Release of Gelatinase from a Novel Secretory Compartment of Human Neutrophils

Dewald, Béatrice; Bretz, Ursula; Baggiolini, Marco

doi:10.1172/jci110643

Cited by 250 publications

(141 citation statements)

References 21 publications

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“…This is consistent with our findings with free ICs (11). That auranofin and sulfasalazine, at concentrations sufficient to prevent 90% of lysozyme release, inhibited gelatinase release by only 20-30% suggests that the 2 enzymes are under separate control, and supports the proposal that they are in different granules (27).…”

Section: Resultssupporting

confidence: 92%

“…Gelatinase contributes -30% to the GBM degradation by neutrophils (15,16). It is thought to reside in a separate secretory granule, the C-particle (27), although a recent report (28) suggests a specific granule origin. In contrast to the other enzymes measured, gelatinase release was not greatly altered in the presence of most of the drugs (Table 2).…”

Section: Resultsmentioning

confidence: 99%

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Inhibition of neutrophil‐mediated degradation of isolated basement membrane collagen by nonsteroidal antiinflammatory drugs that inhibit degranulation

Neal

Vissers

Winterbourn

1987

Arthritis & Rheumatism

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The ability of nonsteroidal antiinflammatory drugs to inhibit neutrophil-mediated degradation of type IV collagen in an in vitro tissue injury model using glomerular basement membrane (GBM) containing immune complexes was investigated. Auranofin (2.5-10 p.40, phenylbutazone (50-250 / . . & I ) , sulfasalazine (250-1,000 Eun), and 4-bromophenacyl bromide (5-20 luM) each inhibited up to 70% of the collagen degradation, in parallel with almost complete inhibition of the release of azurophil and specific granule enzymes. These drugs had much less an effect on gelatinase release. Indomethacin and the antimalarials, which inhibited the neutrophil oxidative burst but not degranulation, had little effect on GBM collagen degradation. Our results do not necessarily imply that inhibition of neutrophilmediated degradation of connective tissue is relevant to the action of nonsteroidal antiinflammatory drugs in vivo; however, using the GBM model system, we have shown that when a drug inhibits granule enzyme release, there is an associated decrease in collagen degradation, whereas inhibition of the oxidative burst has relatively little effect.Polymorphonuclear leukocytes (neutrophils) are prominent at sites of inflammation and are implicated as a cause of tissue injury (14). These cells

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Section: Resultssupporting

confidence: 92%

Section: Resultsmentioning

confidence: 99%

Inhibition of neutrophil‐mediated degradation of isolated basement membrane collagen by nonsteroidal antiinflammatory drugs that inhibit degranulation

Neal

Vissers

Winterbourn

1987

Arthritis & Rheumatism

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“…Antibodies against the protein were able to block fertilization of an ovum [23], indicating a role for sperm coating glycoprotein in the penetration by spermatozoa of the extracellular matrix-like zona pellucida, which surrounds the ovum. A role of SGP28 in degradation of the extracellular matrix during neutrophil migration is possible and suggested by its localization in specific granules, where other matrix degradative enzymes are stored [1][2][3]5]. The elucidation of the potential anti-microbial and matrix-degradative actions of SGP28 awaits its recombinant production.…”

Section: -Ementioning

confidence: 99%

“…Granules can be divided into peroxidase positive, azurophil granules and peroxidase negative granules, of which the latter encompass specific granules and gelatinase granules [2,3]. These granules are mobilized in a sequential order [4].…”

Section: Introductionmentioning

confidence: 99%

“…Exocytosis is an important aspect of neutrophil function. Peroxidase negative granule proteins like collagenase and gelatinase indirectly contribute to the microbicidal potential of the neutrophil by degrading extracellular matrix, thus allowing migration of the cell in tissues [2,3,5]. Other matrix proteins are directly involved in the killing of microorganisms, exemplified by cathepsin G, azurozidin, defensins, and bactericidal/permeability increasing protein, all of which are located in azurophil granules [1,6].…”

