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Government-Owned Inventions; Availability for Licensing

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AGENCY:

National Institutes of Health, Public Health Service, HHS.

ACTION:

Notice.

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.

Novel Benztropine Analogs for Treatment of Cocaine Abuse and Other Mental Disorders

Description of Technology: Dopamine is a neurotransmitter that exerts important effects on locomotor activity, motivation and reward, and cognition. The dopamine transporter (DAT) is expressed on the plasma membrane of dopamine synthesizing neurons, and is responsible for clearing dopamine released into the extra-cellular space, thereby regulating neurotransmission. The dopamine transporter plays a significant role in neurotoxicity and human diseases, such as Parkinson's disease, drug abuse (especially cocaine addiction), Attention Deficit Disorder/Attention Deficit Hyperactivity Disorder (ADD/ADHD), and a number of other CNS disorders. Therefore, the dopamine transporter is a strong target for research and the discovery of potential therapeutics for the treatment of these indications.

This invention discloses novel benztropine analogs and methods of using these analogs for treatment of mental and conduct disorders such as cocaine abuse, narcolepsy, ADHD, obesity and nicotine abuse. The disclosed analogs are highly selective and potent inhibitors of DAT, but without an apparent cocaine-like behavioral profile. In addition to their use as a treatment for cocaine abuse, these compounds have also shown efficacy in animal models of ADHD and nicotine abuse, and have also been shown to reduce food intake in animals. They may also be useful medications for other indications where dopamine-related behavior is compromised, such as alcohol addiction, tobacco addiction, and Parkinson's disease.

Applications: Drug leads for treatment of cocaine abuse, ADHD, nicotine abuse, obesity, and other dopamine-related disorders; Imaging probes for dopamine transporter binding sites.

Development Status: Pre-clinical data are available.

Inventors: Amy H. Newman, Mu-fa Zou, and Jonathan L. Katz (NIDA).

Patent Status: U.S. Provisional Application No. 60/710,956 filed 24 Aug 2005 (HHS Reference No. E-234-2005/0-US-01); PCT Application No. PCT/US2006/33103 filed 24 Aug 2006 (HHS Reference No. E-234-2005/1-PCT-01 and HHS Reference No. E-129-2006/0).

Licensing Status: Available for exclusive or nonexclusive licensing.

Licensing Contact: Tara Kirby, Ph.D.; 301/435-4426; tarak@mail.nih.gov.

Collaborative Research Opportunity: The Medicinal Chemistry and Psychobiology Sections, National Institute on Drug Abuse-Intramural Research Program, National Institutes of Health, is seeking statements of capability or interest from parties interested in collaborative research to further develop, evaluate, or commercialize medications to treat cocaine abuse and addiction. Please contact John D. Hewes, Ph.D. at 301/435-3121 or hewesj@mail.nih.gov for more information.

Protein Arginine N-methyltransferase 2 (PRMT-2), a Modulator of NFΚB, E2F1, and STAT3 Activity

Description of Technology: Protein-arginine methyltransferases (PRMTs) contain methyltransferase domains that modify chromatin and regulate cellular transcription through the post-translational methylation of arginine residues on the guanidine group of target proteins. Members of this family have roles in RNA processing, transcriptional regulation, signal transduction, and DNA repair. Until recently, the functional significance of one member of this family, PRMT-2, was unknown.

Researchers at NHLBI, led by Dr. Elizabeth Nabel, have elucidated the role of PRMT-2. They have found that PRMT-2 modulates the activity of NFΚB, E2F1, and STAT3. PRMT-2 inhibits NFΚB dependent transcription, and therefore PRMT-2 has a role in modulating inflammation and the immune response. Also, PRMT-2 proteins can repress E2F1 transcriptional activity and cause cell cycle arrest, and thus may be used to treat or prevent cancer. PRMT-2 also methylates STAT3, and inhibition or loss of PRMT-2 function causes mammals to lose weight, eat less and become more sensitive to insulin.

The invention describes methods of modulating PRMT-2 activity or expression in cells. These methods can be used to inhibit the function of NF?B, E2F1 and STAT3 for treatment of a number of disorders, including inflammation, cancer, and diabetes.

Applications: Target for treatment and study of a number of disorders, including:

Diabetes, obesity and metabolic syndrome diseases; Inflammation and immune response-related disorders; Cancer.

Inventors: Elizabeth Nabel (NHLBI), Hiroaki Iwasaki (NHLBI), Takanobu Yoshimoto (NHLBI), and Gary Nabel (NIAID).

Patent Status: U.S. Provisional Application No. 60/466,751 filed 30 April 2003 (HHS Reference No. E-190-2003/0-US-01); PCT Application No. PCT2004/013375 filed 30 April 2004, which published as WO 2004/098634 on 18 Nov 2004 (HHS Reference No. E-190-2003/0-PCT-02); U.S. Application No. 11/263,657 filed 31 Oct 2005, which published as WO 2006/0239990 on 26 Start Printed Page 2288Oct 2006 (HHS Reference No. E-190-2003/0-US-04).

Licensing Status: Available for exclusive or nonexclusive licensing.

Licensing Contact: Tara Kirby, Ph.D.; 301/435-4426; tarak@mail.nih.gov.

Methods for Assaying Hair Follicle Growth and Development

Description of Technology: Methods of culturing functionally-intact hair follicles in a collagen matrix are useful for screening baldness treatments and the quantification and study of the effects of agents on hair follicle growth. This technology describes techniques for measuring cell proliferation or for measuring secretion of collagenolytic factors, incorporating a three-dimensional hair follicle culture system. Collagenolytic activity is essential for downgrowth of hair follicles during anagen. One described method measures the effects of a growth factor or pharmaceutical compound on cell proliferation, utilizing the incorporation of tritiated thymidine into DNA of cultured hair follicles. Also described is a method to measure the effect of growth factors on the release of collagenolytic factors, utilizing tritiated collagen or a fluorescent marker.

Applications: Assays for screening drugs or growth factors that may stimulate hair growth; Assays measuring the DNA synthesis and collagenase-secreting activity of hair follicles.

Market: An estimated 40 million men and 20 million women suffer from hair loss; The market size for hair restoration procedures in the United States is approximately $800 million.

Inventor: Stuart H. Yuspa (NCI).

Publications:

1. G Rogers, N Martinet, P Steinert, P Wynn, D Roop, A Kilkenny, D Morgan, SH Yuspa. Cultivation of murine hair follicles as organoids in a collagen matrix. J Invest Dermatol. 1987 Oct;89(4):369-379.

2. W Weinberg, P Brown, WG Stetler-Stevenson, SH Yuspa, Growth factors specifically alter hair follicle cell proliferation and collagenolytic activity alone or in combination. Differentiation. 1990 Dec;45(3):168-178.

Patent Status: U.S. Patent No. 5,616,471 issued 01 Apr 1997 (HHS Reference No. E-213-1987/1-US-01).

Licensing Status: Available for nonexclusive licensing.

Licensing Contact: Tara Kirby, Ph.D.; 301/435-4426; tarak@mail.nih.gov.

Start Signature

Dated: January 9, 2007.

Steven M. Ferguson,

Director, Division of Technology Development and Transfer, Office of Technology Transfer, National Institutes of Health.

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[FR Doc. E7-626 Filed 1-17-07; 8:45 am]

BILLING CODE 4140-01-P