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Discovery of a highly selective caspase-3 substrate for imaging live cells

Academic Article
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Overview

related to degree

  • Vickers, Chris, Ph.D. in Chemistry, Scripps Research 2009 - 2014

authors

  • Vickers, Chris
  • Gonzalez-Paez, G. E.
  • Wolan, Dennis

publication date

  • October 2014

journal

  • ACS Chemical Biology  Journal

abstract

  • Caspases are a family of cysteine proteases that are well-known for their roles in apoptosis and inflammation. Recent studies provide evidence that caspases are also integral to many additional cellular processes, such as differentiation and proliferation. Likewise, aberrant caspase activity has been implicated in the progression of several diseases, including neurodegenerative disorders, cancer, cardiovascular disease, and sepsis. These observations establish the importance of caspases to a diverse array of physiological functions and future endeavors will undoubtedly continue to elucidate additional processes that require caspase activity. Unfortunately, the existence of 11 functional human caspases, with overlapping substrate specificities, confounds the ability to confidently assign one or more isoforms to biological phenomena. Herein, we characterize a first-in-class FRET substrate that is selectively recognized by active caspase-3 over other initiator and executioner caspases. We further apply this substrate to specifically image caspase-3 activity in live cells undergoing apoptosis.

subject areas

  • Apoptosis
  • Caspase 3
  • Fluorescence Resonance Energy Transfer
  • HeLa Cells
  • Humans
  • MCF-7 Cells
  • Molecular Imaging
  • Substrate Specificity
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Identity

International Standard Serial Number (ISSN)

  • 1554-8929

Digital Object Identifier (DOI)

  • 10.1021/cb500586p

PubMed ID

  • 25133295
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Additional Document Info

start page

  • 2199

end page

  • 2203

volume

  • 9

issue

  • 10

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