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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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Proteolytic processing of DSD-1-PG/phosphacan in wild-type mice after KA injection. Partially purified protein extracts from KA-injected (inj) or PBS-injected (uninj) wild-type (wt), tPA^−/− and plg^−/− hippocampi, as described in Materials and Methods, were analyzed by SDS-PAGE and immunoblotting, using an anti-DSD-1-PG/phosphacan antibody. Note the processing that has occurred in the wild-type injected lane, and the absence of such processing in the corresponding tPA^−/− and plg^−/− lanes. The arrows point to the 400-kD DSD-1-PG/phosphacan protein band (upper arrow), and the DSD-1-PG/phosphacan protein core of 180 kD (lower arrow), which appears more susceptible to plasmin cleavage. Top, Coomassie-stained gel showing comparable loading among the different lanes; bottom, Western blot of the Coomassie-stained gel (top). This experiment has been repeated five times.