydrogenase Complex: an updated review. Arch Pathol Lab Med 142:1564-70. https://doi.org/10.5858/arpa.2017-0285-RS |
Rasheed MRHA, Tarjan G (2018) Arch Pathol Lab Med
Abstract: Succinate dehydrogenase (SDH) is uniquely tasked with a dual role in the essential energy-producing processes of a cell. Although SDH subunits and assembly factors form part of the same enzyme complex, mutations in their respective genes lead to significantly different clinical phenotypes. Remarkable discoveries in the last 17 years have led to the delineation of the SDH complex deficiency syndrome and its multiple pathogenic branches. Here we provide an updated overview of SDH deficiency in order to raise awareness of its multiple connotations including nonneoplastic associations and pertinent features of the continually growing list of SDH-mutant tumors so as to better direct genetic counseling and predict prognosis.
• Bioblast editor: Gnaiger E
Figure 1. Succinate dehydrogenase (SDH) complex in the electron transport chain. Succinate dehydrogenase assembly factor 2 (SDHAF2) adds a flavin adenine dinucleotide (FAD) cofactor to SDHA to form an active SDHA flavoprotein. a-Ketoglutarate is converted by a-ketoglutarate dehydrogenase (a-KGDH) to succinyl-CoA, which in turn is converted by succinyl-CoA synthetase (SCS) to succinate. SDHA oversees the oxidation of succinate to fumarate in the citric acid cycle, resulting in the reduction of FAD to FADH2.6 SDHAF1 is thought to interact with SDHB via insertion or retention of the iron-sulphur centers.4 Electrons are transferred through a chain of cofactors including the triple iron-sulphur centers on SDHB to ubiquinone, bound to the membrane-anchoring subunits SDHC and SDHD, reducing it to ubiquinol. Ubiquinol transfers the electrons along the transport chain to complex III (not shown).
Labels: MiParea: nDNA;cell genetics, mt-Medicine
Preparation: Enzyme
Enzyme: Complex II;succinate dehydrogenase
