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  • Fellman, Vineta (författare)
  • Mitochondrial complex III deficiencies in the newborn infant.
  • 2006
  • Ingår i: Drug Discovery Today: Disease Mechanisms. - : Elsevier. - 1740-6765. ; 3:4, s. 421-427
  • Tidskriftsartikel (refereegranskat)abstract
    • New mechanisms for respiratory chain complex III diseases have recently been reported. Deletions, rearrangements and tRNA mutations of mitochondrial DNA cause deficiencies in several complexes. Mutations in the only complex III subunit encoded by mitochondrial DNA, cytochrome b, cause variable clinical phenotypes, such as cardiomyopathy or multisystemic dysfunction after birth. The homozygous serine78alanine mutation in the complex III assembling protein, BCS1L, causes a distinct phenotype, the GRACILE syndrome, whereas in other BCS1L mutations, the clinical picture is variable, but tubulopathy and liver dysfunction are typical.
  • Fellman, Vineta, et al. (författare)
  • Mitochondrial hepatopathies in the newborn period.
  • 2011
  • Ingår i: Seminars in Fetal & Neonatal Medicine. - : Elsevier. - 1878-0946. ; 16, s. 222-228
  • Tidskriftsartikel (refereegranskat)abstract
    • Mitochondrial disorders recognized in the neonatal period usually present as a metabolic crisis combined with one or several organ manifestations. Liver disorder in association with a respiratory chain deficiency may be overlooked since liver dysfunction is common in severely sick newborn infants. Lactacidosis, hypoglycemia, elevated serum transaminases and conjugated bilirubin are common signs of mitochondrial hepatopathy. Hepatosplenomegaly may occur in severe cases. A clinical picture with fetal growth restriction, postnatal lactacidosis, hypoglycemia, coagulopathy, and cholestasis, especially in combination with neurological symptoms or renal tubulopathy, should alert the neonatologist to direct investigations on mitochondrial disorder. A normal lactate level does not exclude respiratory chain defects. The most common liver manifestation caused by mutated mitochondrial DNA (deletion) is Pearson syndrome. Recently, mutations in several nuclear DNA genes have been identified that lead to mitochondrial hepatopathy, e.g. mitochondrial depletion syndrome caused by DGUOK, MPV17, SUCLG1, POLG1, or C10ORF2 mutations. A combination of lactacidosis, liver involvement, and Fanconi type renal tubulopathy is common when the complex III assembly factor BCS1L harbors mutations, the most severe disease with consistent genotype-phenotype correlation being the GRACILE syndrome. Mutations in nuclear translation factor genes (TRMU, EFG1, and EFTu) of the respiratory chain enzyme complexes have recently been identified. Diagnostic work-up of neonatal liver disorder should include assessment of function and structure of the complexes as well as mutation screening for known genes. So far, treatment is mainly symptomatic.
  • Fellman, Vineta (författare)
  • More voice, less noise in NICUs
  • 2017
  • Ingår i: Acta Paediatrica, International Journal of Paediatrics. - : Wiley-Blackwell. - 0803-5253. ; 106:8, s. 1210-1211
  • Tidskriftsartikel (övrigt vetenskapligt)
  • Fellman, Vineta, et al. (författare)
  • One-year survival of extremely preterm infants after active perinatal care in Sweden.
  • 2009
  • Ingår i: JAMA : the journal of the American Medical Association. - : American Medical Association. - 1538-3598 .- 0098-7484. ; 301:21, s. 2225-33
  • Tidskriftsartikel (refereegranskat)abstract
    • Up-to-date information on infant survival after extremely preterm birth is needed for assessing perinatal care services, clinical guidelines, and parental counseling.
