Differences in the Activation Mechanism between the α and β Subunits of Human Meprin
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C. Becker
Abstract
Meprins are zinc-endopeptidases of the astacin family, which are expressed as membrane-bound or secreted forms in renal and intestinal brush-border membranes of mouse, rat and man. There are two types of meprin subunits, α and β, which form disulfide-bonded homo- and heterodimers; further oligomerization is mediated by non-covalent interactions. Both subunits are translated as proenzymes that have to be activated by removal of an N-terminal propeptide. In the gut, the most probable activator is trypsin. In addition, plasmin has been shown to activate the human α subunit in colorectal cancer tissue. In the present study we have overexpressed the human meprin α subunit and a His-tagged soluble tail-switchmutant of meprin β in Baculovirus-infected insect cells. The recombinant homo-oligomeric proteins were purified by gel filtration and affinity chromatography with yields of up to 10 mg/l cell culture medium and analyzed with regard to their activation mechanism. While both α and β homo-oligomers are activated by trypsin, only meprin α homo-oligomers are processed to their mature form by plasmin. These results indicate a different accessibility of the propeptide in meprin homo-oligomers and suggest an explanation for the appearance of meprin hetero-oligomers consisting of active α, but latent β subunits.
Copyright © 2003 by Walter de Gruyter GmbH & Co. KG
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- The Magnetofection Method: Using Magnetic Force to Enhance Gene Delivery
- The Protease Inhibitor Bikunin, a Novel Anti-Metastatic Agent
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- Identification and Characterization of KAT, a Novel Gene Preferentially Expressed in Several Human Cancer Cell Lines
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