[HTML][HTML] TNF-α converting enzyme (TACE) is inhibited by TIMP-3
A Amour, PM Slocombe, A Webster, M Butler… - FEBS letters, 1998 - Elsevier
FEBS letters, 1998•Elsevier
TNF-α converting enzyme (TACE; ADAM-17) is a membrane-bound disintegrin
metalloproteinase that processes the membrane-associated cytokine proTNF-α to a soluble
form. Because of its putative involvement in inflammatory diseases, TACE represents a
significant target for the design of specific synthetic inhibitors as therapeutic agents. In order
to study its inhibition by tissue inhibitors of metalloproteinases (TIMPs) and synthetic
inhibitors of metalloproteinases, the catalytic domain of mouse TACE (rTACE) was …
metalloproteinase that processes the membrane-associated cytokine proTNF-α to a soluble
form. Because of its putative involvement in inflammatory diseases, TACE represents a
significant target for the design of specific synthetic inhibitors as therapeutic agents. In order
to study its inhibition by tissue inhibitors of metalloproteinases (TIMPs) and synthetic
inhibitors of metalloproteinases, the catalytic domain of mouse TACE (rTACE) was …
TNF-α converting enzyme (TACE; ADAM-17) is a membrane-bound disintegrin metalloproteinase that processes the membrane-associated cytokine proTNF-α to a soluble form. Because of its putative involvement in inflammatory diseases, TACE represents a significant target for the design of specific synthetic inhibitors as therapeutic agents. In order to study its inhibition by tissue inhibitors of metalloproteinases (TIMPs) and synthetic inhibitors of metalloproteinases, the catalytic domain of mouse TACE (rTACE) was overexpressed as a soluble Ig fusion protein from NS0 cells. rTACE was found to be well inhibited by peptide hydroxamate inhibitors as well as by TIMP-3 but not by TIMP-1, -2 and -4. These results suggest that TIMP-3, unlike the other TIMPs, may be important in the modulation of pathological events in which TNF-α secretion is involved.
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