[Federal Register Volume 71, Number 238 (Tuesday, December 12, 2006)]
[Notices]
[Pages 74551-74552]
From the Federal Register Online via the Government Publishing Office [www.gpo.gov]
[FR Doc No: E6-21037]


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DEPARTMENT OF HEALTH AND HUMAN SERVICES

National Institutes of Health


Government-Owned Inventions; Availability for Licensing

AGENCY: National Institutes of Health, Public Health Service, HHS.

ACTION: Notice.

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SUMMARY: The inventions listed below are owned by an agency of the U.S. 
Government and are available for licensing in the U.S. in accordance 
with 35 U.S.C. 207 to achieve expeditious commercialization of results 
of federally-funded research and development. Foreign patent 
applications are filed on selected inventions to extend market coverage 
for companies and may also be available for licensing.

ADDRESSES: Licensing information and copies of the U.S. patent 
applications listed below may be obtained by writing to the indicated 
licensing contact at the Office of Technology Transfer, National 
Institutes of Health, 6011 Executive Boulevard, Suite 325, Rockville, 
Maryland 20852-3804; telephone: 301/496-7057; fax: 301/402-0220. A 
signed Confidential Disclosure Agreement will be required to receive 
copies of the patent applications.

ARH3, a Therapeutic Target for Cancer, Ischemia, and Inflammation

    Description of Technology: ADP-ribosylation is important in many 
cellular processes, including DNA replication and repair, maintenance 
of genomic stability, telomere dynamics, cell differentiation and 
proliferation, and necrosis and apoptosis. Poly-ADP-ribose is important 
in a number of critical physiological processes such as DNA repair, 
cellular differentiation, and carcinogenesis. Until recently, only one 
human enzyme, PARG, had been identified that degrades the ADP-ribose 
polymer. Another ADP-ribose, O-acetyl-ADP ribose, is formed via the 
deacetylation of proteins, such as acetyl-histone, by proteins in the 
Sir2 family. Sir2 proteins have been implicated in regulation of 
chromatin structure and longevity.
    The NIH announces the discovery of a novel PARG-like enzyme, ARH3. 
ARH3 possesses PARG activity, yet is structurally distinct from PARG. 
ARH3 also hydrolyzes O-acetyl-ADP-ribose, and is the only protein 
recognized to date with such activity. ARH3 thus appears to function in 
two important signaling pathways, serving to regulate both poly-ADP-
ribose and O-acetyl-ADP-ribose levels. It may affect chromatin 
structure through effects on both pathways. Since ARH3 structures 
differs from PARG or other enzymes that participate in these pathways, 
it may be possible to design specific inhibitors to target both the 
poly-ADP-ribose and Sir2 pathways. These drugs may be used as 
anticancer agents, radiosensitizers or antiviral agents, or for 
treating disorders involving oxidative damage, such as acute tissue 
injury, ischemia, and inflammation.
    Applications: (1) Development of therapeutics for cancer or 
disorders associated with excessive DNA damage; (2) Development of 
therapeutics for diseases involving oxidative damage, such as acute 
tissue injury, ischemia and inflammation.
    Market: (1) Patients with chemotherapy-resistant tumors, or with 
cancers that are genetically deficient in DNA repair; (2) Patients with 
inflammatory or ischemia/reperfusion diseases, particularly those 
associated with acute cardiovascular disease.
    Development Status: Early stage.
    Inventors: Joel Moss et al. (NHLBI).
    Related Publications:
    1. S Oka, J Kato, J Moss. Identification and characterization of a 
mammalian 39-kDa poly(ADP-ribose) glycohydrolase. J Biol Chem. 2006 Jan 
13;281(2):705-713.
    2. T Ono, A Kasamatsu, S Oka, J Moss. The 39-kDa poly(ADP-ribose) 
glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the 
Sir2 family of acetyl-histone deacetylases. Proc Natl Acad Sci USA 2006 
Nov 7;103(45):16687-16691. Epub 2006 Oct 30, doi 10.1073/
pnas.0607911103.
    Patent Status: U.S. Provisional Application No. 60/716,807 filed 12 
Sep 2005 (HHS Reference No. E-347-2004/0-US-01); PCT Application No. 
PCT/US2006/035771 filed 12 Sep 2006 (HHS Reference No. E-347-2004/0-
PCT-02).
    Licensing Status: Available for exclusive or non-exclusive 
licensing.
    Licensing Contact: Tara L. Kirby, PhD; 301/435-4426; 
[email protected].
    Collaborative Research Opportunity: The Pulmonary Critical Care 
Medicine Branch in the National Heart, Lung, and Blood Institute is 
seeking statements of capability or interest from parties interested in 
collaborative research to further develop, evaluate, or commercialize 
the invention. Please contact Marianne Lynch in the NHLBI Office of 
Technology Transfer and Development by phone (301-594-4094) or e-mail 
([email protected]) for more information.

Antisera To Detect Phosphorylated Phosphoinositide-Dependent Kinase 1 
(PDK-1)

    Description of Technology: PDK-1 phosphorylates and activates a 
number of cellular kinases, and plays a major role in insulin and 
growth factor signaling. PDK-1 also represents a promising drug target 
for a number of cancers. Autophosphorylation at Ser244 (mouse) or 
Ser241 (human) is critical for PDK-1 activity.
    Available for licensing are polyclonal rabbit antisera that 
specifically detect mouse PDK-1 protein phosphorylated at Ser244. These 
antisera are also expected to be specific for the human PDK-1 protein 
phosphorylated at Ser241.
    Applications: (1) Tool for screening PDK-1 autophosphorylation 
inhibitors for cancer and other indications; (2) Tool for studying 
insulin and growth factor signaling.
    Inventor: Michael J. Quon (NCCAM).
    Publication: MJ Wick, FJ Ramos, H Chen, MJ Quon, LQ Dong, F Liu. 
Mouse 3-phosphoinositide-dependent protein kinase-1 undergoes 
dimerization and trans-phosphorylation in the activation loop. J Biol 
Chem. 2003 Oct 31;278(44):42913-42919.
    Patent Status: HHS Reference No. E-330-2003/0--Research Tool.
    Licensing Status: This technology is available as a research tool 
under a Biological Materials License.
    Licensing Contact: Tara Kirby, PhD; 301/435-4426; 
[email protected]
    Collaborative Research Opportunity: The NIH, NCCAM, Diabetes Unit 
is seeking statements of capability or interest from parties interested 
in collaborative research to further

[[Page 74552]]

develop, evaluate, or commercialize phospho-specific PDK-1 antibody and 
insulin signaling. Please contact Michael J. Quon, Chief, Diabetes 
Unit, NCCAM, NIH at [email protected] for more information.

    Dated: December 6, 2006.
Steven M. Ferguson,
Director, Division of Technology Development and Transfer, Office of 
Technology Transfer, National Institutes of Health.
[FR Doc. E6-21037 Filed 12-11-06; 8:45 am]
BILLING CODE 4140-01-P