[The C1155G mutation of the red blood cell glucose-6-phosphate dehydrogenase gene in a subject with severe hereditary chronic nonspherocytic anaemia]. / Mutacja C1155G genu dehydrogenazy 6-glukozo-fosforanowej krwinek czerwonych u chorego z ciezka wrodzona niesferocytowa niedokrwistoscia hemolityczna.

UNLABELLED: THE AIM of the study is a genetic analysis of hereditary chronic nonspherocytic anaemia in a case, caused by mutation in the glucose-6-phosphate dehydrogenase gene. MATERIALS AND METHODS: The activity of G6PD enzyme was established. PCR method and DNA sequencing were implemented for molecular studies. Bioinformatic methods were used to check the effect of the mutation on the enzyme structure. RESULTS: Direct sequencing of g6pd gene revealed the presence of 1155 C > G mutation which results in cysteine to tryptophan substitution at position 385. Bioinformatic analysis established that this mutation may be responsible for protein destabilization. CONCLUSIONS: 1. G6PD deficiency should be considered in patients with haemolytic anaemia of unknown etiology. 2. Molecular tests are necessary, especially in cases of suspected mutation carriers in G6PD gene.

[A case of hereditary over-hydrated stomatocytosis with stomatospherocytes and spherocytes in the blood]. / Przypadek diedzicznej uwodnionej stomatocytozy z obecnoscia stomatosferocytów i sferocytów we krwi.

UNLABELLED: A patient of 31 years of age with an atypical overhydrated hereditary stomatocytosis is described. The diagnosis was established on the basis of a markedly increased red cell volume with low MCHC, high osmotic fragility of red cells, but increased binding of eosin-5-maleimide (EMA) to red cells, presence of stomatospherocytes and large spherocytes in blood and a high sodium and low potassium concentration in erythrocytes. A double band 7 was found by SDS-PAGE of the erythrocyte membrane, but even when only one them was taken into account, the level of stomatin was normal. Expression of stomatospherocytes in patient's blood was erratic: in blood films prepared in 2005, both stomatospherocytes and large spherocytes were present but in those from 2008 large erythrocytes of spherocyte morphology predominated. Clinically, the disease symptoms were typical for haemolytic anemia. When heparinized blood of the patient was kept at 0 degrees Celsius for 24 h, the haemolysis of red cells amounted only to 2%. The patient's son, 5 years old, suffers from the same disease. CONCLUSION: In spite of its rarity, hereditary stomatocytosis and allied disorders should be taken into consideration in differential diagnosis of haemolytic anemia including newborns. The diagnosis is supported by finding increased binding of eosin-5-maleimide (EMA) dye to patients' erythrocytes associated with their elevated osmotic fragility. Absence of a significant count of stomatocytes in the blood does not exclude the diagnosis of overyhydrated hereditary stomatocytosis.

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

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.

Paul-Bunnell antigen and a possible mechanism of formation of heterophile antibodies in patients with infectious mononucleosis.

Sera of patients with infectious mononucleosis contain heterophile anti-Paul- Bunnell (PB) antibodies to erythrocytes of numerous mammalian species. Evidence is presented that the corresponding antigen of bovine erythrocytes is not, as previously described, a single molecule, but a series of glycoproteins with glycans terminated with N-glycolylneuraminic acid (Neu5Gc). The latter compound should be an important part of the PB epitope because, in agreement with the results of others, we found that desialylation of the PB antigen abolishes almost completely its activity. We examined three different preparations of GM3 ganglioside for their capacity to bind anti-PB and found that only GM3 from horse erythrocytes containing Neu5Gc exhibited a low although ELISA measurable PB activity. The other two GM3 preparations, from bovine milk and dog erythrocytes, containing N-acetylneuraminic acid (Neu5Ac) bound little if any anti-PB antibodies. This finding confirms a previous report that human erythrocyte Neu5Ac containing sialoglycoprotein with similar O-linked glycans as the PB-antigen of bovine erythrocytes exhibits only very low PB activity (Patarca & Fletcher, 1995, Crit Rev Oncogen., 6: 305). In conclusion, we present a hypothesis that anti-PB antibodies in patients with infectious mononucleosis are formed against infection-induced cell membrane glycoconjugates containing highly immunogenic Neu5Gc.