TY  - JOUR
AU  - Heckmann, K.*
AU  - Iuso, A.
AU  - Reunert, J.*
AU  - Grueneberg, M.*
AU  - Seelhoefer, A.*
AU  - Rust, S.*
AU  - Fiermonte, G.*
AU  - Paradies, E.*
AU  - Piazzolla, C.*
AU  - Mannil, M.*
AU  - Marquardt, T.*
C1  - 73410
C2  - 56839
CY  - 111 River St, Hoboken 07030-5774, Nj Usa
TI  - Correction to “Expanding the genetic and clinicalspectrum of SLC25A42 associated disorders and testing ofpantothenic acid to improve CoA level in vitro”.
JO  - JIMD Rep.
VL  - 66
IS  - 2
PB  - Wiley
PY  - 2025
SN  - 2192-8304
ER  - 

TY  - JOUR
AB  - SLC25A42 encodes the mitochondrial coenzyme A (CoA) transporter localized at the inner mitochondrial membrane. SLC25A42 deficiency leads to a congenital disease with a heterogeneous clinical presentation, including myopathy, developmental delay, lactic acidosis, and encephalopathy. Twenty-one patients have been described so far. In the current study, we report on the identification of new biallelic variants in SLC25A42 in three siblings. Patients presented with symmetrical T2 hyperintensity of the putamen with minor volume depression at the brain MRI, elevated lactate, reduced oxygen consumption rates in muscle and fibroblasts, and reduced CoA levels in fibroblasts. Administration of pantothenic acid led to clinical stabilization and increased CoA levels in fibroblasts, thus confirming a role for SLC25A42 in energy metabolism and CoA homeostasis.
AU  - Heckmann, K.*
AU  - Iuso, A.
AU  - Reunert, J.*
AU  - Grüneberg, M.*
AU  - Seelhöfer, A.*
AU  - Rust, S.*
AU  - Fiermonte, G.*
AU  - Paradies, E.*
AU  - Piazzolla, C.*
AU  - Mannil, M.*
AU  - Marquardt, T.*
C1  - 72320
C2  - 56596
CY  - 111 River St, Hoboken 07030-5774, Nj Usa
SP  - 417-425
TI  - Expanding the genetic and clinical spectrum of SLC25A42-associated disorders and testing of pantothenic acid to improve CoA level in vitro.
JO  - JIMD Rep.
VL  - 65
IS  - 6
PB  - Wiley
PY  - 2024
SN  - 2192-8304
ER  - 

TY  - JOUR
AU  - Della Marina, A.*
AU  - Leiendecker, B.*
AU  - Roesch, S.*
AU  - Wortmann, S.B.
C1  - 59091
C2  - 48568
SP  - 10-11
TI  - Ketogenic diet for treating alopecia in BCS1l-related mitochondrial disease (Bjornstad syndrome).
JO  - JIMD Rep.
VL  - 53
IS  - 1
PY  - 2020
SN  - 2192-8304
ER  - 

TY  - JOUR
AB  - SLC25A42 is an inner mitochondrial membrane protein which has been shown to transport coenzyme A through a lipid bilayer in vitro. A homozygous missense variant in this gene has been recently reported in 13 subjects of Arab descent presenting with mitochondriopathy with variable clinical manifestations. By exome sequencing, we identified two additional individuals carrying rare variants in this gene. One subject was found to carry the previously reported missense variant in homozygous state, while the second subject carried a homozygous canonical splice site variant resulting in a splice defect. With the identification of two additional cases, we corroborate the association between rare variants in SLC25A42 and a clinical presentation characterized by myopathy, developmental delay, lactic acidosis, and encephalopathy. Furthermore, we highlight the biochemical consequences of the splice defect by measuring a mild decrease of coenzyme A content in SLC25A42-mutant fibroblasts.
AU  - Iuso, A.
AU  - Alhaddad, B.*
AU  - Weigel, C.*
AU  - Kotzaeridou, U.*
AU  - Mastantuono, E.
AU  - Schwarzmayr, T.
AU  - Graf, E.
AU  - Terrile, C.
AU  - Prokisch, H.
AU  - Strom, T.M.
AU  - Hoffmann, G.F.*
AU  - Meitinger, T.
AU  - Haack, T.B.*
C1  - 53683
C2  - 44949
SP  - 1–7
TI  - A homozygous splice site mutation in SLC25A42, encoding the mitochondrial transporter of coenzyme A, causes metabolic crises and epileptic encephalopathy.
JO  - JIMD Rep.
VL  - 44
PY  - 2018
SN  - 2192-8304
ER  - 

