Antibiotic proteins of human polymorphonuclear leukocytes.

Gabay, Joëlle E.; Scott, Randy W.; Campanelli, David; Griffith, J E; Wilde, Craig G.; Marra, Marian N.; Seeger, Mary; Nathan, Carl

doi:10.1073/pnas.86.14.5610

Cited by 253 publications

(177 citation statements)

References 24 publications

Supporting

Mentioning

169

Contrasting

Order By: Relevance

“…As demonstrated by ELISA, purified BPI reacted with monoclonal or polyclonal anti-BPI antibody, purified azurocidin reacted with rabbit anti-azurocidinpositive serum, and neither BPI nor azurocidin contained MPO, PR3, elastase, cathepsin G, lactoferrin or lysozyme based on reactivity with specific monoclonal or polyclonal antibodies. The first 20 N-terminal amino acid residues sequenced from the purified BPI and purified azurocidin were identical to the published sequences [16,17]: purified BPI sequence: VNPGVVVRISQKGL-DYASQQ; purified azurocidin sequence: IVGGRKARPRQFP-FLASIQN.…”

Section: Purity Of Bpi and Azurocidinmentioning

confidence: 63%

Frequency of anti-bactericidal/permeability-increasing protein (BPI) and anti-azurocidin in patients with renal disease

Jia

Tuttle

Falk

et al. 1996

Clinical and Experimental Immunology

View full text Add to dashboard Cite

SUMMARYThe major subtypes of anti-neutrophil cytoplasmic antibodies (ANCA) detected by indirect immunofluorescence assay (IFA) are P-ANCA and C-ANCA. In patients with vasculitis, myeloperoxidase (MPO) is the major P-ANCA antigen and proteinase 3 (PR3) is the major C-ANCA antigen. BPI and azurocidin, which are also called 57-kD cationic antimicrobial protein (CAP 57) and 37-kD cationic antimicrobial protein (CAP 37), respectively, have been proposed as less frequent target antigens for C-ANCA and P-ANCA. In patients with renal disease, we determined the frequency of antibodies against BPI and azurocidin. By IFA on alcohol-fixed neutrophils, monoclonal and polyclonal anti-BPI antibodies produced a C-ANCA pattern, whereas rabbit anti-azurocidin antibody produced a P-ANCA pattern. By ELISA, sera from 229 P-ANCA-positive patients, 99 C-ANCA-positive patients and 48 ANCA-negative (by IFA) patients with renal biopsies were tested for reactivity with recombinant human BPI and purified human azurocidin. Of these sera, 17 . 5% of P-ANCA, 30 . 3% of C-ANCA and 20 . 8% of IFA-ANCA-negative sera were positive for anti-BPI; and 8 . 3% of P-ANCA, 3 . 0% of C-ANCA and 8 . 3% of IFA-ANCA-negative sera were positive for anti-azurocidin. There was no statistical difference in frequency of anti-BPI between pauci-immune necrotizing and crescentic glomerulonephritis (NCGN) and other glomerular disease (OGD), and there was a lower frequency of antiazurocidin in NCGN samples than in OGD samples. By Western blot, anti-BPI-positive sera reacted with a 57-kD BPI band and anti-azurocidin-positive sera with a 29-kD azurocidin band. In conclusion, there is a low frequency of anti-BPI and anti-azurocidin antibodies in ANCA-positive patient sera; however, this does not correlate with NCGN, which is a marker for ANCA-associated small vessel vasculitis, and a similar positivity is found in IFA-ANCA-negative patients with renal disease. Therefore, serologic detection of anti-BPI and anti-azurocidin is not diagnostically specific in patients with renal disease.

show abstract

Section: Purity Of Bpi and Azurocidinmentioning

confidence: 63%

Frequency of anti-bactericidal/permeability-increasing protein (BPI) and anti-azurocidin in patients with renal disease

