[Federal Register Volume 70, Number 250 (Friday, December 30, 2005)]
[Notices]
[Pages 77413-77414]
From the Federal Register Online via the Government Publishing Office [www.gpo.gov]
[FR Doc No: E5-8122]


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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.

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; 
[email protected].

    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

[[Page 77414]]

dependent 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; 
[email protected].

    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.

    Dated: December 19, 2005.
Steven M. Ferguson,
Director, Division of Technology Development and Transfer, Office of 
Technology Transfer, National Institutes of Health.
[FR Doc. E5-8122 Filed 12-29-05; 8:45 am]
BILLING CODE 4140-01-P