A rapid method of purification of human granulocyte cationic neutral proteases: purification and further characterization of human granulocyte elastase

Feinstein, Gad; Janoff, Aaron

doi:10.1016/0005-2744(75)90077-7

Cited by 74 publications

(23 citation statements)

References 16 publications

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“…MPO and NE were isolated from purulent sputum as described previously (21,22). L F purified from human milk was obtained from Sigma (St. Louis, MO).…”

Section: Methodsmentioning

confidence: 99%

Antilactoferrin antibodies in patients with rheumatoid arthritis are associated with vasculitis

Coremans

Hagen

Daha

et al. 1992

Arthritis & Rheumatism

127

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Objective. To determine the occurrence of antineutrophil cytoplasmic antibodies (ANCA) and the specificity of these antibodies (Ab) in serum from patients with rheumatoid arthritis (RA) and patients with rheumatoid arthritis complicated by vasculitis (rheumatoid vasculitis [RV]).Methods. ANCA was detected with an indirect immunofluorescence test on ethanol-fixed granulocytes. Ab against the cytoplasmic antigens proteinase-3, elastase, lactoferrin (LF), and myeloperoxidase were measured by enzyme-linked immunosorbent assay.Results. ANCA were found in the serum of 43% of 49 patients with RV and in 36% of 50 patients with RA. Anti-LF Ab occurred more frequently in RV patients (45%) than in RA patients (4%), whereas reactivity against the other cytoplasmic antigens did not differ significantly between these groups.

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“…MPO and NE were isolated from purulent sputum as described previously (21,22). L F purified from human milk was obtained from Sigma (St. Louis, MO).…”

Section: Methodsmentioning

confidence: 99%

Antilactoferrin antibodies in patients with rheumatoid arthritis are associated with vasculitis

Coremans

Hagen

Daha

et al. 1992

Arthritis & Rheumatism

127

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“…PGS was dissolved in 0.4 M NaOH and kept at room temperature for 24 h. After neutralization with dilute HCl and dialysis against distilled water, the free chondroitin sulfate chains were isolated by DEAE-cellulose chromatography, as described previously (13 PMN granule enzymes and inhibitors. The preparation of G and the isolation of E and CT and their properties have been described in detail previously (15)(16)(17). The activity of the preparation of E used in these studies on tertiary-butyloxyl-carbamyl L-alanine paranitrophenyl ester was 6.9 /umol/min/mg protein, and the activity of the CT preparation on benzoyl tyrosine ethyl ester was 11.0 /hmol/ min/mg protein.…”

Section: Methodsmentioning

confidence: 99%

Degradation of cartilage proteoglycan by human leukocyte granule neutral proteases--a model of joint injury. II. Degradation of isolated bovine nasal cartilage proteoglycan.

Keiser¹,

Greenwald²,

Feinstein³

et al. 1976

J. Clin. Invest.

134

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A B S T R A C T Extracts of human peripheral blood polymorphonuclear leukocyte granules, and two purified proteases derived from such extracts, an elastase and a chymotrypsin-like enzyme, degrade isolated bovine nasal cartilage proteoglycan at neutral pH. Viscosity studies indicate that the leukocyte granule extracts lack hyaluronidase activity and that their degradative effect on proteoglycan at physiological pH is due entirely to proteolytic action. Sepharose 4B gel chromatography and SDS-polyacrylamide gel electrophoresis of proteoglycan fractions treated with leukocyte granule enzymes at pH 7.0 indicate that they degrade one of the proteoglycan link proteins, release a fragment from the hyaluronic acid-binding portion of the proteoglycan subunit core protein, and break down the remainder of the proteoglycan subunit molecule into peptide fragments with varying numbers of chondroitin sulfate chains. Immunodiffusion studies indicate that the antigenic determinants of the proteoglycan subunit core protein and the link proteins survive treatment with granule proteases. Similar degradation of human articular cartilage proteoglycan by granule neutral proteases can be presumed to occur, in view of the similarity of structure of human articular and bovine nasal cartilage proteoglycans. The release of granule enzymes in the course of neutrophil-mediated inflammation can thus result in the Dr. Feinstein's permanent address is:

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“…The first of these enzymes, PMN E, was originally described by one of the present authors (16,28,29), who also demonstrated its activity against synthetic E substrates (27, 30). Purification of the E (17, 21, 31-33) and its subsequent characterization ( 17,21,22,33) have revealed that this PMN enzyme has a mol wt between 25,000 and 35,000 daltons and is a highly basic glycoprotein. The second enzyme, PMN chymotrypsin (CT), has been described by several laboratories (22,23,34), and this enzyme has also been purified recently (18,24,35).…”

Section: Discussionmentioning

confidence: 99%

“…The rabbit antiserum to E that we used in these experiments gave a single p)recipitin line of identity when reacted against E and G in double immunodiffusion tests, but it failed to react against any other component of G. It was also found to be monospecific for E when tested against serial extracts of acrylamide gel electrophoretograms of G. The preparation and characterization of this antiserum has been reported in greater detail elsewhere (17). The same antiserum was used for two different purposes in these experiments.…”

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confidence: 81%

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Degradation of cartilage proteoglycan by human leukocyte granule neutral proteases--a model of joint injury. I. Penetration of enzyme into rabbit articular cartilage and release of 35SO4-labeled material from the tissue.

Janoff¹,

Feinstein²,

Malemud³

et al. 1976

J. Clin. Invest.

120

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A B S T R A C T The present work was undertaken to explore the effect of two purified neutral proteases derived from human peripheral blood polymorphonuclear leukocytes (PMN) on articular cartilage as a model of joint injury. Human leukocyte elastase and chymotrypsin-like enzyme, purified by affinity chromatography, released 'SO4 from labeled rabbit articular cartilage slices in vitro. Release of isotope was initially delayed, suggesting that either a lag in enzyme penetration occurs or that size of degradation fragments is a limiting factor in diffusion of label out of the tissue. The release of 'SO4 was inhibited by preincubation of elastase and chymotrypsin-like enzyme with human alpha 1-antitrypsin, or with their specific chloromethyl ketone inactivators, and the action of elastase was also inhibited by a monospecific antiserum to PMN elastase, freed of major serum proteinase inhibitors. Immunohistochemical staining procedures revealed the presence of PMN elastase inside the matrix of cartilage slices after a 20-min exposure of tissue to either the pure enzyme or crude PMN granule extract. Serum alpha 1-antitrypsin failed to penetrate into the cartilage slices under identical in vitro conditions. In association with the results reported in the accompanying paper, these findings suggest a model of cartilage matrix degradation by PMN neutral proteases in which local protease-antiprotease imbalance, coupled with different rates of penetration of protease and antiprotease into target tissue, plays a key role in accounting for matrix damage.Dr. Feinstein's permanent address is:

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A rapid method of purification of human granulocyte cationic neutral proteases: purification and further characterization of human granulocyte elastase

Cited by 74 publications

References 16 publications

Antilactoferrin antibodies in patients with rheumatoid arthritis are associated with vasculitis

Antilactoferrin antibodies in patients with rheumatoid arthritis are associated with vasculitis

Degradation of cartilage proteoglycan by human leukocyte granule neutral proteases--a model of joint injury. II. Degradation of isolated bovine nasal cartilage proteoglycan.

Degradation of cartilage proteoglycan by human leukocyte granule neutral proteases--a model of joint injury. I. Penetration of enzyme into rabbit articular cartilage and release of 35SO4-labeled material from the tissue.

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