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1

Polymorphisms of the 5,10-methylenetetrahydrofolate and the methionine synthase reductase genes as independent risk factors for spina bifida

100%
Pietrzyk J. J., Bik-Multanowski M., Sanak M., Twardowska M.
Journal of Applied Genetics
|
2003
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vol. 44
|
issue 1
111-113
EN
We analyzed the role of the C677T polymorphism of the 5,10-methylenetetrahydrofolate and the A66G polymorphism of the methionine synthase reductase genes as risk factors for occurrence of spina bifida. The studied population included 106 mothers and 104 children from affected families, and a control group of 100 adults. We found statistically significant differences between the occurrence of the homozygosity in these polymorphisms in the groups of mothers and children with thoracolumbal defects (C677T polymorphism) and lumbosacral defects (A66G polymorphism). We postulate that these polymorphisms should be regarded as independent risk factors for spina bifida.
2

Molecular studies in osteogenesis imperfecta (OI). I. Clinical analysis of patients with osteogenesis imperfecta

100%
Pietrzyk J. J., Kruczek A., Sucharski P., Piatkowska E.
Journal of Applied Genetics
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1998
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vol. 39
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issue 4
331-348
EN
The goal of this study is to develop optimal diagnostic methods for osteogenesis imperfecta (OI), which will allow to distinguish familial from spontaneous cases and can be used in prenatal diagnostics as well. The paper summarizes the clinical part of the study, in which 69 families were analyzed. The families with OI were registered, their pedigrees were studied, a clinical classification of the disease was carried out and the dermatoglyphics of the affected patients were analyzed. Based on the above results a diagnostic algorithm was elaborated.
3

Molecular studies in osteogenesis imperfecta (OI). III. cDNA of COL1A1 and COL1A2 analysis using the BESS-T-Scan technique

88%
Sucharski P., Sanak M., Kostyk E., Pietrzyk J. J., Kruczek A.
Journal of Applied Genetics
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1998
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vol. 39
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issue 4
367-373
EN
A BESS-T-Scan analysis of cDNA COL1A1 and COL1A2 obtained by RT-PCR derived from five patients with sporadic forms of ostegenesis imperfecta was performed. The study was done in four patients with type I and one patient with type III OI. The analysis revealed the presence of structural changes in two regions of cDNA COL1A1 in two patients. No quantitative changes referring to COL1A2 gene were noted in any patient. The above analysis was the first application of the BESS-T-Scan technique in a molecular diagnosis of OI. The applied method seems to be useful and fulfil the basic criteria of the screening method to detect and locate mutations.
4

Two novel COL1A1 mutations in patients with osteogenesis imperfecta (OI) affect the stability of the collagen type I triple-helix

64%
Witecka J., Augusciak-Duma A. M., Kruczek A., Szydlo A., Lesiak M., Krzak M., Pietrzyk J. J., Mannikko M., Sieron A. L.
Journal of Applied Genetics
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2008
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vol. 49
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issue 3
283-295
EN
Osteogenesis imperfecta (OI) is a bone dysplasia caused by mutations in the COL1A1 and COL1A2 genes. Although the condition has been intensely studied for over 25 years and recently over 800 novel mutations have been published, the relation between the location of mutations and clinical manifestation is poorly understood. Here we report missense mutations in COL1A1 of several OI patients. Two novel mutations were found in the D1 period. One caused a substitution of glycine 200 by valine at the N-terminus of D1 in OI type I/IV, lowering collagen stability by 50% at 34?C. The other one was a substitution of valine 349 by phenylalanine at the C-terminus of D1 in OI type I, lowering collagen stability at 37.5?C. Two other mutations, reported before, changed amino residues in D4. One was a lethal substitution changing glycine 866 to serine in genetically identical twins with OI type II. That mutated amino acid was near the border of D3 and D4. The second mutation changed glycine 1040 to serine located at the border of D4 and D0.4, in a proband manifesting OI type III, and lowered collagen stability at 39?C (2?C lower than normal). Our results confirm the hypothesis on a critical role of the D1 and D4 regions in stabilization of the collagen triple-helix. The defect in D1 seemed to produce a milder clinical type of OI, whereas the defect in the C-terminal end of collagen type caused the more severe or lethal types of OI.
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