03-15547. Government-Owned Inventions; Availability for Licensing

AGENCY:

National Institutes of Health, Public Health Service, DHHS.

ACTION:

Notice.

SUMMARY:

The inventions listed below are owned by agencies 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: [phone]; fax: [phone]. A signed Confidential Disclosure Agreement will be required to receive copies of the patent applications.

Protein Arginine N-methyltransferase 2 (PRMT-2)

Dr. Elizabeth Nabel (NHLBI)

DHHS Reference No. E-190-2003

Licensing Contact: Marlene Shinn-Astor; 301/435-4426; [e-mail]

The Protein Arginine Methyltansferases (PRMTs) include a family of proteins with related putative methyltransferase domains that modify chromatin and regulate cellular transcription. These PRMTs catalyze the posttranslational methylation of arginine residues in proteins, resulting in the mono- and dimethylation of arginine on the guanidine group.

The NIH announces the characterization of one member of the PRMT family, PRMT-2. It has been found that PRMT-2 proteins can modulate the activity of Nuclear Factor kappa B (NFκB) and STAT3. PRMT-2 inhibits NFκB dependent transcription by causing nuclear accumulation of IκBα, which concomitantly decreases nuclear NFκB DNA binding. PRMT-2 modulates glucose and lipid metabolism, and controls body weight. The regulation of leptin and insulin signaling by PRMT-2 methylation of STAT3 may be a new target for treatment of diabetes and metabolic syndrome diseases such as type2 diabetes mellitus and hyperlipidemia. By screening for drugs that modulate PRMT-2 activity or expression, or cellular factors that are influenced by PRMT-2, one will be able to treat or prevent diseases such as, inflammation, allergies, cancer, obesity, diabetes, hyperlipidemia, adult respiratory distress syndrome (ARDS), asthma, allograft rejection, vasculitis, and vascular restenosis, as well as other conditions that are typically responsive to inhibition of NFκB or that are responsive to methylated STAT3.

Mouse Monoclonal Antibodies Against Human IKKgamma/NEMO Protein

Dr. Kuan-Teh Jeang (NIAID)

DHHS Reference No. E-118-2003—Research Tool

Licensing Contact: Marlene Shinn-Astor; 301/435-4426; [e-mail].

NF-kB has been found to be important in immune responses, cell proliferation, apoptosis, and in organ development. Several years ago it was discovered that an IKKgamma/NEMO protein was essential as an adaptor molecule to mediate TNF-alpha, IL-1, and oncoprotein induced activation of NF-kB. Mutation in IKKgamma/NEMO also results in two human genetic diseases, Familial incontinentia pigmenti and hypohidrotic/anhidrotic ectodermal dysplasia. The NIH announces mouse monoclonal antibodies to IKKgamma/NEMO that are far superior to other immunological reagents. It is anticipated that the antibodies would have both research and diagnostic capabilities.

Method for Preparing 17α-acetoxy-11β-(4,N,N-dimethylaminophenyl)-19-norpregna-4,9-diene-3,20-dione, Intermediates Thereof, and Methods for the Preparation of Such Intermediates

H.K. Kim, et al. (NICHD)

DHHS Reference No. E-113-2002/0-US-01

Licensing Contact: Marlene Shinn-Astor; 301/435-4426; [e-mail].

The compound 17α-acetoxy-11β-(4-N,N-dimethylamino-phenyl)-19-norpregna-4,9-diene-3,20-dione (CDB-2914) is a well known steroid which possesses antiprogestational and antiglucocorticodal activity. CDB-2914 could be used in contraception and therapeutic applications, including fibroids and endometriosis. The NIH announces improvements in the process of producing CDB-2914. The new process shortens the overall number of synthetic steps from seven to five and shows an improvement in yield from 13% to 20%.

This research is further described in Rao et al., Steroids, 65 (2000), 395-400.

Dated: June 13, 2003.

Steven M. Ferguson,

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