Intracellular maturation and localization of the tumour necrosis factor alpha convertase (TACE) Journal Article


Authors: Schlöndorff, J.; Becherer, J. D.; Blobel, C. P.
Article Title: Intracellular maturation and localization of the tumour necrosis factor alpha convertase (TACE)
Abstract: Tumour necrosis factor α convertase (TACE) is a metalloprotease/disintegrin involved in the ectodomain shedding of several proteins, a process thought to be important in inflammation, rheumatoid arthritis and murine development. The characterization of the intracellular maturation and subcellular localization of endogenous TACE is decribed in the present study. Similarly to other proteolytically active metalloprotease/disintegrins, two forms of TACE are found in cells; a full-length precursor and a mature form lacking the prodomain. Prodomain removal occurs in a late Golgi compartment, consistent with the proposed role of a furin type proprotein convertase in this process. An additional form of TACE, lacking the pro and cytoplasmic domains, is detected when cell lysates are prepared in the presence of EDTA instead of a hydroxamate-based metalloprotease inhibitor or 1,10-phenanthroline. This form appears to be generated by mature TACE cleaving its own cytoplasmic tail and may explain why little mature TACE has been detected in previous studies. In cell-surface labelling experiments, mature TACE was detected on the cell surface but immunofluorescence data indicate that TACE is predominantly localized to a perinuclear compartment similar to that described for tumour necrosis Factor (TNF)α. This raises the possibility that TACE-mediated ectodomain shedding may occur in an intracellular compartment in addition to the cell surface.
Keywords: human cell; nonhuman; animal cell; animals; cell line; immunofluorescence; transfection; cos cells; animalia; tumor necrosis factor alpha; recombinant proteins; cell membrane; murinae; cellular distribution; subcellular fractions; metalloproteinase; adam proteins; cell lysate; metalloproteinases; furin; golgi complex; protein ectodomain shedding; phenanthrolines; edetic acid; golgi apparatus; disintegrin; adam; metalloendopeptidases; humans; human; priority journal; article; mdc; 1,10 phenanthroline
Journal Title: Biochemical Journal
Volume: 347
Issue: 1
ISSN: 0264-6021
Publisher: Portland Press Ltd  
Date Published: 2000-04-01
Start Page: 131
End Page: 138
Language: English
DOI: 10.1042/0264-6021:3470131
PUBMED: 10727411
PROVIDER: scopus
PMCID: PMC1220940
DOI/URL:
Notes: Export Date: 18 November 2015 -- Source: Scopus
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  1. Carl Blobel
    52 Blobel