Barriers to start the physical activity among seniors living in lesser Poland

Society of our civilization is aging. People are living longer and therefore the number of older people increases thus it becomes important not only a long life, but above all, the quality of life. The quality of life which depends mainly on care for health, physical activity including their lifestyles. Physical activity is seen as one of the most important factors of human health. This article aims at analysing the structure of physical activity among seniors living in Lesser Poland as well as the barriers of starting such activity. The research was conducted within the scope of the PolSenior nationwide programme, financed in the form of a grant by the Ministry of Science and Higher Education (ref. no. PBZ-MEIN-9/2/2006). The sample selection of respondents had a random character (of three-stage process). The study used some of the results – survey data of 157 men and 187 women of 65+ years of age, inhabitants of the province of Lesser Poland. The results were analysed in terms of the three age groups: 65–74, 75–84 and over 85 years; of age and gender, place of residence due to the number of inhabitants (20 thousand / over 20 thousand) as well as socio – professional status (blue-collar workers / non-physical workers). The most common barrier to start physical activity for seniors surveyed in the region are considerations of health and mental condition

Glycoprotein Hypersecretion Alters the Cell Wall in Trichoderma reesei Strains Expressing the Saccharomyces cerevisiae Dolichylphosphate Mannose Synthase Gene

Expression of the Saccharomyces cerevisiae DPM1 gene (coding for dolichylphosphate mannose synthase) in Trichoderma reesei (Hypocrea jecorina) increases the intensity of protein glycosylation and secretion and causes ultrastructural changes in the fungal cell wall. In the present work, we undertook further biochemical and morphological characterization of the DPM1-expressing T. reesei strains. We established that the carbohydrate composition of the fungal cell wall was altered with an increased amount of N-acetylglucosamine, suggesting an increase in chitin content. Calcofluor white staining followed by fluorescence microscopy indicated changes in chitin distribution. Moreover, we also observed a decreased concentration of mannose and alkali-soluble β-(1,6) glucan. A comparison of protein secretion from protoplasts with that from mycelia showed that the cell wall created a barrier for secretion in the DPM1 transformants. We also discuss the relationships between the observed changes in the cell wall, increased protein glycosylation, and the greater secretory capacity of T. reesei strains expressing the yeast DPM1 gene

Abnormalities of erythrocyte glycoconjugates are identical in two families with congenital dyserythropoietic anemia type II with different chromosomal localizations of the disease gene.

We analyzed erythrocyte glycoconjugates in two families with congenital dyserythropoietic anemia type II (CDA-II): family 2 with the typical localization of the disease gene to chromosome 20q11.2 and family 1 in which this localization was excluded. Despite the different genetics, the erythrocyte glycoconjugate abnormalities in the two families were identical suggesting a complex inheritance of CDA-II. We also found that erythrocyte anion exchanger 1 protein is decreased in CDA-II homozygotes and obligate carriers alike

Abnormalities of erythrocyte glycoconjugates are identical in two families with congenital dyserythropoietic anemia type II with different chromosomal localizations of the disease gene

We analyzed erythrocyte glycoconjugates in two families with congenital dyserythropoietic anemia type II (CDA-II): family 2 with the typical localization of the disease gene to chromosome 20q11.2 and family 1 in which this localization was excluded. Despite the different genetics, the erythrocyte glycoconjugate abnormalities in the two families were identical suggesting a complex inheritance of CDA-II. We also found that erythrocyte anion exchanger 1 protein is decreased in CDA-II homozygotes and obligate carriers alike