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Originally published as JHC exPRESS on March 30, 2009.
doi:10.1369/jhc.2009.953380
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Journal of Histochemistry and Cytochemistry
Volume 57 (7): 675-685, 2009
Copyright ©The Histochemical Society, Inc.

Assessment of PARP-3 Distribution in Tissues of Cynomolgous Monkeys

Michèle Rouleau, Mohamed El-Alfy, Marie-Hélène Lévesque and Guy G. Poirier

Health and Environment Unit (MR,GGP) and Molecular and Oncologic Endocrinology (ME-A,M-HL), Centre Hospitalier Universitaire de Québec, Laval University Research Center, Québec, Québec, Canada

Correspondence to: Guy G. Poirier, PhD, Université Laval Research Center, Health and Environment Unit and Department of Medical Biology, 2705 Blvd Laurier, Rm 9700, Québec, QC, G1V 4G2, Canada. E-mail: guy.poirier{at}crchul.ulaval.ca

Poly(ADP-ribose) polymerase 3 (PARP-3) is a newly characterized PARP. In contrast to the two best-studied nuclear PARPs, PARP-1 and PARP-2, PARP-3 activity is apparently not stimulated by DNA damage. However, our previous work has demonstrated that PARP-3 interacts with several DNA damage response proteins, including Ku70/Ku80, DNA-PK, and PARP-1, suggesting that it contributes to the DNA damage response. Furthermore, a possible function for PARP-3 in the regulation of gene expression has been inferred from our observations that it associates with polycomb group proteins, which are responsible for epigenetic modifications leading to gene silencing. In this report, we extend our characterization of PARP-3 by revealing its distribution in the tissues and cell types of adult cynomolgous monkeys using a well-characterized PARP-3 polyclonal antibody. This study is the first to demonstrate that PARP-3 is genuinely expressed in most of the examined tissues. However, its expression is highly restricted to specific cell types of each tissue, indicating that PARP-3 expression is tightly regulated. One of the key findings of this study is that PARP-3 is highly expressed in the nuclei of epithelial cells forming the ducts of prostate, salivary glands, liver, and pancreas and in the neurons of terminal ganglia. (J Histochem Cytochem 57:675–685, 2009)

Key Words: poly(ADP-ribose) polymerase • immunohistochemistry • monkey • tissue distribution • ductal epithelia


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O. Loseva, A.-S. Jemth, H. E. Bryant, H. Schuler, L. Lehtio, T. Karlberg, and T. Helleday
PARP-3 Is a Mono-ADP-ribosylase That Activates PARP-1 in the Absence of DNA
J. Biol. Chem., March 12, 2010; 285(11): 8054 - 8060.
[Abstract] [Full Text] [PDF]



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