Ewa Jablonska-Skwiecinska

Publications (4)7.81 Total impact

• Source

  Available from: Monika Maciag

  Article: Molecular analysis of three novel G6PD variants: G6PD Pedoplis-Ckaro, G6PD Piotrkow and G6PD Krakow.

  Monika Maciag, Danuta Plochocka, Ewa Jablonska-Skwiecinska, Ewa Mendek-Czajkowska, Ewa Golaszewska, Wojciech Strojny, Walentyna Balwierz, Ewa Zdebska, Beata Burzynska
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  ABSTRACT: We present three novel mutations in the G6PD gene and discuss the changes they cause in the 3-dimensional structure of the enzyme: 573C-->G substitution that predicts Phe to Leu at position 191 in the C-terminus of helix alphae, 851T-->C mutation which results in the substitution 284Val--> -->Ala in the beta+alpha domain close to the C-terminal part of helix alphaj, and 1175T-->C substitution that predicts Ile to Thr change at position 392.
  Acta biochimica Polonica 01/2007; 54(4):877-81. · 1.49 Impact Factor
• Article: Molecular and haematological studies of four families with hereditary spherocytosis resulting from band 3 deficiency.

  Monika Maciag, Danuta Plochocka, Ewa Mendek-Czajkowska, Anna Adamowicz-Salach, Justyna Spychalska, Ewa Zdebska, Ewa Jablonska-Skwiecinska, Jerzy Koscielak, Beata Burzynska
  Acta Haematologica 02/2006; 116(2):143-5. · 1.35 Impact Factor
• Article: Compound heterozygosity of two missense mutations in the NADH-cytochrome b5 reductase gene of a Polish patient with type I recessive congenital methaemoglobinaemia.

  Dorota Grabowska, Danuta Plochocka, Ewa Jablonska-Skwiecinska, Anna Chelstowska, Irmina Lewandowska, Krystyna Staniszewska, Zofia Majewska, Iwona Witos, Beata Burzynska
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  ABSTRACT: A case of type I methaemoglobinaemia observed in a Polish subject with compound heterozygosity for two mutations in the reduced nicotinamide adenine dinucleotide (NADH) cytochrome b5 reductase (b5R) gene is described. One is a novel mutation 647T-->C which leads to substitution of isoleucine by threonine at position 215 (I215T). This maternal mutation was found in several family members. A previously known mutation, 757G-->A, leads to the replacement of valine by methionine at position 252 (V252M). The latter mutation was found also in the father and one of the two brothers. The effects of these mutations were analysed on a model of the human b5R protein obtained by homology modelling. Although both amino acid substitutions are located in the NADH-binding domain, the whole protein structure, especially the region between the flavin adenine dinucleotide and NADH-binding domains, is disturbed. The structural changes in the I215T mutant are less prominent than those in the V252M mutant. We presume that the 647T-->C mutation is a type I mutation, however, it has not been observed in the homozygous state.
  European Journal Of Haematology 07/2003; 70(6):404-9. · 2.61 Impact Factor
• Article: A novel mutation in the glucose-6-phosphate dehydrogenase gene in a subject with chronic nonspherocytic hemolytic anemia--characterization of enzyme using yeast expression system and molecular modeling.

  Dorota Grabowska, Ewa Jablonska-Skwiecinska, Danuta Plochocka, Anna Chelstowska, Irmina Lewandowska, Iwona Witos, Zofia Majewska, Roma Rokicka-Milewska, Beata Burzynska
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  ABSTRACT: Glucose-6-phosphate dehydrogenase (G6PD) deficiency is the most common human enzymopathy. Human G6PD gene is highly polymorphic, with over 130 mutations identified, many of which cause hemolytic anemia. We studied a novel point mutation in the G6PD gene 1226 C-->G, predicting the proline 409 to arginine substitution (G6PD Suwalki). We expressed the human wild-type and mutated G6PD gene in yeast Saccharomyces cerevisiae which allowed the characterization of the Suwalki variant. We showed that human wild-type, as well as the mutated (1226 C-->G) G6PD gene, functionally complemented the phenotype displayed by the yeast strain with disruption of the ZWF1 gene (homologue of the human G6PD gene). Comparison of wild-type (wt) human G6PD purified from yeast and from blood shows no significant differences in the Km values for G6P and in the utilization rate for the substrate analogue, 2-deoxyG6P. The P409R substitution leads to drastic changes in G6PD kinetics. The specific activity as well as stability of mutated G6PD is also significantly reduced. Besides this, the effect of this mutation was analyzed using a model of the tertiary structure of the human enzyme. The localization of the P409R mutation suggests that it may influence the stability of the whole protein by changing tetramer interactions and disturbing the binding of structural NADP+.
  Blood Cells Molecules and Diseases 32(1):124-30. · 2.35 Impact Factor