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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.

Molecular Cloning and Characterization of SNAPIN: A Synaptic Vesicle Protein Implicated in Neurotransmitter

Dr. Zu-hang Sheng et al. (NINDS),

HHS Reference No. E-182-1999/0—Research Tool,

Licensing Contact: Marlene Shinn-Astor; 301/435-4426; shinnm@mail.nih.gov.

Neurotransmitter release is dependent on a binding complex (designated as SNAR) of three proteins, synaptic-vesicle-associated protein synaptobrevin/VAMP, syntaxin and SNAP-25 (snaptosome-associated protein-25) with results in a calcium Start Printed Page 77414dependent fusion between synaptic vesicles and the presynaptic terminal. SNAPIN, a neuron specific protein found predominately on synaptic vesicles, binds to the SNAR complex, most likely to the SNAP-25. Although the complete function of SNAPIN has not been determined, it appears to regulate a step between vesicle docketing and neurotransmitter release through its ability to potentiate the interaction of synaptotagmin with the SNAREs, which then leads to the final fusion step triggered by calcium influx into nerve terminals through voltage-dependent calcium channels.

A Mouse With a Targeted Mutation in the Uncoupling Protein-3 (upc3) Gene

Dr. Marc Reitman et al. (NIDDK),

HHS Reference No. E-031-1999/0—Research Tool,

Licensing Contact: Marlene Shinn-Astor; 301/435-4426; shinnm@mail.nih.gov.

The NIH announces the development of a transgenic mouse with a targeted mutation in the ucp3 gene. The ucp3 gene is implicated I the function of regulating energy metabolism. This regulatory function is thought to be accomplished by changing metabolic efficiency (causing energy expended as heat rather than used for ADP/ATP conversion) and/or by participating in fat metabolism. The mutation should inactivate the ucp3 function and the mouse provided a testing vehicle for the above hypotheses.

If in fact ucp3 is involved in energy efficiency and/or fat metabolism, then variation in its sequence or level of expression may explain some of human obesity. If ucp3 is involved in fever generation, it would be of interest in testing inactivating drugs.

In summary, this mouse model provides a model for evaluating the role of ucp3 in obesity, energy efficiency, and selective use of energy sources (i.e., fat vs. carbohydrates), body temperature regulation, such as fever, or other forms of stimulated thermogenesis (e.g., by diet of dietary fat). For example, a drug candidate thought to act via ucp3 should have no effect in these mice.

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Dated: December 19, 2005.

Steven M. Ferguson,

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

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[FR Doc. E5-8122 Filed 12-29-05; 8:45 am]

BILLING CODE 4140-01-P