The Experts below are selected from a list of 52221 Experts worldwide ranked by ideXlab platform
Elsebet Ostergaard - One of the best experts on this subject based on the ideXlab platform.
-
the severity of phenotype linked to suclg1 mutations could be correlated with Residual Amount of suclg1 protein
Journal of Medical Genetics, 2010Co-Authors: Cecile Rouzier, Le S Guedardmereuze, Sylvie Tufferygiraud, Sylvie Bannwarth, C Caruba, Jeanluc Miro, Konstantina Fragaki, Annabelle Chaussenot, Elsebet OstergaardAbstract:Background Succinate-CoA ligase deficiency is responsible for encephalomyopathy with mitochondrial DNA depletion and mild methylmalonic aciduria. Mutations in SUCLA2 , the gene encoding a β subunit of succinate-CoA ligase, have been reported in 17 patients until now. Mutations in SUCLG1 , encoding the α subunit of the enzyme, have been described in two pedigrees only. Methods and findings In this study, two unrelated patients harbouring three novel pathogenic mutations in SUCLG1 were reported. The first patient had a severe disease at birth. He was compound heterozygous for a missense mutation (p.Pro170Arg) and a c.97+3G>C mutation, which leads to the complete skipping of exon 1 in a minigene expression system. The involvement of SUCLG1 was confirmed by western blot analysis, which showed absence of SUCLG1 protein in fibroblasts. The second patient has a milder phenotype, similar to that of patients with SUCLA2 mutations, and is still alive at 12 years of age. Western blot analysis showed some Residual SUCLG1 protein in patient9s fibroblasts. Conclusions Our results suggest that SUCLG1 mutations that lead to complete absence of SUCLG1 protein are responsible for a very severe disorder with antenatal manifestations, whereas a SUCLA2 -like phenotype is found in patients with Residual SUCLG1 protein. Furthermore, it is shown that in the absence of SUCLG1 protein, no SUCLA2 protein is found in fibroblasts by western blot analysis. This result is consistent with a degradation of SUCLA2 when its heterodimer partner, SUCLG1, is absent.
Cecile Rouzier - One of the best experts on this subject based on the ideXlab platform.
-
the severity of phenotype linked to suclg1 mutations could be correlated with Residual Amount of suclg1 protein
Journal of Medical Genetics, 2010Co-Authors: Cecile Rouzier, Le S Guedardmereuze, Sylvie Tufferygiraud, Sylvie Bannwarth, C Caruba, Jeanluc Miro, Konstantina Fragaki, Annabelle Chaussenot, Elsebet OstergaardAbstract:Background Succinate-CoA ligase deficiency is responsible for encephalomyopathy with mitochondrial DNA depletion and mild methylmalonic aciduria. Mutations in SUCLA2 , the gene encoding a β subunit of succinate-CoA ligase, have been reported in 17 patients until now. Mutations in SUCLG1 , encoding the α subunit of the enzyme, have been described in two pedigrees only. Methods and findings In this study, two unrelated patients harbouring three novel pathogenic mutations in SUCLG1 were reported. The first patient had a severe disease at birth. He was compound heterozygous for a missense mutation (p.Pro170Arg) and a c.97+3G>C mutation, which leads to the complete skipping of exon 1 in a minigene expression system. The involvement of SUCLG1 was confirmed by western blot analysis, which showed absence of SUCLG1 protein in fibroblasts. The second patient has a milder phenotype, similar to that of patients with SUCLA2 mutations, and is still alive at 12 years of age. Western blot analysis showed some Residual SUCLG1 protein in patient9s fibroblasts. Conclusions Our results suggest that SUCLG1 mutations that lead to complete absence of SUCLG1 protein are responsible for a very severe disorder with antenatal manifestations, whereas a SUCLA2 -like phenotype is found in patients with Residual SUCLG1 protein. Furthermore, it is shown that in the absence of SUCLG1 protein, no SUCLA2 protein is found in fibroblasts by western blot analysis. This result is consistent with a degradation of SUCLA2 when its heterodimer partner, SUCLG1, is absent.
Jeanluc Miro - One of the best experts on this subject based on the ideXlab platform.
