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A closer look at PARP-1 reveals potential new drug targets
Date:5/11/2012

PHILADELPHIAA new study published in Science May 11 is shedding light on the molecular details of PARP-1, a DNA damage-detecting enzyme that when inhibited has been shown to be effective in fighting cancer and other diseases.

The investigation led by John M. Pascal, Ph.D., an assistant professor in the Department of Biochemistry and Molecular Biology at Thomas Jefferson University and Jefferson's Kimmel Cancer Center, revealed new target sitesincluding specialized "zinc finger" domainsfor drugs aiming to stop PARP-1 activity.

The idea for this area of research is to identify more specific PARP-1 inhibitors that achieve a targeted inhibition, with less potential for side effects. Drugs inhibiting PARP-1 have also been proven effective in treating inflammation and cardiac disease.

"PARP-1 has been identified as a valuable target, but what's special about it? What really are its weak points in the way it gets activated?" said Dr. Pascal. "We wanted to define a structural and mechanistic framework to better understand how to specifically inhibit PARP-1."

The weak points were found to be multi-domain interfaces that are uniquely found in PARP-1. What researchers now know is that multiple domains of PARP-1 come together and bind to DNA damage, and this "communication" between domains is essential for DNA damage-dependent PARP-1 activity.

PARP-1 is a protein that detects and responds to breaks in the structure of DNA, a potentially lethal form of damage to our genetic information. If PARP-1 activity is impaired, DNA strand breaks are not repaired and instead are converted into more dangerous types of DNA damage. In normal tissue, a repair mechanism called homologous recombination picks up the slack and fixes the damaged DNA. However, in cancers that carry the BRCA mutation, like
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Contact: Steve Graff
stephen.graff@jefferson.edu
215-955-5291
Thomas Jefferson University
Source:Eurekalert  

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