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Engineering a photoactivated caspase-7 for rapid induction of apoptosis.

Authors
  • Mills, Evan
  • Chen, Xi
  • Pham, Elizabeth
  • Wong, Stanley
  • Truong, Kevin
Type
Published Article
Journal
ACS Synthetic Biology
Publisher
American Chemical Society
Publication Date
Mar 16, 2012
Volume
1
Issue
3
Pages
75–82
Identifiers
DOI: 10.1021/sb200008j
PMID: 23651071
Source
Medline
License
Unknown

Abstract

Apoptosis is a cell death program involved in the development of multicellular organisms, immunity, and pathologies ranging from cancer to HIV/AIDS. We present an engineered protein that causes rapid apoptosis of targeted cells in monolayer culture after stimulation with blue light. Cells transfected with the protein switch L57V, a tandem fusion of the light-sensing LOV2 domain and the apoptosis-executing domain from caspase-7, rapidly undergo apoptosis within 60 min after light stimulation. Constant illumination of under 5 min or oscillating with 1 min exposure had no effect, suggesting that cells have natural tolerance to a short duration of caspase-7 activity. Furthermore, the overexpression of Bcl-2 prevented L57V-mediated apoptosis, suggesting that although caspase-7 activation is sufficient to start apoptosis, it requires mitochondrial contribution to fully commit.

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