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J. Biol. Chem., Vol. 279, Issue 31, 32142-32150, July 30, 2004

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Temporal Regulation of VEID-7-amino-4-trifluoromethylcoumarin Cleavage Activity and Caspase-6 Correlates with Organelle Loss during Lens Development^*

John D. Foley, Heidi Rosenbaum, and Anne E. Griep

From the Department of Anatomy, University of Wisconsin Medical School, Madison, Wisconsin 53706

Lens fiber cell differentiation involves extensive reconstruction of the cell's architecture, including the degradation and elimination of all membrane-bound organelles via a process that has been likened to apoptosis. Using caspase reporter assays under conditions in which nonspecific cleavage of the reporter peptides by the proteasome has been inhibited, we investigated whether any specific caspase activities are temporally correlated with this process of organelle loss. Extracts from neonatal mouse lenses contained strong VEID-7-amino-4-trifluoromethylcoumarin (AFC) and minor IETD-AFC and LEVD-AFC cleavage activities, but no DEVD-AFC cleavage activity. Further testing suggested that the VEID-AFC and IETD-AFC cleavage activities were likely due to the same enzyme. In lens extracts from rat embryos, VEID-AFC cleavage activity increased during the period when organelles are eliminated, between embryonic days 15.5 and 18.5, whereas procaspase-6 protein levels decreased, suggesting that this enzyme is responsible for VEID-AFC cleavage. By contrast, in extracts from AE7 transgenic mouse lenses in which apoptosis was induced, strong DEVD-AFC cleavage activity and activated caspase-3 protein were detected. Thus, within the same tissue, different caspase activities can predominate depending on the context, normal differentiation versus apoptosis. These results highlight the difference between normal fiber cell differentiation and apoptosis and the capacity of the lens to differentially regulate these two processes.

Received for publication, December 15, 2003 , and in revised form, May 24, 2004.

^* This work was supported by National Institutes of Health Grants EY09091 and HD1007477. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Anatomy, University of Wisconsin Medical School, 1300 University Ave., Madison, WI 53706. Tel.: 608-262-8988; Fax: 608-262-7306; E-mail: aegriep{at}wisc.edu.

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