{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,31]],"date-time":"2026-07-31T10:29:57Z","timestamp":1785493797453,"version":"3.56.0"},"reference-count":62,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2022,8,9]],"date-time":"2022-08-09T00:00:00Z","timestamp":1660003200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["SFB877"],"award-info":[{"award-number":["SFB877"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2023,1]]},"abstract":"<jats:p>\n                    Membrane\u2010type\u2010I matrix metalloproteinase (MT1\u2010MMP) is one of six human membrane\u2010bound MMPs and is responsible for extracellular matrix remodelling by degrading several substrates like fibrillar collagens, including types I\u2010III, or fibronectin. Moreover, MT1\u2010MMP was described as a key player in cancer progression and it is involved in various inflammatory processes, as well as in the pathogenesis of Alzheimer's disease (AD). The membrane\u2010tethered metalloprotease meprin \u03b2 as well as a disintegrin and metalloproteinase 10 (ADAM10) and ADAM17 are also associated with these diseases. Interestingly, meprin \u03b2, ADAM10\/17 and MT1\u2010MMP also have a shared substrate pool including the interleukin\u20106 receptor and the amyloid precursor protein. We investigated the interaction of these proteases, focusing on a possible connection between MT1\u2010MMP and meprin \u03b2, to elucidate the potential mutual regulations of both enzymes. Herein, we show that besides ADAM10\/17, MT1\u2010MMP is also able to shed meprin \u03b2 from the plasma membrane, leading to the release of soluble meprin \u03b2. Mass spectrometry\u2010based cleavage site analysis revealed that the cleavage of meprin \u03b2 by all three proteases occurs between Pro\n                    <jats:sub>602<\/jats:sub>\n                    and Ser\n                    <jats:sub>603<\/jats:sub>\n                    , N\u2010terminal of the EGF\u2010like domain. Furthermore, only inactive human pro\u2010meprin \u03b2 is shed by MT1\u2010MMP, which is again in accordance with the shedding capability observed for ADAM10\/17.\n                    <jats:italic>Vice versa<\/jats:italic>\n                    , meprin \u03b2 also appears to shed MT1\u2010MMP, indicating a complex regulatory network. Further studies will elucidate this well\u2010orchestrated proteolytic web under distinct conditions in health and disease and will possibly show whether the loss of one of the above\u2010mentioned sheddases can be compensated by the other enzymes.\n                  <\/jats:p>","DOI":"10.1111\/febs.16586","type":"journal-article","created":{"date-parts":[[2022,7,30]],"date-time":"2022-07-30T03:38:22Z","timestamp":1659152302000},"page":"93-111","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":24,"title":["<scp>MT1\u2010MMP<\/scp>\n                    and\n                    <scp>ADAM10<\/scp>\n                    \/17 exhibit a remarkable overlap of shedding properties"],"prefix":"10.1111","volume":"290","author":[{"given":"Ludwig","family":"Werny","sequence":"first","affiliation":[{"name":"Institute of Biochemistry University of Kiel  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