The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs

摘要: The ADAM family of proteases are type I transmembrane proteins with both metalloproteinase and disintegrin containing extracellular domains. ADAMs implicated in the proteolytic processing membrane-bound precursors involved modulating cell–cell cell–matrix interactions. ADAM8 (MS2, CD156) has been identified myeloid B cells. In this report we demonstrate that soluble is an active metalloprotease vitro able to hydrolyse myelin basic protein a variety peptide substrates based on cleavage sites cytokines, growth factors receptors which known be processed by metalloproteinases. Interestingly, although was inhibited number analogue hydroxamate inhibitors, it not tissue inhibitors metalloproteinases (TIMPs). We also activity recombinant ADAM9 (meltrin-γ, MDC9) lacks inhibition TIMPs, but can inhibitors. lack TIMP 9 contrasts other membrane-associated characterised date respect (ADAM10, 12, 17, membrane-type metalloproteinases) have at cell surface.