Section: Introductionmentioning

confidence: 99%

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SGP28, a novel matrix glycoprotein in specific granules of human neutrophils with similarity to a human testis‐specific gene product and to a rodent sperm‐coating glycoprotein

et al. 1996

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A novel 28 kDa glycoprotein was purified from exocytosed material from human nentrophils and its primary structure partially determined. Degenerate oligonucleotide primers were used to amplify cDNA clones from a human bone marrow cDNA library. The deduced 245 amino acid sequence of the 2124 bp full-length cDNA showed high degrees of similarity to the deduced sequences of the human gene TPX-1 and of sperm coating glycoprotein from rat and mouse. Subcellular fractionation of human neutrophils indicated that the protein is localized in specific granules. The protein was named SGP28 (specific granule protein of 28 kDa).Key words: TPX-1; Acidic epididymal glycoprotein; Pathogenesis related protein 1; Subcellular fractionation Materials and methods Purification of SGP28Isolated neutrophils were resuspended in Krebs-Ringer phosphate at approximately 5 x 108 cells/ml and preincubated at 37°C for 5 min. Phorbol myristate-acetate (PMA, Sigma) was added at 5 ~tg/ml and the neutrophils stimulated for 20 min. Protease inhibitors were added (phenylmethylsulfonylfluoride (1 mM), aprotinin (200 KIE/ml), pepstatin (1 mM)) and the cells pelleted by centrifugation. After precipitation in 18% PEG, removal of PEG from non-precipitated proteins by addition of 0.5 M K2HPO4, and a change of buffer to 0.05 M sodium acetate, the PEG supernatant was subjected to cation exchange-chromatography on Mono S using FPLC (Pharmacia) (all procedures as described in [8]). Fractions containing SGP28, as evaluated by SDS-PAGE, were pooled and re-chromatographed on MonoS and the eluate subjected to gel filtration on Superose 12 (Pharmacia), using 25 mM Tris-HCl, pH 8.0, 100 mM NaC1 as buffer.

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Effects of the aqueous fraction of the ethanol extract of the leaves ofCissampelos sympodialis eichl. in human neutrophils

1999

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An aqueous fraction (10–300 µg/mL) of the ethanol extract of the leaves of Cissampelos sympodialis Eichl inhibited N‐formyl‐Met‐Leu‐Phe (fMLP)‐induced release of lysozyme and myeloperoxidase from human neutrophils. Inhibition by the fraction, as well as by dibutyryl‐cAMP and prostaglandin E2, was substantially greater when the cells were pretreated with the phosphodiesterase (PDE) inhibitor isobutyl methyl xanthine (IBMX) indicating that the effect may be mediated by cAMP. Measurement of intracellular cAMP levels showed that the fraction (30–100 µg/mL) increased the nucleotide levels in IBMX‐pretreated neutrophils which was unaffected by propranolol. Cyclic AMP dependent protein kinase A activity was also increased by the fraction (1.5–100 µg/mL). Superoxide anion generation induced by fMLP in cytochalasin B‐treated cells primed with PAF was not inhibited by the aqueous fraction. The results indicate that the aqueous fraction of Cissampelos sympodialis inhibits neutrophil degranulation by a cAMP‐dependent mechanism which may be relevant to the use of the plant as an anti‐asthmatic agent in folk medicine. Copyright © 1999 John Wiley & Sons, Ltd.

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Release of Gelatinase from a Novel Secretory Compartment of Human Neutrophils

Cited by 250 publications

References 21 publications

Inhibition of neutrophil‐mediated degradation of isolated basement membrane collagen by nonsteroidal antiinflammatory drugs that inhibit degranulation

Inhibition of neutrophil‐mediated degradation of isolated basement membrane collagen by nonsteroidal antiinflammatory drugs that inhibit degranulation

SGP28, a novel matrix glycoprotein in specific granules of human neutrophils with similarity to a human testis‐specific gene product and to a rodent sperm‐coating glycoprotein

Effects of the aqueous fraction of the ethanol extract of the leaves ofCissampelos sympodialis eichl. in human neutrophils

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