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. 1999 Dec 27;147(7):1493–1502. doi: 10.1083/jcb.147.7.1493

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© 1999 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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graphic file with name JCB9906064.f4a.jpg — Effect of ANT-1 on protein and DNA degradation. (A) ANT-1 induces internucleosomal DNA cleavage. 293T cells were transfected with an empty vector or with an expression construct for ANT-1. Low molecular mass DNA was isolated from transfected cells, separated on a 2% agarose gel, and stained with ethidium bromide. (B) ANT-1 leads to the degradation of PARP. 293T cells were transfected with an empty control vector, an expression vector for the death domain protein RIP or with ANT-1. 16 h later, nuclear extracts of the transfected cells were prepared and investigated for the status of PARP in a Western blot. The generated PARP fragment is indicated by an arrow. An unspecific signal (o) served as an internal control for equal loading of the gel. (C) Inhibition of ANT-1 apoptosis by a specific inhibitor for caspases. ANT-1 (1 μg) and a control vector (10 μg) or an expression vector (10 μg) for the caspase inhibitor p35 from baculovirus were cotransfected, and the specific apoptosis induction was determined by FACS analysis. The means and the SDs are indicated (n = 3).

graphic file with name JCB9906064.f4b.jpg — Effect of ANT-1 on protein and DNA degradation. (A) ANT-1 induces internucleosomal DNA cleavage. 293T cells were transfected with an empty vector or with an expression construct for ANT-1. Low molecular mass DNA was isolated from transfected cells, separated on a 2% agarose gel, and stained with ethidium bromide. (B) ANT-1 leads to the degradation of PARP. 293T cells were transfected with an empty control vector, an expression vector for the death domain protein RIP or with ANT-1. 16 h later, nuclear extracts of the transfected cells were prepared and investigated for the status of PARP in a Western blot. The generated PARP fragment is indicated by an arrow. An unspecific signal (o) served as an internal control for equal loading of the gel. (C) Inhibition of ANT-1 apoptosis by a specific inhibitor for caspases. ANT-1 (1 μg) and a control vector (10 μg) or an expression vector (10 μg) for the caspase inhibitor p35 from baculovirus were cotransfected, and the specific apoptosis induction was determined by FACS analysis. The means and the SDs are indicated (n = 3).