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Wyszukujesz frazę "Olczak, Teresa" wg kryterium: Autor


Wyświetlanie 1-2 z 2
Tytuł:
Subcellular localization of UDP-GlcNAc, UDP-Gal and SLC35B4 transporters
Autorzy:
Maszczak-Seneczko, Dorota
Olczak, Teresa
Olczak, Mariusz
Powiązania:
https://bibliotekanauki.pl/articles/1039897.pdf
Data publikacji:
2011
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
MDCK-RCAr
nucleotide sugar transporter
Golgi apparatus
endoplasmic reticulum
Opis:
The mechanisms of transport and distribution of nucleotide sugars in the cell remain unclear. In an attempt to further characterize nucleotide sugar transporters (NSTs), we determined the subcellular localization of overexpressed epitope-tagged canine UDP-GlcNAc transporter, human UDP-Gal transporter splice variants (UGT1 and UGT2), and human SLC35B4 transporter splice variants (longer and shorter version) by indirect immunofluorescence using an experimental model of MDCK wild-type and MDCK-RCAr mutant cells. Our studies confirmed that the UDP-GlcNAc transporter was localized to the Golgi apparatus only and its localization was independent of the presence of endogenous UDP-Gal transporter. After overexpression of UGT1, the protein colocalized with the Golgi marker only. When UGT2 was overexpressed, the protein colocalized with the endoplasmic reticulum (ER) marker only. When UGT1 and UGT2 were overexpressed in parallel, UGT1 colocalized with the ER and Golgi markers and UGT2 with the ER marker only. This suggests that localization of the UDP-Gal transporter may depend on the presence of the partner splice variant. Our data suggest that proteins involved in nucleotide sugar transport may form heterodimeric complexes in the membrane, exhibiting different localization which depends on interacting protein partners. In contrast to previously published data, both splice variants of the SLC35B4 transporter were localized to the ER, independently of the presence of endogenous UDP-Gal transporter.
Źródło:
Acta Biochimica Polonica; 2011, 58, 3; 413-419
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Analysis of individual azurocidin N-glycosylation sites in regard to its secretion by insect cells, susceptibility to proteolysis and antibacterial activity
Autorzy:
Indyk, Katarzyna
Olczak, Teresa
Ciuraszkiewicz, Justyna
Wątorek, Wiesław
Olczak, Mariusz
Powiązania:
https://bibliotekanauki.pl/articles/1041040.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
glycosylation
protein secretion
azurocidin
antimicrobial activity
Opis:
Azurocidin is an inactive serine protease homolog with primary sequence similarity to neutrophil elastase, cathepsin G, and proteinase 3. The aim of this study was to investigate possible consequences of differential glycosylation of azurocidin in regard to its secretion, protein stability as measured by susceptibility to proteolysis, and antibacterial activity. Site-directed mutagenesis was employed to generate mutant azurocidin variants lacking individual N-glycosylation sites. Our results show that N-linked glycans may play a role in proper azurocidin folding and subsequent secretion by insect cells. We also demonstrate that N-linked glycosylation contributes to azurocidin stability by protecting it from proteolysis. The lack of N-glycosylation at individual sites does not significantly influence the azurocidin antibacterial activity.
Źródło:
Acta Biochimica Polonica; 2007, 54, 3; 567-573
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-2 z 2

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