ArticleThe Biochemical journal1996
Expression of functional recombinant human procathepsin B in mammalian cells.
Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 17 citations in OpenAlex.
- Redox-based inactivation of cysteine cathepsins by compounds containing the 4-aminophenol moiety.PloS one · 2011Article
- Molecular and biochemical characterization of a cathepsin B-like protease family unique to Trypanosoma congolense.Eukaryotic cell · 2008Article
- Characterization of recombinant human cathepsin B expressed at high levels in baculovirus.Protein science : a publication of the Protein Society · 1998Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Cathepsin B has been implicated in numerous pathobiological processes. In order to study its interactions with other proteins implicated in these processes, quantities of functional recombinant cathepsin B are needed. Therefore, we expressed recombinant human procathepsin B in mammalian cells (BSC-1 monkey kidney cells and HeLa human cervical carcinoma cells) using a vaccinia virus expression system. The recombinant human procathepsin B appeared to be authentic and expressed in its native conformation as indicated by: (1) N-terminal sequencing; (2) molecular size; (3) processing intracellularly to mature double-chain cathepsin B; (4) in vitro cleavage by pepsin to mature cathepsin B coincident with appearance of activity against a selective synthetic substrate; and (5) substrate/inhibitor profiles. This is the first report of the expression of functional recombinant human procathepsin B in mammalian cells. We also report a single-step immunoaffinity purification procedure for the isolation of electrophoretically pure proenzyme. By the methodologies described, human procathepsin B can now be obtained in high yield. This should facilitate studies of its interactions with protease inhibitors, other proteases, extracellular matrices, cell-surface proteins and biological substrates that may be of relevance to the pathobiological functions of this enzyme.
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Registered trials
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