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. 2000 Mar 20;148(6):1295–1304. doi: 10.1083/jcb.148.6.1295

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© 2000 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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In vitro cleavage of neurocan and DSD-1-PG/phosphacan by plasmin, but not tPA. Radiolabeled with ¹²⁵I, purified neurocan (∼9.75 ng) and DSD-1-PG/phosphacan (∼6.5 ng) were incubated with recombinant mouse tPA or human plasmin in the absence or presence of PAI-1 or α₂-antiplasmin. The inhibitors were preincubated with the recombinant enzymes for 5 min at 37°C. The samples were analyzed by SDS-PAGE and autoradiography. Lane 1, tPA 1 ng; lane 2, tPA 10 ng; lane 3, tPA 100 ng; lane 4, tPA 100 ng and PAI1 100 ng; lane 5, proteoglycan incubated with buffer alone; lane 6, proteoglycan by itself; lane 7, plasmin 1 ng; lane 8, plasmin 10 ng; lane 9, plasmin 100 ng; lane 10, plasmin 10 ng and α ₂-antiplasmin 50 ng; lane 11, plasmin 10 ng and α₂-antiplasmin 100 ng. The arrows point to bands that disappear after incubation with plasmin.