Pecina 2004 Physiol Res

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Pecina P, Houstkova H, Hansikova H, Zeman J, Houstek J (2004) Genetic defects of cytochrome c oxidase assembly. Physiol Res 53 Suppl 1:S213-23.

» PMID: 15119951 Open Access

Pecina P, Houstkova H, Hansikova H, Zeman J, Houstek J (2004) Physiol Res

Abstract: Cytochrome c oxidase (COX), the terminal enzyme of the mitochondrial respiratory chain, is one of the key functional and regulatory sites of the mammalian energy metabolism. Owing to the importance of the enzyme, pathogenetic mutations affecting COX frequently result in severe, often fatal metabolic disorders. No satisfactory therapy is currently available so that the treatment remains largely symptomatic and does not improve the course of the disease. While only few genetic defects of COX are caused by mutations in mitochondrial genome, during the last five years a large number of pathogenetic mutations in nuclear genes have been discovered. All these mutations are located in genes encoding COX-specific assembly proteins including SURF1, SCO1, SCO2, COX10, and COX15. Despite the identification of increasing number of mutations, their precise etiopathogenetic mechanisms, which are necessary for the development of future therapeutic protocols, still remain to be elucidated. This review summarizes recent developments, including our efforts in elucidation of the molecular basis of human mitochondrial diseases due to specific defects of COX with special focus on SURF1 assembly protein.

Keywords: Cytochrome c oxidase, SURF1, Leigh syndrome, Mitochondrial disorders

O2k-Network Lab: CZ Prague Houstek J, CZ Prague Zeman J


Labels: MiParea: Respiration, mtDNA;mt-genetics, mt-Medicine, Patients  Pathology: Inherited 

Organism: Human  Tissue;cell: Skeletal muscle, Fibroblast 

Enzyme: Complex IV;cytochrome c oxidase 


HRR: Oxygraph-2k