Heat Shock Protein 27 Inhibits Apoptosis by Binding Cytochrome c

Abstract

The purpose of this research project is to investigate the interaction between heat shock protein 27 (hsp27) and cytochrome c in the inhibition of apoptosis. The scope of the study was to include: measuring the binding of hsp27 to cytochrome c in vivo, determining why hsp27 binds to cytochrome c and determining the fate of the hsp27:cytochrome c complex. Major findings include cellular survival curves to cytochrome C, ATP, FAD and NAD. All electron carriers were cytotoxic to human breast cancer cell lines, with FAD being the most cytotoxic. This finding could have applications in the treatment of breast cancer. Molecular chaperone assays with hsp27 and alphaglucosidase and citrate synthase indicate that hsp27 binds to cytochrome c in a non-specific manner.

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Document Details

Document Type
Technical Report
Publication Date
Jun 01, 2003
Accession Number
ADA417947

Entities

People

  • Stephen W. Carper

Organizations

  • University of Nevada, Las Vegas

Tags

Communities of Interest

  • Biomedical

DTIC Thesaurus Topics

  • Breast Cancer
  • Cell Membrane
  • Cell Physiological Processes
  • Cells
  • Chemical Synthesis
  • Chemistry
  • Medical Personnel
  • Neoplasms
  • Programmed Cell Death
  • Proteins

Fields of Study

  • Biology
  • Computer science

Readers

  • Chemistry (specifically Chemical Fluorescence)
  • Immunology and Pathology
  • Prostate Cancer Biology.

Technology Areas

  • Microelectronics