Cytochrome a3 deficiency in human achondroplasia

• Published in: Biochimica et biophysica acta Vol. 891; no. 2; pp. 145 - 149
• Main Authors: MACKLER, B, DAVIS, K. A, GRACE, R
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier 15.04.1987; North-Holland
• Subjects: Achondroplasia - enzymology; Achondroplasia - genetics; Biological and medical sciences; Cytochrome a Group; Cytochrome b Group - metabolism; Cytochrome-c Oxidase Deficiency; Cytochromes - metabolism; Diseases of the osteoarticular system; Fibroblasts - enzymology; Genetic Carrier Screening; Homozygote; Humans; Infant; Malformations and congenital and or hereditary diseases involving bones. Joint deformations; Medical sciences; Mitochondria - enzymology; Reference Values; Skin - enzymology; Succinate Dehydrogenase - metabolism; Achondroplasia; Cytochrome aa3; Osteochondrodysplasia; Deficiency
• ISSN: 0006-3002
• DOI: 10.1016/0005-2728(87)90006-5

Mitochondria prepared from tissue culture cells (skin fibroblasts) from normal subjects and subjects with homozygous achondroplasia were studied to determine the concentrations of cytochromes a and a3 in the preparations. Cytochrome a3 was markedly decreased (80%) in the achondroplastic preparations with cytochrome a present in normal amounts. Determination of total heme a (as the pyridine hemochromogen) in the normal and achondroplastic preparations demonstrated that the observed decrease in concentration of cytochrome a3 in the achondroplastic preparations was due to an absence of cytochrome a3 and not to a change in its absorbancy (extinction coefficient). The decreased concentrations of cytochrome a3 in the achondroplastic cells may decrease the reactivity or affinity of the mitochondrial oxidative systems for oxygen and result in the phenotypic expression of the disease.