Characterization of two azurphil granule proteases with active-site homology to neutrophil elastase.

Wilde, Craig G.; Snable, J L; Griffith, J E; Scott, Randy W.

doi:10.1016/s0021-9258(19)39936-3

Cited by 85 publications

(13 citation statements)

References 16 publications

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“…To improve protein integrity, we introduced three modifications into our nuclear extraction procedure. First, intact cells were incubated with DFP, a very strong covalent serine protease inhibitor which can traverse cell membranes (60). DFP was also included in the cell lysis buffer.…”

Section: Resultsmentioning

confidence: 99%

PEBP2/CBF, the Murine Homolog of the Human Myeloid AML1 and PEBP2β/CBFβ Proto-oncoproteins, Regulates the Murine Myeloperoxidase and Neutrophil Elastase Genes in Immature Myeloid Cells

Nuchprayoon

Meyers

Scott

et al. 1994

Molecular and Cellular Biology

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The myeloperoxidase (MPO) and neutrophil elastase genes are expressed specifically in immature myeloid cells. The integrity of a polyomavirus enhancer core sequence, 5'-AACCACA-3', is critical to the activity of the murine MPO proximal enhancer. This element binds two species, myeloid nuclear factors 1 alpha and 1 beta (MyNF1 alpha and -beta), present in 32D cl3 myeloid cell nuclear extracts. The levels of the MyNF1s increase during early 32D cl3 cell granulocytic differentiation. Both MyNF1 alpha and -beta supershift with an antiserum raised by using a peptide derived from the N terminus of polyomavirus enhancer-binding protein 2/core-binding factor (PEBP2/CBF) alpha subunit. The specific peptide inhibits these supershifts. In vitro-translated PEBP2/CBF DNA-binding domain binds the murine MPO PEBP2/CBF site. An alternate PEBP2/CBF consensus site, 5'-GACCGCA-3', but not a simian virus 40 enhancer core sequence, 5'-TTCCACA-3', binds the MyNF1s in vitro and activates a minimal murine MPO-thymidine kinase promoter in vivo. The murine neutrophil elastase gene 100-bp 5'-flanking sequences contain several functional elements, including potential binding sites for PU.1, C/EBP, c-Myb, and PEBP2/CBF. The functional element 5'-GGCCACA-3' located at positions -66 to 72 differs from the PEBP2/CBF consensus (5'-PuACCPuCA-3') only by an A-to-G transition at position 2. This DNA element binds MyNF1 alpha and -beta weakly. The N terminis of two PEBP2/CBF alpha subunit family members, PEBP2 alpha A and PEBP2 alpha B (murine AML1), are nearly identical, and 32D c13 cl3 cells contain both corresponding mRNAs. Since t(8;21), t(3;21), and inv(16), associated with myeloid leukemias, disrupt subunits of PEBP2/CBF, we speculate that the resulting oncoproteins, AML1-ETO, AML1-EAP, AML1-Evi1, and CBF beta-MYH11, inhibit early myeloid differentiation.

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Section: Resultsmentioning

confidence: 99%

PEBP2/CBF, the Murine Homolog of the Human Myeloid AML1 and PEBP2β/CBFβ Proto-oncoproteins, Regulates the Murine Myeloperoxidase and Neutrophil Elastase Genes in Immature Myeloid Cells

Nuchprayoon

Meyers

Scott

et al. 1994

Molecular and Cellular Biology

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“…Azurocidin is known to consist of at least three glycoisomers (16). The size heterogeneity we observed would explain the reported disparity between the molecular weights of azurocidin and CAP37 (3,9,16). Also, it may explain why CAP37 is reportedly a fairly minor azurophil granule protein but azurocidin is a major azurophil granule protein (3, 11).…”

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confidence: 83%

“…The neutrophil neutral serine proteases (NSP) are a family of antimicrobial glycoproteins. Four members of the NSP family have been identified in neutrophils: cathepsin G, leukocyte elastase, p29b, and azurocidin and the related or identical molecule CAP37 (azurocidin/CAP37) (3,8,9,12,16). The natural substrates for the enzymatically active NSP are unknown (15).…”

mentioning

confidence: 99%

“…Reminiscent of most granzymes from cytotoxic T cells (4), azurocidin is enzymatically inert, and its catalytic serine is replaced by glycine (16). CAP37, a molecule which exhibits amino-terminal-sequence homology with azurocidin (first 20 amino acids), is also enzymatically inert and possesses a serine substitution for the catalytic histidine (3,9).…”

mentioning

confidence: 99%

“…Both enzyme-dependent and enzyme-independent bactericidal activities are inhibited by plasma antiproteases (6). Azurocidin/CAP37 exhibits potent antimicrobial activities against nonoral bacteria (3,12,16), and we wanted to determine whether it exerted bactericidal effects against periodontal bacteria.…”

