Wyniki wyszukiwania

1

The use of sequential affinity chromatography for separation of human neutrophil elastase, cathepsin G and azurocidin

100%

Watorek W., Polanowski A., Wilusz T.

Acta Biochimica Polonica

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1996

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tom 43

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nr 3

Elastase, cathepsin G and azurocidin from human neutrophils are key components of body inflammatory defense. Perturbations in regulation of their activities lead to many serious pathological states. The paper describes a simple, fast and efficient method of joint purification of these proteins with the use of sequential affinity chromatography on squash trypsin inhibitor (CMTI I) and bovine pancreatic trypsin inhibitor (BPTI).

2

Analysis of individual azurocidin N-glycosylation sites in regard to its secretion by insect cells, susceptibility to proteolysis and antibacterial activity

84%

Indyk K., Olczak T., Ciuraszkiewicz J., Watorek W., Olczak M.

Acta Biochimica Polonica

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2007

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tom 54

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nr 3

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.

3

Azurocidin - inactive serine proteinase homolog acting as a multifunctional inflammatory mediator

84%

Watorek W.

Acta Biochimica Polonica

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2003

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tom 50

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nr 3

Azurocidin, also known as cationic antimicrobial protein 37 kDa (CAP37) or heparin-binding protein (HBP) is an inactive homolog of serine proteinases residing in granulocytes. The ability to cleave peptide bond was lost due to replacement of two of the three residues from the conserved catalytic triad characteristic for serine protein- ases. Azurocidin has a broad spectrum of antimicrobial activity, mainly against Gram-negative bacteria. It is also recognized as a multifunctional inflammatory mediator for its contracting effects on endothelial cells causing an increase of vascular permeability, capacity to bind endotoxin and ability to attract monocytes to inflammation sites.

Ograniczanie wyników

3 Acta Biochimica Polonica

3 Watorek W.

1 Ciuraszkiewicz J.

1 Indyk K.

1 Olczak M.

1 Olczak T.

1 Polanowski A.

1 Wilusz T.

1 2007

1 2003

1 1996

The use of sequential affinity chromatography for separation of human neutrophil elastase, cathepsin G and azurocidin

Analysis of individual azurocidin N-glycosylation sites in regard to its secretion by insect cells, susceptibility to proteolysis and antibacterial activity

Azurocidin - inactive serine proteinase homolog acting as a multifunctional inflammatory mediator