The Isolation of a Neutral Proteinase from the Urine of a Patient with Goodpasture's Syndrome

Davies, Malcolm; Sanders, E.; Coles, Gerald A.; Hughes, Kelvin T.

doi:10.1042/bst0060947

Cited by 2 publications

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“…Clinically 12 of the 13 patients had acute or rapidly progressive glomerular disease, severe proliferative changes and evidence of PMN infiltration. The urinary neutral proteinase in one of the patients with Goodpasture's disease was purified and shown to be identical to PMN elastase in respect to Mr, substrate specificity and inhibitor profile [7]. These findings support the important contribution of PMN neutral proteinases to the induction of proteinuria in clinical forms of nephritis.…”

Section: (Ii) Proteolytic Destruction By Serine Proteinasesmentioning

confidence: 86%

Proteinases and the glomerulus: Their role in glomerular diseases

Davies¹,

Coles²,

Thomas³

et al. 1990

Klin Wochenschr

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Degradation of matrix in normal glomeruli occurs through the action of neutral metalloproteinases which are in turn regulated by specific inhibitors. Both of these proteins are secreted by mesangial cells. Macrophages and IL-1 enhance the secretion of the proteinase. Decreased production of the metalloproteinase and for increased secretion of its inhibitor may lead to matrix accumulation. Neutrophil serine paternases degrade glomerular basement membrane (GBM) in vitro. In both animal and human disease urine excretion of these enzymes is accompanied by proteinuria and the presence of GBM-fragments. Further knowledge of the processes involved in matrix degradation may lead to improved therapy of glomerular disease.

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Section: (Ii) Proteolytic Destruction By Serine Proteinasesmentioning

confidence: 86%

Proteinases and the glomerulus: Their role in glomerular diseases

Davies¹,

Coles²,

Thomas³

et al. 1990

Klin Wochenschr

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“…Characterization of proteinases found in the urine from one patient with Goodpastures's syndrome [3] as well as from patients with severe proliferative glomerulonephritis [2] by testing their activity against specific substrates and their ability to degrade GBM also in vitro showed them to be neutral pro teinases with the properties of elastase and cathepsin G [2,3]. But which enzymes un derlie GBM degradation is by far not fully understood at present.…”

mentioning

confidence: 99%

Proteolytic Degradation of the Glomerular Basement Membrane and Immunochemical Characterization of Split Products

Lübec¹,

O²,

Coradello³

et al. 1980

Kidney Blood Press Res

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Glomerular basement membranes (GBM) were isolated and subjected to enzymatic degradation with the protease trypsin (Serva), chymotrypsin (Serva), papain (Sigma), pepsin (Serva) and collagenase (Worthington) as well as a lysosomal preparation from glass adherent rat blood and peritoneal exudate cells. Split products were characterized by immunoelectrophoresis and cellulose acetate electrophoresis. Urine was obtained from healthy rats and rats with Masugi’s experimental glomerulonephritis, dialyzed and concentrated and applied on immunoelectrophoresis, using anti-GBM antibody from rabbit. Urinary GBM split products from healthy and nephritic rats showed two precipitation lines like digestion products obtained after chymotrypsin degradation. This finding was supported by characterizing individual antigenic degradation products obtained after inhibition of GBM degradation by the lysosomal preparation with ethylenediaminetetraacetic acid and Trasylol alone and in combination, as well as with o-phenanthrolin. It is concluded that GBM-antigens excreted into urine indicate limited digestion of GBM by chymotrypsin-type protease.

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The Isolation of a Neutral Proteinase from the Urine of a Patient with Goodpasture's Syndrome

Cited by 2 publications

References 0 publications

Proteinases and the glomerulus: Their role in glomerular diseases

Proteinases and the glomerulus: Their role in glomerular diseases

Proteolytic Degradation of the Glomerular Basement Membrane and Immunochemical Characterization of Split Products

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