  • Fellman, Vineta, et al. (författare)
  • Screening of BCS1L mutations in severe neonatal disorders suspicious for mitochondrial cause
  • 2008
  • Ingår i: Journal of Human Genetics. - : Springer. - 1434-5161. ; 53:6, s. 554-558
  • Tidskriftsartikel (refereegranskat)abstract
    • The BCS1L gene encodes a chaperone responsible for assembly of respiratory chain complex III (CIII). A homozygous point mutation (232A -> G) has been found as the genetic etiology for fetal growth retardation, amino aciduria, cholestasis, iron overload, lactic acidosis, and early death (GRACILE) syndrome (MIM 603358). Variable phenotypes have been found with other mutations. Our aim was to assess whether 232A -> G or other BCS1L mutations were present in infants (n = 21) of Finnish origin with severe, lethal disease compatible with mitochondrial disorder. A further aim was to confirm the GRACILE genotype-phenotype constancy (n = 8). Three new cases with homozygous 232A -> G mutation were identified; all had the primary GRACILE characteristics. No other mutations were found in the gene in other cases. All infants with GRACILE syndrome had the typical mutation. In conclusion, the rather homogenous population of Finns seems to have a specific BCS1L mutation that, as homozygous state, causes GRACILE syndrome, whereas other mutations are rare or not occurring. Thus, the novel clinical implication of this study is to screen for BCS1L mutations only if CIII is dysfunctioning or lacking Rieske protein, and to assess 232A -> G mutation in cases with GRACILE syndrome.
  • Fellman, Vineta, et al. (författare)
  • Severe neonatal MEGDHEL syndrome with a homozygous truncating mutation in SERAC1
  • 2022
  • Ingår i: Biochimica et Biophysica Acta - Molecular Basis of Disease. - : Elsevier. - 0925-4439. ; 1868:1
  • Tidskriftsartikel (refereegranskat)abstract
    • In the diagnostic work-up of a newborn infant with a metabolic crisis, lethal multiorgan failure on day six of life, and increased excretion of 3-methylglutaconic acid, we found using whole genome sequencing a homozygous SERAC1 mutation indicating MEGDHEL syndrome (3-methylglutaconic aciduria with deafness-dystonia, hepatopathy, encephalopathy, and Leigh-like syndrome). The SERAC1 protein is located at the contact site between mitochondria and the endoplasmic reticulum (ER) and is crucial for cholesterol trafficking. Our aim was to investigate the effect of the homozygous truncating mutation on mitochondrial structure and function. In the patient fibroblasts, no SERAC1 protein was detected, the mitochondrial network was severely fragmented, and the cristae morphology was altered. Filipin staining showed uneven localization of unesterified cholesterol. The calcium buffer function between cytoplasm and mitochondria was deficient. In liver mitochondria, complexes I, III, and IV were clearly decreased. In transfected COS-1 cells the mutant protein with the a 45-amino acid C-terminal truncation was distributed throughout the cell, whereas wild-type SERAC1 partially colocalized with the mitochondrial marker MT-CO1. The structural and functional mitochondrial abnormalities, caused by the loss of SERAC1, suggest that the crucial disease mechanism is disrupted interplay between the ER and mitochondria leading to decreased influx of calcium to mitochondria and secondary respiratory chain deficiency.
  • Gram, Magnus, et al. (författare)
  • The radical-binding lipocalin A1M binds to a Complex I subunit and protects mitochondrial structure and function.
  • 2013
  • Ingår i: Antioxidants & Redox Signaling. - : Mary Ann Liebert, Inc.. - 1557-7716. ; 18:16, s. 2017-2028
  • Tidskriftsartikel (refereegranskat)abstract
    • Aims: During cell death, energy-consuming cell degradation and recycling programs are performed. Maintenance of energy-delivery during cell death is therefore crucial but the mechanisms to keep the mitochondrial functions intact during these processes are poorly understood. We have investigated the hypothesis that the heme- and radical-binding ubiquitous protein A1M (α1-microglobulin) is involved in protection of the mitochondria against oxidative insult during cell death. Results: Using blood cells, keratinocytes and liver cells, we show that A1M binds with high affinity to apoptosis-induced cells and is localized to mitochondria. The mitochondrial Complex I subunit NDUFAB1 was identified as a major molecular target of the A1M-binding. Furthermore, A1M was shown to inhibit the swelling of mitochondria, and to reverse the severely abrogated ATP-production of mitochondria when exposed to heme and ROS. Innovation: Import of the radical- and heme-binding protein A1M from the extracellular compartment confers protection of mitochondrial structure and function during cellular insult. Conclusion: A1M binds to a subunit of Complex I and has a role in assisting the mitochondria to maintain its energy delivery during cell death. A1M may also, at the same time, counteract and eliminate the ROS generated by the mitochondrial respiration to prevent oxidative damage to surrounding healthy tissue.
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