-
the severity of phenotype linked to suclg1 mutations could be correlated with Residual Amount of suclg1 protein
Journal of Medical Genetics, 2010Co-Authors: Cecile Rouzier, Le S Guedardmereuze, Sylvie Tufferygiraud, Sylvie Bannwarth, C Caruba, Jeanluc Miro, Konstantina Fragaki, Annabelle Chaussenot, Elsebet OstergaardAbstract:Background Succinate-CoA ligase deficiency is responsible for encephalomyopathy with mitochondrial DNA depletion and mild methylmalonic aciduria. Mutations in SUCLA2 , the gene encoding a β subunit of succinate-CoA ligase, have been reported in 17 patients until now. Mutations in SUCLG1 , encoding the α subunit of the enzyme, have been described in two pedigrees only. Methods and findings In this study, two unrelated patients harbouring three novel pathogenic mutations in SUCLG1 were reported. The first patient had a severe disease at birth. He was compound heterozygous for a missense mutation (p.Pro170Arg) and a c.97+3G>C mutation, which leads to the complete skipping of exon 1 in a minigene expression system. The involvement of SUCLG1 was confirmed by western blot analysis, which showed absence of SUCLG1 protein in fibroblasts. The second patient has a milder phenotype, similar to that of patients with SUCLA2 mutations, and is still alive at 12 years of age. Western blot analysis showed some Residual SUCLG1 protein in patient9s fibroblasts. Conclusions Our results suggest that SUCLG1 mutations that lead to complete absence of SUCLG1 protein are responsible for a very severe disorder with antenatal manifestations, whereas a SUCLA2 -like phenotype is found in patients with Residual SUCLG1 protein. Furthermore, it is shown that in the absence of SUCLG1 protein, no SUCLA2 protein is found in fibroblasts by western blot analysis. This result is consistent with a degradation of SUCLA2 when its heterodimer partner, SUCLG1, is absent.
Le S Guedardmereuze - One of the best experts on this subject based on the ideXlab platform.
-
the severity of phenotype linked to suclg1 mutations could be correlated with Residual Amount of suclg1 protein
Journal of Medical Genetics, 2010Co-Authors: Cecile Rouzier, Le S Guedardmereuze, Sylvie Tufferygiraud, Sylvie Bannwarth, C Caruba, Jeanluc Miro, Konstantina Fragaki, Annabelle Chaussenot, Elsebet OstergaardAbstract:Background Succinate-CoA ligase deficiency is responsible for encephalomyopathy with mitochondrial DNA depletion and mild methylmalonic aciduria. Mutations in SUCLA2 , the gene encoding a β subunit of succinate-CoA ligase, have been reported in 17 patients until now. Mutations in SUCLG1 , encoding the α subunit of the enzyme, have been described in two pedigrees only. Methods and findings In this study, two unrelated patients harbouring three novel pathogenic mutations in SUCLG1 were reported. The first patient had a severe disease at birth. He was compound heterozygous for a missense mutation (p.Pro170Arg) and a c.97+3G>C mutation, which leads to the complete skipping of exon 1 in a minigene expression system. The involvement of SUCLG1 was confirmed by western blot analysis, which showed absence of SUCLG1 protein in fibroblasts. The second patient has a milder phenotype, similar to that of patients with SUCLA2 mutations, and is still alive at 12 years of age. Western blot analysis showed some Residual SUCLG1 protein in patient9s fibroblasts. Conclusions Our results suggest that SUCLG1 mutations that lead to complete absence of SUCLG1 protein are responsible for a very severe disorder with antenatal manifestations, whereas a SUCLA2 -like phenotype is found in patients with Residual SUCLG1 protein. Furthermore, it is shown that in the absence of SUCLG1 protein, no SUCLA2 protein is found in fibroblasts by western blot analysis. This result is consistent with a degradation of SUCLA2 when its heterodimer partner, SUCLG1, is absent.
Sylvie Tufferygiraud - One of the best experts on this subject based on the ideXlab platform.
-
the severity of phenotype linked to suclg1 mutations could be correlated with Residual Amount of suclg1 protein
Journal of Medical Genetics, 2010Co-Authors: Cecile Rouzier, Le S Guedardmereuze, Sylvie Tufferygiraud, Sylvie Bannwarth, C Caruba, Jeanluc Miro, Konstantina Fragaki, Annabelle Chaussenot, Elsebet OstergaardAbstract:Background Succinate-CoA ligase deficiency is responsible for encephalomyopathy with mitochondrial DNA depletion and mild methylmalonic aciduria. Mutations in SUCLA2 , the gene encoding a β subunit of succinate-CoA ligase, have been reported in 17 patients until now. Mutations in SUCLG1 , encoding the α subunit of the enzyme, have been described in two pedigrees only. Methods and findings In this study, two unrelated patients harbouring three novel pathogenic mutations in SUCLG1 were reported. The first patient had a severe disease at birth. He was compound heterozygous for a missense mutation (p.Pro170Arg) and a c.97+3G>C mutation, which leads to the complete skipping of exon 1 in a minigene expression system. The involvement of SUCLG1 was confirmed by western blot analysis, which showed absence of SUCLG1 protein in fibroblasts. The second patient has a milder phenotype, similar to that of patients with SUCLA2 mutations, and is still alive at 12 years of age. Western blot analysis showed some Residual SUCLG1 protein in patient9s fibroblasts. Conclusions Our results suggest that SUCLG1 mutations that lead to complete absence of SUCLG1 protein are responsible for a very severe disorder with antenatal manifestations, whereas a SUCLA2 -like phenotype is found in patients with Residual SUCLG1 protein. Furthermore, it is shown that in the absence of SUCLG1 protein, no SUCLA2 protein is found in fibroblasts by western blot analysis. This result is consistent with a degradation of SUCLA2 when its heterodimer partner, SUCLG1, is absent.
