Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

Tumor necrosis factor-alpha is released from cells by a proteolytic cleavage. Previous work suggested that a specific, non-matrix metalloproteinase carries out this cleavage, but matrix metalloproteinases have also been implicated. In this paper, we report that none of the matrix metalloproteinases tested cleaved peptide substrates as specifically as the non-matrix metalloproteinase. A matrix metalloproteinase did process tumor necrosis factor-alpha extracted from COS cells, but neither tissue inhibitor of metalloproteinases-1 nor -2 blocked tumor necrosis factor-alpha processing by human monocytes. Moreover, tissue inhibitor of metalloproteinases-1 had at most a partial effect on the in vivo release of the cytokine in mice. We conclude that a non-matrix metalloproteinase is the major physiological tumor necrosis factor-alpha convertase.

Original publication

DOI

10.1006/bbrc.1996.1186

Type

Journal article

Journal

Biochem Biophys Res Commun

Publication Date

14/08/1996

Volume

225

Pages

400 - 405

Keywords

ADAM Proteins, ADAM17 Protein, Animals, CHO Cells, Cell Line, Cells, Cultured, Cricetinae, Glycoproteins, Humans, Metalloendopeptidases, Mice, Mice, Inbred BALB C, Protein Processing, Post-Translational, Recombinant Proteins, Substrate Specificity, Tissue Inhibitor of Metalloproteinases, Tumor Cells, Cultured, Tumor Necrosis Factor-alpha