Characterization of a latent cysteine proteinase from ascitic fluid as a high molecular weight form of cathepsin B

Mort, John S.; Leduc, Michèle; Recklies, Anneliese D.

doi:10.1016/0304-4165(83)90240-4

Cited by 68 publications

(32 citation statements)

References 19 publications

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“…In order to test whether the M r 42 000 species did actually constitute a latent -but activatable reservoir of proteolytically active cathepsin B, we treated a series of synovial fluid samples with pepsin, essentially according to the protocols described in previous work (23,24). Figure 3 records the levels of these latent activities.…”

Section: Resultsmentioning

confidence: 99%

“…2, lane 1) complete with the generation of the new species M r 20000. The detection and characterisation, üsing antibodies raised against active human cathepsin B, of latent forms of the proteinase has been previously reported, malignant asoites cells in culture aire known to produce a M r 40 000 proform of the enzyme which can be converted into a M r 33 000 species by pepsin activation (24).…”

Section: Iminunological Characterisation Of Cathepsin B-like Speciesmentioning

confidence: 99%

“…As pepsin-activatable precursor forms of cathepsin B-like proteinases have been detected in such fluids s ascitic fluid from patients with ovarian cancer (23,24) and in medium conditioned by tumour breast cancer cells in culture (15). The activation protocol described by these workers was applied to the synovial fluid samples in order to reveal any latent cathepsin B precursors that may have been present.…”

Section: Pepsin Activationmentioning

confidence: 99%

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The Detection, Quantification and Partial Characterisation of Cathepsin B-Like Activity in Human Pathological Synovial Fluids

Duffy¹,

Walker²,

Guthrie³

et al. 1994

CCLM

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Summary:In this study, the levels of the cysteine proteinase -cathepsin B were measured in diseased synovial fluids using a steady state fluorometric assay. Cathepsin B-like activity was shown to be present in all the samples analysed, with the rheumatoid arthritic synovial fluids possessing significantly higher concentrations (mean value ca. 416 mg/1) than the osteoarthritic fluids (mean value ca. 142.4 mg/1). In addition, upon treatment with pepsin, all of the rheumatoid arthritis samples were shown to possess additional cathepsin B-like activity, suggesting the presence of a reservoir of latent precursor molecules. By utilising a recently developed biotinylated affmity label for cathepsin B-like proteinases and sheep anti-(human cathepsin B) antibodies, used in combination with SDS-PAGE and Western blotting, the rheumatoid arthritic synovial cathepsin B was shown to exist in two forms with apparent molecular masses of M r 29 000 and 42 000. We propose that the former is a ftmctionally active proteinase, whereas the latter is a pepsin activatable proform which, when cleaved by this aspartyl proteinase, is converted into a catalytically competent species of M f 20000.

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Section: Resultsmentioning

confidence: 99%

Section: Iminunological Characterisation Of Cathepsin B-like Speciesmentioning

confidence: 99%

Section: Pepsin Activationmentioning

confidence: 99%

See 1 more Smart Citation

The Detection, Quantification and Partial Characterisation of Cathepsin B-Like Activity in Human Pathological Synovial Fluids

Duffy¹,

Walker²,

Guthrie³

et al. 1994

CCLM

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“…The amino terminus of the 56-kDa enzyme was blocked, and so the sequence could not be directly determined. (63,64), spontaneous mammary tumors (80), and melanoma cell lines (109). The production and secretion of cathepsin B have been linked to the invasiveness of human carcinomas (94,110).…”

Section: Multiple Forms Of Cysteine Proteinasesmentioning

confidence: 99%

Cysteine Proteinases and the Pathogenesis of Amebiasis

Que

Reed

2000

Clinical Microbiology Reviews

206

108

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“…Their proteolytic activities may also be relevant to human diseases such as neoplasia [13][14][15][16], arthritis [17], emphysema [18,19], and Alzheimer's disease [20,21]. Although they share identical active site amino acids (i.e.…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning of human cathepsin O, a novel endoproteinase and homologue of rabbit OC2

et al. 1995

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A 1670-bp cDNA coding for a novel human cysteine protease has been isolated from a monocyte-derived macrophage cDNA library. This cDNA predicts a 329-amino acid preprocathepsin with more than 50% identity to both human cathepsin S and cathepsin L and 94% identity to a rabbit cDNA, termed OC2, recently isolated from osteoclasts. Based on its high homology to OC2, we have named the human enzyme cathepsin O. Cathepsin O mRNA was identified as a single ~ 1.7 kb transcript in cultures of 15-day-old monocyte-derived macrophages, but was not expressed in human monocytes or alveolar macrophages. When transfected into COS-7 cells, cathepsin O displayed potent endoprotease activity against fibrinogen at acid pH. This novel endoprotease may play an important role in extracellular matrix degradation.

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Characterization of a latent cysteine proteinase from ascitic fluid as a high molecular weight form of cathepsin B

Cited by 68 publications

References 19 publications

The Detection, Quantification and Partial Characterisation of Cathepsin B-Like Activity in Human Pathological Synovial Fluids

The Detection, Quantification and Partial Characterisation of Cathepsin B-Like Activity in Human Pathological Synovial Fluids

Cysteine Proteinases and the Pathogenesis of Amebiasis

Molecular cloning of human cathepsin O, a novel endoproteinase and homologue of rabbit OC2

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