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Sökning: L773:1096 7206

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1.
  • Aguiar, A., et al. (författare)
  • Practices in prescribing protein substitutes for PKU in Europe : No uniformity of approach
  • 2015
  • Ingår i: Molecular Genetics and Metabolism. - 1096-7192 .- 1096-7206. ; 115:1, s. 17-22
  • Tidskriftsartikel (refereegranskat)abstract
    • Background: There appears little consensus concerning protein requirements in phenylketonuria (PKU). Methods: A questionnaire completed by 63 European and Turkish IMD centres from 18 countries collected data on prescribed total protein intake (natural/intact protein and phenylalanine-free protein substitute [PS]) by age, administration frequency and method, monitoring, and type of protein substitute. Data were analysed by European region using descriptive statistics. Results: The amount of total protein (from PS and natural/intact protein) varied according to the European region. Higher median amounts of total protein were prescribed in infants and children in Northern Europe (n = 24 centres) (infants <1 year, >2-3 g/kg/day; 1-3 years of age, >2-3 g/kg/day; 4-10 years of age, >1.5-2.5 g/kg/day) and Southern Europe (n = 10 centres) (infants <1 year, 2.5 g/kg/day, 1-3 years of age, 2 g/kg/day; 4-10 years of age, 1.5-2 g/kg/day), than by Eastern Europe (n = 4 centres) (infants <1 year, 2.5 g/kg/day, 1-3 years of age, >2-2.5 g/kg/day; 4-10 years of age, >1.5-2 g/kg/day) and with Western Europe (n = 25 centres) giving the least (infants <1 year, >2-2.5 g/kg/day, 1-3 years of age, 1.5-2 g/kg/day; 4-10 years of age, 1-1.5 g/kg/day). Total protein prescription was similar in patients aged >10 years (1-1.5 g/kg/day) and maternal patients (1-1.5 g/kg/day). Conclusions: The amounts of total protein prescribed varied between European countries and appeared to be influenced by geographical region. In PKU, all gave higher than the recommended 2007 WHO/FAO/UNU safe levels of protein intake for the general population.
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  • Möllsten, Anna, et al. (författare)
  • A polymorphism in the angiotensin II type 1 receptor gene has different effects on the risk of diabetic nephropathy in men and women.
  • 2011
  • Ingår i: Molecular Genetics and Metabolism. - : Elsevier. - 1096-7192 .- 1096-7206. ; 103:1, s. 66-70
  • Tidskriftsartikel (refereegranskat)abstract
    • Background The etiology of diabetic nephropathy depends partly on genetic factors. Elevated systemic and intraglomerular blood pressure and glomerular filtration rate, partly regulated by the renin–angiotensin system, increase the risk of diabetic nephropathy. Methods The present case–control study investigated the association of the rs5186 polymorphism, in the angiotensin II type 1 receptor gene (AGTR1), with diabetic nephropathy. The study included 3561 patients with type 1 diabetes from Denmark, Finland, France and Sweden. Microalbuminuria was defined as albumin excretion rate (AER) ≥ 20 to < 200 μg/min or albumin concentration ≥ 30 to < 300 mg/l (n = 707), macroalbuminuria was defined as AER ≥ 200 μg/min or ≥ 300 mg/l (n = 1546), and patients with renal replacement therapy were also included in this group. The controls had > 15 years diabetes duration, AER < 20 μg/min or < 30 mg/l, and no antihypertensive treatment (n = 1308). Results AA genotype of the rs5186 polymorphism significantly increased the risk of diabetic nephropathy in male patients, OR = 1.27 (95% CI = 1.02–1.58), P = 0.03, adjusted for age at diabetes onset, HbA1c, diabetes duration, smoking and country of origin. Among the women, there were no significant associations between rs5186 and diabetic nephropathy, OR = 0.89 (0.71–1.11), P = 0.30. Conclusion We conclude that the AGTR1 gene may be associated with increased risk of diabetic nephropathy in men with type 1 diabetes.
