The metalloprotease disintegrin ADAM8. Processing by autocatalysis is required for proteolytic activity and cell adhesion

Article


Schlomann, U., Wildeboer, D., Webster, A., Antropova, O., Zeuschner, D., Knight, C., Docherty, A., Lambert, M., Skelton, L., Jockusch, H. and Bartsch, J. 2002. The metalloprotease disintegrin ADAM8. Processing by autocatalysis is required for proteolytic activity and cell adhesion. Journal of Biological Chemistry. 277 (50), pp. 48210-48219. https://doi.org/10.1074/jbc.M203355200
TypeArticle
TitleThe metalloprotease disintegrin ADAM8. Processing by autocatalysis is required for proteolytic activity and cell adhesion
AuthorsSchlomann, U., Wildeboer, D., Webster, A., Antropova, O., Zeuschner, D., Knight, C., Docherty, A., Lambert, M., Skelton, L., Jockusch, H. and Bartsch, J.
Abstract

ADAMs (a disintegrin and metalloprotease domains) are metalloprotease and disintegrin domain-containing transmembrane glycoproteins with proteolytic, cell adhesion, cell fusion, and cell signaling properties. ADAM8 was originally cloned from monocytic cells, and its distinct expression pattern indicates possible roles in both immunology and neuropathology. Here we describe our analysis of its biochemical properties. In transfected COS-7 cells, ADAM8 is localized to the plasma membrane and processed into two forms derived either by prodomain removal or as remnant protein comprising the extracellular region with the disintegrin domain at the N terminus. Proteolytic removal of the ADAM8 propeptide was completely blocked in mutant ADAM8 with a Glu(330) to Gln exchange (EQ-A8) in the Zn(2+) binding motif (HE(330)LGHNLGMSHD), arguing for autocatalytic prodomain removal. In co-transfection experiments, the ectodomain but not the entire MP domain of ADAM8 was able to remove the prodomain from EQ-ADAM8. With cells expressing ADAM8, cell adhesion to a substrate-bound recombinant ADAM8 disintegrin/Cys-rich domain was observed in the absence of serum, blocked by an antibody directed against the ADAM8 disintegrin domain. Soluble ADAM8 protease, consisting of either the metalloprotease domain or the complete ectodomain, cleaved myelin basic protein and a fluorogenic peptide substrate, and was inhibited by batimastat (BB-94, IC(50) approximately 50 nm) but not by recombinant tissue inhibitor of matrix metalloproteinases 1, 2, 3, and 4. Our findings demonstrate that ADAM8 processing by autocatalysis leads to a potential sheddase and to a form of ADAM8 with a function in cell adhesion.

Research GroupBiophysics and Bioengineering group
LanguageEnglish
PublisherAmerican Society for Biochemistry and Molecular Biology
JournalJournal of Biological Chemistry
ISSN0021-9258
Publication dates
Print13 Dec 2002
Online07 Oct 2002
Publication process dates
Deposited01 Mar 2012
Accepted02 Oct 2002
Output statusPublished
Digital Object Identifier (DOI)https://doi.org/10.1074/jbc.M203355200
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