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tom 14
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nr 2
EN
This is an introductory work of cyclic examination of lichenflora of Biebrza National Park. The area of the Emperor’s Road of Biebrza Lower Basin was examined. The presence of 92 species from 17 families was observed. The most numerous representatives were the Cladoniaceae family (21 taxons) and Lecanoraceae (15 taxons). Epiphytic lichens (59 species) were dominant among 4 ecological groups. The richest epiphytic flora was found in Populus tremula (26 species) and Populus nigra (12 species). Crust thalluses were the most representative morphological form with 43% of all described species. The examined area revealed 1 species, extinct in the rest of Poland, 12 dying out species, and 16 extinct-threatened species. The area of the Emperor’s Road can be qualified to the 7th zone of air purity as species of Usneaceae family occur there. Lichen collection was carried out in 2000-02. Taxonomy was based on standard methods used in lichenology. Identification was based on nomenclature by Fałtynowicz . Extinct-threatened species were chosen on the basis of “The Red List” by Cieśliński. The study of the Emperor’s Road lichenflora of Biebrza National Park is an introductory record for future comparative studies. It will also enable us to follow changes caused by an increase in anthropopressure and specifically air contamination.
EN
Three acidic glycosidases: β-galactosidase (β-GAL, EC 3.2.1.23), α-neuraminidase (NEUR, sialidase, EC 3.2.1.18), N-acetylaminogalacto-6-sulfate sulfatase (GALNS, EC 3.1.6.4) and serine carboxypepidase cathepsin A (EC 3.4.16.1) form a functional high molecular weight complex in the lysosomes. The major constituent of this complex is cathepsin A, the so-called “lysosomal protective protein” (PPCA). By forming a multienzyme complex, it protects the glycosidases from rapid intralysosomal proteolysis, and it is also required for the intracellular sorting and proteolytic processing of their precursors. In man, a deficiency of cathepsin A leads to a combined deficiency of β-GAL and NEUR activities, called “galactosialidosis”. Multiple mutations identified in the cathepsin A gene are the molecular basis of this lysosomal storage disease. This review describes the structural organization of the lysosomal high molecular weight multienzyme complex and the importance of the protective protein/cathepsin A in physiology and pathology.
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