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  • Möllsten, Anna, et al. (författare)
  • The endothelial nitric oxide synthase gene and risk of diabetic nephropathy and development of cardiovascular disease in type 1 diabetes
  • 2009
  • Ingår i: Molecular Genetics and Metabolism. - 1096-7192 .- 1096-7206. ; 97:1, s. 80-84
  • Tidskriftsartikel (refereegranskat)abstract
    • Nitric oxide (NO) is important in the maintenance of vascular tone and regulation of blood pressure. NO may also play a role in the development of both nephropathy and cardiovascular disease (CVD) in patients with diabetes. The susceptibility to nephropathy and CVD depends to some extent on genetic factors, therefore polymorphisms in the gene coding for endothelial NO-synthase, NOS3, can affect the risk of developing these diseases. Type 1 diabetes patients attending the Steno Diabetes Center, Denmark, between 1993 and 2001 were enrolled in this study. A total of 458 cases with diabetic nephropathy (albumin excretion >300 mg/24h) and 319 controls with persistent normoalbuminuria (<30 mg/24h), despite > or =20 years of diabetes duration at follow-up were identified. Patients were followed until death or end of the study. Associations between seven NOS3-gene polymorphisms and nephropathy, progression of nephropathy and CVD were studied. There was significant association between the rs743507 TT-genotype and diabetic nephropathy. When including age at diabetes onset, diabetes duration at follow-up, baseline Hb(A1c), sex and ever smoking in the analysis the OR was 1.43 (95% CI=1.03-2.00), P=0.035. In analyses of CVD development using Cox-regression the rs1799983 GG-genotype was a significant protective factor in normoalbuminuric patients, HR=0.32 (0.12-0.82), P=0.018, but not in patients with macroalbuminuria (covariates were; age at follow-up, baseline Hb(A1c), baseline systolic blood pressure, baseline cholesterol, sex and ever smoking). Our conclusion is that the NOS3-gene may be involved in the development of diabetic nephropathy in patients with type 1 diabetes and can be predictive of CVD during follow-up.
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  • Nakajima, Yoko, et al. (författare)
  • Dihydropyrimidinase deficiency in four East Asian patients due to novel and rare DPYS mutations affecting protein structural integrity and catalytic activity
  • 2017
  • Ingår i: Molecular Genetics and Metabolism. - 1096-7192 .- 1096-7206. ; 122:4, s. 216-222
  • Tidskriftsartikel (refereegranskat)abstract
    • Dihydropyrimidinase (DHP) is the second enzyme of the pyrimidine degradation pathway and catalyzes the ring opening of 5,6-dihydrouracil and 5,6-dihydrothymine. To date, only 31 genetically confirmed patients with a DHP deficiency have been reported and the clinical, biochemical and genetic spectrum of DHP deficient patients is, therefore, still largely unknown. Here, we show that 4 newly identified DHP deficient patients presented with strongly elevated levels of 5,6-dihydrouracil and 5,6-dihydrothymine in urine and a highly variable clinical presentation, ranging from asymptomatic to infantile spasm and reduced white matter and brain atrophy. Analysis of the DHP gene (DPYS) showed the presence of 8 variants including 4 novel/rare missense variants and one novel deletion. Functional analysis of recombinantly expressed DHP mutants carrying the p.M250I, p.H295R, p.Q334R, p.T418I and the p.R490H variant showed residual DHP activities of 2.0%, 9.8%, 9.7%, 64% and 0.3%, respectively. The crystal structure of human DHP indicated that all point mutations were likely to cause rearrangements of loops shaping the active site, primarily affecting substrate binding and stability of the enzyme. The observation that the identified mutations were more prevalent in East Asians and the Japanese population indicates that DHP deficiency may be more common than anticipated in these ethnic groups.
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  • Palm, Fredrik (författare)
  • Commentary on Wilcken et al. Asymmetric Dimethylarginine (ADMA) in Vascular and Renal Disease
  • 2007
  • Ingår i: Molecular Genetics and Metabolism. - 1096-7192 .- 1096-7206. ; 91:4, s. 308-
  • Tidskriftsartikel (refereegranskat)abstract
    • Wilcken and co-workers summarize our current knowledge about the role of asymmetric dimethylarginine (ADMA) as a key regulation of nitric oxide (NO) production, and examine the putative role of ADMA in the development of vascular and organ dysfunction [1]. Impaired NO production is closely associated with vascular dysfunction, especially during states of increased oxidative stress such as smoking, renal dysfunction requiring dialysis, hypertension and diabetes. Vallance et al. early identified increased ADMA levels in patients requiring dialysis, a state commonly associated with vascular dysfunction [2]. ADMA competitively inhibits NOS and competes with arginine for cellular uptake via the cationic amino acid-specific y+-system. Both mechanisms result in reduced NO production. ADMA levels are regulated by the interplay between the production by protein arginine methyltransferases (PRMTs), and the elimination by the metabolizing enzymes dimethylarginine dimethylaminohydrolase (DDAH) and, to a much lesser extent, by urinary excretion. However, as pointed out by the authors, numerous human studies have shown no beneficial effects of arginine supplementation, indicating a level of complexity for the regulation of ADMA levels that is not yet fully understood. The pioneering work by the authors themselves reveals a new mechanism that can explain some of these discrepancies. By showing that arginine directly inhibits DDAH in hepatic (HepG2) cells [3], they provide important information why arginine administration often fails to improve NO production. The knowledge about the cellular regulation of ADMA is constantly growing and will hopefully result in improved therapeutic strategies, especially for patients with vascular dysfunction due to impaired NO production.