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confidence: 99%

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Human neutrophil azurocidin synergizes with leukocyte elastase and cathepsin G in the killing of Capnocytophaga sputigena

Miyasaki

Bodeau

1992

Infect Immun

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Azurocidin was purified in the presence of phenylmethylsulfonyl fluoride. Electrophoresis revealed at least seven species which exhibited N-terminal sequences consistent with azurocidin. Azurocidin exhibited no bactericidal activity against Capnocytophaga sputigena or other oral bacteria but synergized the bactericidal activity of enzymatically active elastase. Azurocidin also interacted synergistically with cathepsin G.

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Diagnostic value of aMMP‐8 and azurocidin in peri‐implant sulcular fluid as biomarkers of peri‐implant health or disease

Xanthopoulou,

Räisänen,

Sorsa

et al. 2024

Clinical & Exp Dental Res

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ObjectiveThe objective of this study was to investigate the effectiveness of testing for active matrix metalloproteinase‐8 (aMMP‐8) by a quantitative point‐of‐care (PoC), chairside lateral flow immunotest and azurocidin, in the peri‐implant sulcular fluid (PISF), as biomarkers for the presence or absence of peri‐implant diseases.BackgroundCurrent research indicates that proinflammatory cytokines and extracellular matrix‐degrading enzymes may be of value to diagnose and predict peri‐implant disease initiation and progression, but more data are needed.MethodsEighty patients with implants were recruited. PISF samples were collected and quantitatively analyzed for aMMP‐8 (chairside) and azurocidin with ELISA. Radiographic assessments and clinical indices (probing depth, probing attachment level, bleeding on probing, and plaque) were recorded after sampling. Kruskal‐Wallis test and pairwise post hoc Dunn‐Bonferroni test were used to relate aMMP‐8 levels and azurocidin levels to clinical parameters. The diagnostic ability of aMMP‐8 (ng/mL) and azurocidin was analyzed by receiver operator curve analysis. Area under the curve (AUC) was calculated and the Spearman's rho, and the coefficient of determination (R2) were used to calculate the correlations between aMMP‐8, azurocidin, and periodontal parameters.ResultsStatistically significant differences were observed for aMMP‐8 levels but not for azurocidin between healthy implants, implants with mucositis, and those with peri‐implantitis (13.65 ± 7.18, 32.33 ± 21.20, and 73.07 ± 43.93 ng/mL, respectively), (Kruskall–Wallis test p < .05). The aMMP‐8 test with a threshold of 20 ng/mL has a sensitivity of 71.7% and a specificity of 77.8% to identify peri‐implantitis and healthy implants, respectively. AUC was found to be 0.814, and the accuracy of the method reaches 73.8%. Above a cutoff value of 33.7 ng/mL of aMMP‐8, the accuracy of the test to detect peri‐implantitis reaches 77.5% in relation to 62.5% of BoP from the same site.ConclusionTaken collectively, present data indicate that the aMMP‐8 PoC lateral flow immunotest can be a beneficial, adjunctive diagnostic quantitative tool for real‐time screening for peri‐implant diseases.

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Characterization of two azurphil granule proteases with active-site homology to neutrophil elastase.

Cited by 85 publications

References 16 publications

PEBP2/CBF, the Murine Homolog of the Human Myeloid AML1 and PEBP2β/CBFβ Proto-oncoproteins, Regulates the Murine Myeloperoxidase and Neutrophil Elastase Genes in Immature Myeloid Cells

PEBP2/CBF, the Murine Homolog of the Human Myeloid AML1 and PEBP2β/CBFβ Proto-oncoproteins, Regulates the Murine Myeloperoxidase and Neutrophil Elastase Genes in Immature Myeloid Cells

Human neutrophil azurocidin synergizes with leukocyte elastase and cathepsin G in the killing of Capnocytophaga sputigena

Diagnostic value of aMMP‐8 and azurocidin in peri‐implant sulcular fluid as biomarkers of peri‐implant health or disease

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