case_images: PMC10800918_01
case_images: Pedigree of the family. Individuals with SDHC c.197C>T (p.Ala66Val) positive test are indicated by the plus sign.
case_images: fonc-13-1324013-g001.jpg
case_images: PMC10800918_01_fonc-13-1324013-g001.jpg
case_images: f1
case_images: Unfortunately, a bone marrow evaluation during early follow-up showed the onset of secondary AML carrying t(9;11) MLL-AF9 translocation ( Supplementary Figure S1 ).
case_images: Cytochemistry for succinate dehydrogenase on fibroblasts. No variation is observed between control (A) and patient (B).
case_images: fonc-13-1324013-g002.jpg
case_images: PMC10800918_01_fonc-13-1324013-g002.jpg
case_images: f2
case_images: Fibroblasts underwent a cytochemical investigation for the enzyme succinate dehydrogenase ( Figure 2 ); through mitochondrial respiratory chain complex V enzyme activity, we evaluated adenosine triphosphate (ATP) production in mitochondria purified from fibroblasts using different substrates: succinate, specific for succinate dehydrogenase (respiratory chain complex II) and two others specific for NADH dehydrogenase (respiratory chain complex I) ( Figure 3A ); by western blotting we evaluated the content of the C subunit and 2 other subunits of succinate dehydrogenase ( Figure 3B ).
case_images: Western blotting on homogenate of fibroblasts. (A) Densitometric analysis of five experiments on three different fibroblast extractions for SDHC, SDHA and SDHB subunits. TOMM20 has been used for normalization of the referred proteins. (B) A representative experiment out of the five performed. No variation is observed between control and patient for the SDHC subunit, as well for SDHA and SDHB. Ct.1 and Ct.2: two different controls fibroblasts; Pr.1sr and Pt.2nd: two different protein extraction from patient's fibroblasts.
case_images: fonc-13-1324013-g003.jpg
case_images: PMC10800918_01_fonc-13-1324013-g003.jpg
case_images: f3
case_images: Fibroblasts underwent a cytochemical investigation for the enzyme succinate dehydrogenase ( Figure 2 ); through mitochondrial respiratory chain complex V enzyme activity, we evaluated adenosine triphosphate (ATP) production in mitochondria purified from fibroblasts using different substrates: succinate, specific for succinate dehydrogenase (respiratory chain complex II) and two others specific for NADH dehydrogenase (respiratory chain complex I) ( Figure 3A ); by western blotting we evaluated the content of the C subunit and 2 other subunits of succinate dehydrogenase ( Figure 3B ).