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  • van Kuilenburg, André B P, et al. (författare)
  • Clinical, biochemical and genetic findings in two siblings with a dihydropyrimidinase deficiency
  • 2007
  • Ingår i: Molecular Genetics and Metabolism. - 1096-7192 .- 1096-7206. ; 91:2, s. 157-164
  • Tidskriftsartikel (refereegranskat)abstract
    • Dihydropyrimidinase (DHP) is the second enzyme of the pyrimidine degradation pathway and it catalyses the ring opening of 5,6-dihydrouracil and 5,6-dihydrothymine to N-carbamyl-beta-alanine and N-carbamyl-beta-aminoisobutyric acid, respectively. To date, only nine individuals have been reported suffering from a complete DHP deficiency. We report two siblings presenting with strongly elevated levels of 5,6-dihydrouracil and 5,6-dihydrothymine in plasma, cerebrospinal fluid and urine. One of the siblings had a severe delay in speech development and white matter abnormalities, whereas the other one was free of symptoms. Analysis of the DHP gene (DPYS) showed that both patients were compound heterozygous for the missense mutation 1078T>C (W360R) in exon 6 and a novel missense mutation 1235G>T (R412M) in exon 7. Heterologous expression of the mutant enzymes in Escherichia coli showed that both missense mutations resulted in a mutant DHP enzyme without residual activity. Analysis of the crystal structure of eukaryotic DHP from the yeast Saccharomyces kluyveri and the slime mold Dictyostelium discoideum suggests that the W360R and R412M mutations lead to structural instability of the enzyme which could potentially impair the assembly of the tetramer.
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9.
  • Wuolikainen, Anna, 1980-, et al. (författare)
  • ALS patients with mutations in the SOD1 gene have an unique metabolomic profile in the cerebrospinal fluid compared with ALS patients without mutations
  • 2012
  • Ingår i: Molecular Genetics and Metabolism. - : Elsevier. - 1096-7192 .- 1096-7206. ; 105:3, s. 472-478
  • Tidskriftsartikel (refereegranskat)abstract
    • A specific biochemical marker for early diagnosing and for monitoring disease progression in amyotrophic lateral sclerosis (ALS) will have important clinical applications. ALS is a heterogeneous syndrome with multiple subtypes with ill-defined borders. A minority of patients carries mutations in the Cu/Zn-superoxide dismutase (SOD1) gene but the disease mechanism remains unknown for all types of ALS. Using a GC-TOFMS platform we studied the cerebrospinal fluid (CSF) metabolome in 16 ALS patients with six different mutations in the SOD1 gene and compared with ALS-patients without such mutations. OPLS-DA was used for classification modeling. We find that patients with a SOD1 mutation have a distinct metabolic profile in the CSF. In particular, the eight patients homozygous for the D90A SOD1 mutation showed a distinctively different signature when modeled against ALS patients with other SOD1 mutations and sporadic and familial ALS patients without a SOD1 gene mutation. This was found irrespective of medication with riluzole and survival time. Among the metabolites that contributed most to the CSF signature were arginine, lysine, ornithine, serine, threonine and pyroglutamic acid, all found to be reduced in patients carrying a D90A SOD1 mutation. ALS-patients with a SOD1 gene mutation appear as a distinct metabolic entity in the CSF, in particular in patients with the D90A mutation, the most frequently identified cause of ALS. The findings suggest that metabolomic profiling using GC-TOFMS and multivariate data analysis may be a future tool for diagnosing and monitoring disease progression, and may cast light on the disease mechanisms in ALS.
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