Jia

Tuttle

Falk

et al. 1996

Clinical and Experimental Immunology

View full text Add to dashboard Cite

show abstract

“…The neutrophil azurophil granule constituent proteinase 3 (PR3; EC 3.4.21.76) is a neutral serine protease with substantial amino acid sequence homology with elastase, cathepsin G and azurocidin [1][2][3]. PR3 has enzymatic activity for elastin, fibronectin and the basement membrane proteins collagen type IV and laminin [4].…”

Section: Introductionmentioning

confidence: 99%

“…Since activated neutrophils express PR3 on their surface [5], it could facilitate their migration through basement membranes. PR3 may be instrumental in host defense and regulation of proliferation and differentation of hematopoetic cells [2,6]. PR3 can also proteolytically process interleukin 8 into a chemotactically more potent form [7], and cleave the mammalian heat shock protein hsp28 [8].…”

Section: Introductionmentioning

confidence: 99%

Recombinant human proteinase 3, the Wegener's autoantigen, expressed in HMC‐1 cells is enzymatically active and recognized by c‐ANCA

Specks¹,

Fass²,

Fautsch³

et al. 1996

FEBS Letters

View full text Add to dashboard Cite

We developed a stable expression system for conformationally intact recombinant human PR3 (rPR3) using the human mast cell line HMC-I. Like in U937 cells, the rPR3 is processed from a 34 kDa precursor to the 29 kDa mature form, primarily as the result of oligosaccharide trimming. The rPR3 binds [3H]DFP and hydrolyzes the snbstrate N-methoxysuccinylAla-Ala-Pro-Val-pNA. The enzymatic activity is inhibited by greater than 95% by al-PI. The rPR3 and the enzymatically inactive mutant rPR3-S176A are both packaged in granules. Thus, proteolytic autoprocessing is not required for PRYs targeting to granules. This rPR3 is the first to be recognized by most c-ANCA from WG patients and all anti-PR3 ANCA that were detected by standard anti-PR3 specific ELISA. This expression system for rPR3 represents a versatile tool for the analysis of its intraceHular processing, structure-function relationships and interaction with autoantibodies.

show abstract

“…Heparin-binding protein (HBP), also termed CAP37 [1] and azurocidin [2], is a human neutrophil-derived serine protease homologue exhibiting 45% sequence identity to neutrophil elastase, and 30-37% identity to several other granule serine proteases [3,4]. Despite these similarities, HBP is devoid of proteolytic activity because the active site residues serine and histidine have been replaced.…”

Section: Introductionmentioning

confidence: 99%

“…Despite these similarities, HBP is devoid of proteolytic activity because the active site residues serine and histidine have been replaced. Beside its lipopolysaccharide (LPS) binding capacity and antimicrobial action [2,5], HBP has been shown to be a specific and strong chemoattractant for monocytes in vitro and to induce longevity and differentiation of these cells towards a macrophage phenotype [1,3]. In addition, HBP has been shown to induce detachment and homotypic aggregation on confluent monolayers of endothelial cells and fibroblasts [6].…”

Section: Introductionmentioning

confidence: 99%

Characterization of recombinant human HBP/CAP37/azurocidin, a pleiotropic mediator of inflammation‐enhancing LPS‐induced cytokine release from monocytes

et al. 1996

View full text Add to dashboard Cite

Antibiotic proteins of human polymorphonuclear leukocytes.

Cited by 253 publications

References 24 publications

Frequency of anti-bactericidal/permeability-increasing protein (BPI) and anti-azurocidin in patients with renal disease

Frequency of anti-bactericidal/permeability-increasing protein (BPI) and anti-azurocidin in patients with renal disease

Recombinant human proteinase 3, the Wegener's autoantigen, expressed in HMC‐1 cells is enzymatically active and recognized by c‐ANCA

Characterization of recombinant human HBP/CAP37/azurocidin, a pleiotropic mediator of inflammation‐enhancing LPS‐induced cytokine release from monocytes

Contact Info

Product

Resources

About