TY  - JOUR
AB  - Barth syndrome is known as a highly recognizable X-linked disorder typically presenting with the three hallmarks: (left ventricular non-compaction) cardiomyopathy, neutropenia, and 3-methylglutaconic aciduria. Furthermore, growth retardation, mild skeletal myopathy, and specific facial features as well as mitochondrial dysfunction in muscle are frequently seen. Underlying mutations are found in TAZ and lead to defective cardiolipin remodeling.Here, we report atypical clinical manifestations of TAZ mutations in two male patients initially presenting with growth retardation and very mild skeletal myopathy. As other phenotypic hallmarks were missing, Barth syndrome had not been suspected in these patients. One of them has been incidentally diagnosed in the frame of an in-depth cardiolipin research analysis, while the underlying genetic defect was unexpectedly identified in the second one by exome sequencing. CONCLUSION: These cases underline that TAZ mutations might well be an underdiagnosed cause of skeletal myopathy and growth retardation and do not necessarily manifest with the full clinical picture of Barth syndrome.
AU  - Thiels, C.*
AU  - Fleger, M.*
AU  - Huemer, M.-T.*
AU  - Rodenburg, R.J.*
AU  - Vaz, F.M.*
AU  - Houtkooper, R.H.*
AU  - Haack, T.B.
AU  - Prokisch, H.
AU  - Feichtinger, R.G.*
AU  - Lücke, T.*
AU  - Mayr, J.A.*
AU  - Wortmann, S.B.*
C1  - 47900
C2  - 39720
SP  - 89-93
TI  - Atypical clinical presentations of TAZ mutations: An underdiagnosed cause of growth retardation?
JO  - JIMD Rep.
PY  - 2016
SN  - 2192-8304
ER  - 

TY  - JOUR
AB  - ATP synthase or complex V (cV) of the oxidative phosphorylation system is responsible for the production of ATP, dissipating the electrochemical gradient generated by the mitochondrial respiratory chain. In addition to maternally transmitted cV dysfunction caused by mutations in mtDNA genes (MT-ATP6 or MT-ATP8), encoding cV subunits, recessive mutations in the nuclear TMEM70 are the most frequent cause of ATP synthase deficiency.We report on a cohort of ten Italian patients presenting with neonatal lactic acidosis, respiratory distress, hypotonia, cardiomyopathy and psychomotor delay and harbouring mutations in TMEM70, including the common splice mutation and four novel variants. TMEM70 protein was virtually absent in all tested TMEM70 patients' specimens.The exact function of TMEM70 is not known, but it is considered to impact on cV assembly since TMEM70 mutations have been associated with isolated cV activity reduction. We detected a clear cV biochemical defect in TMEM70 patients' fibroblasts, whereas the assay was not reliable in frozen muscle. Nevertheless, the evaluation of the amount of holocomplexes in patients with TMEM70 mutations showed a nearly absent cV in muscles and a strong decrease of cV with accumulation of sub-assembly species in fibroblasts. In our cohort we found not only cV deficiencies but also impairment of other OXPHOS complexes. By ultrastructural analysis of muscle tissue from one patient with isolated cV deficiency, we found a severely impaired mitochondrial morphology with loss of the cristae. These findings indicate that cV impairment could indirectly alter other respiratory chain complex activities by disrupting the mitochondrial cristae structure.
AU  - Diodato, D.*
AU  - Invernizzi, F.*
AU  - Lamantea, E.*
AU  - Fagiolari, G.*
AU  - Parini, R.*
AU  - Menni, F.*
AU  - Parenti, G.*
AU  - Bollani, L.*
AU  - Pasquini, E.*
AU  - Donati, M.A.*
AU  - Cassandrini, D.*
AU  - Santorelli, F.M.*
AU  - Haack, T.B.
AU  - Prokisch, H.
AU  - Ghezzi, D.*
AU  - Lamperti, C.*
AU  - Zeviani, M.*
C1  - 31213
C2  - 34207
SP  - 71-78 
TI  - Common and novel TMEM70 mutations in a cohort of Italian patients with mitochondrial encephalocardiomyopathy.
JO  - JIMD Rep.
VL  - 15
PY  - 2015
SN  - 2192-8304
ER  -