Government-Owned Inventions; Availability for Licensing

[Federal Register Volume 64, Number 161 (Friday, August 20, 1999)]
[Notices]
[Pages 45555-45556]
From the Federal Register Online via the Government Publishing Office [www.gpo.gov]
[FR Doc No: 99-21706]


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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, DHHS.

ACTION: Notice.

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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: 301/496-7057; fax: 301/402-0220. A 
signed Confidential Disclosure Agreement will be required to receive 
copies of the patent applications.

Surface Coating for Hot-Melt Adhesive Films

    John I. Peterson, Tristan Gorrindo (ORS), DHHS Reference No. E-015-
99/0 filed 10 May 1999.
    Licensing Contact: John Fahner-Vihtelic; 301/496-7735 ext. 270; e-
mail: jf36z@nih.gov.
    The present application describes a method and apparatus for 
applying thin-film coatings to poly(ethylene/vinyl acetate, CAS24937-
78-8) (EVA) hot-melt layers used in Laser Capture Microdissection 
(LCM). These methods result in the placement of a hard, non-adhering 
surface on the EVA layer. The placement of this layer overcomes the 
problems associated with nonspecific pickup of tissue. Analysis errors 
in tissue samples captured by laser melting are easily prevented, and 
using various brush-off or wash-off techniques the removal of undesired 
tissue material from EVA with thin-film coatings is easily 
accomplished. Additional advantages include the protection of the hard 
surface against ambient humidity and temperature variations that 
adversely affect performance. A desirable coating is one that is a 
water or water-ethanol solution since it does not deform the EVA 
surface. Three materials have been tested and are acceptable for this 
application.

A Method of Preventing Tumor Metastasis

S Rong, G Vande Woude, DL Faletto, I Tsarfaty, M Oskarsson (NCI),
Serial No. 09/248,901 filed 12 Feb 1999.
Licensing Contact: Susan S. Rucker; 301/496-7056 ext. 245; e-mail: 
sr156v@nih.gov

    This application generally relates to signal transduction involving 
hepatocyte growth factor/scatter factor (HGF/SF) and its receptor the 
met proto-oncogene. In vitro experiments have indicated that some 
tumors, such as sarcomas, exhibit metastatic behavior due to 
inappropriate HGF/SF signaling. The application describes a method 
whereby this signaling can be inhibited by a substance such as an HGF/
SF variant, an HGF/SF mimetic or an antibody or antibody fragment that 
prevents HGF/SF from binding to met.
    Several related cases are also available for licensing: U.S. Patent 
5,871,959 issued 2/16/1999 entitled ``A Method of Producing HGF/SF and 
Related Cell Lines'' and U.S. Patent 5,648,273 issued 7/15/1997 
entitled ``Hepatic growth factor receptor is the MET proto-oncogene''.

Expressed Sequence Tags of Genes Expressed in Drosophila Testes

Brian Oliver, Justen Andrews, Jining Lu (NIDDK)
DHHS Reference No. E-023-99/0.
Licensing Contact: Peter Soukas, 301/496-7056 ext. 268; e-mail: 
ps193c@nih.gov.

    This unpatented invention describes the generation of high quality 
Expressed Sequence Tags (ESTs) of genes expressed in Drosophila testes 
obtained through ongoing sequencing. Approximately sixty percent (60%) 
of the generated ESTs have no significant homology to existing 
Drosophila EST sets. Thus, this invention represents a valuable 
addition to the Drosophila unigene set. Additionally, approximately 
forty-three percent (43%) of these ESTs have no significant similarity 
to sequences to any other organism in public databases, representing 
possibly previously unidentified genes.
    Approximately 3000 sequence reads have been submitted to dbEST at 
the present time. The ESTs were prepared from a library derived from 
poly-A+ RNA isolated from 700 y* w67c1 
1-5 day post-eclosion testis. cDNA was cloned in the Stratagene Uni-Zap 
XR vector according to the manufacturer's instructions. The primary 
unamplified library contained 8  x  106 plaque forming units 
(pfu). The library was amplified once (1  x  106 pfu yielded 
1.75  x  1012 pfu). There are no NIH patent rights 
associated with this invention; it is available for commercialization 
through a Biological Materials License Agreement.

Fibroblast Growth Factor Receptor Activating Gene 1 (FRAG1), 
Related Proteins and Methods

MV Lorenzi (NCI), T Miki (NCI)
Serial No. 09/202,548 filed 15 Dec 98 claiming priority to PCT/US97/
10660 filed 18 Jun 97 and 60/020,009 filed 18 Jun 96
Licensing Contact: Susan S. Rucker; 301/496-7056 ext. 245; e-mail: 
sr156v@nih.gov

    These applications describe the identification, isolation and 
cloning of the human gene named Fibroblast Growth Factor Receptor 
Activating Gene I (FRAG1) as well as its rat homolog. A full length 
clone of the human FRAG1 was deposited and the partial sequence (about 
90%) is disclosed. The complete sequence of the rat homolog is 
disclosed.
    The gene for FRAG1 encodes a protein which activates the known 
growth factor receptor, Fibroblast Growth Factor Receptor 2 (FGFR2).

[[Page 45556]]

FRAG1, when fused to FGFR2, leads to a transformed phenotype when 
transfected into cells and enhanced levels of phosphorylation/
activation of FGFR2. The FGFR2-FRAG1 fusion protein was isolated from 
an osteosarcoma. Products derived from the FRAG1 cDNA, protein or 
antibodies which recognize the FRAG1 antigen are likely to be useful as 
diagnostics, therapeutics and research reagents.
    This work has appeared, in part, in Lorenzi, MV, et al. ``FRAG1, a 
gene that potently activates fibroblast growth factor receptor by C-
terminal fusion through chromosomal rearrangement'' PNAS, USA 93(17): 
8956-61 (Aug. 20, 1996).

Spontaneous Breathing Apparatus and Method

Theodor Kolobow (NHLBI)
Serial No. 08/933,003 filed 18 Sep 1997.
Licensing Contact: Girish Barua; 301/496-7056 ext. 263; e-mail: 
gb18t@nih.gov

    A novel assisted breathing system and method has been developed to 
greatly decrease/eliminate work of breathing, and is under the total 
control of a patient.
    The system includes a minitracheostomy tube, a reverse thrust gas 
insufflation catheter introduced through a special minitracheostomy 
tube to deliver well humidified air/oxygen to near the carina, and a 
threshold valve to limit airway plateau pressure. Inspiration is 
effected through spontaneous closing of the glottic opening, while 
expiration follows opening of the glottis. Such breathing is under the 
exclusive, spontaneous control of a patient to determine respiratory 
rate and tidal volumes. Lung inflation is hence passive, and accounts 
for the greatly decreased (even zero) work of breathing. Speech, cough 
and swallowing remain unimpeded.

    Dated: August 16, 1999.
Jack Spiegel,
Director, Division of Technology Development and Transfer, Office of 
Technology Transfer, National Institutes of Health.
[FR Doc. 99-21706 Filed 8-19-99; 8:45 am]
BILLING CODE 4140-01-M