Identification and Characterization of a Pro-tumor Necrosis Factor-α-processing Enzyme from the ADAM Family of Zinc Metalloproteases*
By M. Rosendahl, S. Ko, D. L. Long, M. T. Brewer, B. Rosenzweig, Erik Hedl, L. Anderson, S. Pyle, Julie Moreland, Mark A Meyers and 3 more. 1997
Tumor necrosis factor-α (TNF) is initially expressed as a 26-kDa membrane-bound precusor protein (pro-TNF) that is shed proteolytically from the cell surface, releasing soluble 17-kDa TNF. We have identified human ADAM 10 (HuAD10) from THP-1 membrane extracts as a metalloprotease that specifically clips a peptide substrate spanning the authentic cleavage site between Ala76 and Val77 in pro-TNF. To confirm that HuAD10 has TNF processing activity, we cloned, expressed, and purified an active, truncated form of HuAD10. Characterization of recombinant HuAD10 (rHuAD10) suggests that this enzyme has many of the properties (i.e. substrate specificity, metalloprotease activity, cellular location) expected for a physiologically relevant TNF-processing enzyme.
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Citations in the corpus
- A Disintegrin and Metalloproteinase (ADAM) and ADAM with Thrombospondin Motifs (ADAMTS) Family in Vascular Biology and Disease (2019, background): “Of note, TNFα processing is not completely inhibited by the lack of ADAM-17 in ADAM-17 knockout cells, and other proteins including ADAM-9 and 10 [91, 92], and MT4-MMP (MMP17) [93] may also be involved in the shedding of TNFα.”
- The ADAMs family of metalloproteases: multidomain proteins with multiple functions. (2003, background): “vitro (Lunn et al. 1997; Rosendahl et al. 1997; Roghani et al. 1999; Amour et al. 2000), although expressing ADAM10 in ADAM17 null cells does not reconstitute full TNF shedding (Reddy et al.”