- 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