[Federal Register Volume 65, Number 79 (Monday, April 24, 2000)]
[Notices]
[Pages 21773-21774]
From the Federal Register Online via the Government Publishing Office [www.gpo.gov]
[FR Doc No: 00-10180]


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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 contacting Susan S. 
Rucker, J.D., at the Office of Technology Transfer, National Institutes 
of Health, 6011 Executive Boulevard, Suite 325, Rockville, Maryland 
20852-3804; telephone: 301/496-7056 ext. 245; fax: 301/402-0220; e-
mail: <a href="/cdn-cgi/l/email-protection#f88b8ac9cdce8eb8969190d69f978e"><span class="__cf_email__" data-cfemail="3e4d4c0f0b08487e50575610595148">[email protected]</span></a>. A signed Confidential Disclosure Agreement will 
be required to receive copies of the patent applications.

Hybrid Adeno-Retroviral Vector for the Transformation of Cells

C Zheng, B O'Connell, BJ Baum (NIDCR)
Serial No. E-258-98/0 filed 31 Jan 2000

    The invention described and claimed in this patent application 
provides for novel hybrid vectors which may be used for cell 
transformation, either in vivo or in vitro. The hybrid vectors have an 
adenoviral backbone with retroviral long terminal repeats (LTRs). Such 
vectors are capable of transforming dividing or non-dividing cells and 
integrate stably into the chromosome providing a means of efficient, 
reliable, long-term gene expression. The vector was packaged as a 
recombinant adenovirus and delivered to the target cell. Unlike other 
chimeric or hybrid vector systems, only a single vector is required to 
deliver a transgene of interest, and retroviral structural proteins are 
not required.
    This work has been published in part in Nature Biotechnology Zheng, 
et al. 18(2): 176-180 (Feb 2000).

Calcium Channel Compositions and Methods of Use Thereof

MI Lerman (NCI) et al.
Serial No. 09/470,443 filed 22 Dec 1999 and 60/114,359 filed 30 Dec 
1998 (now abandoned)

    This invention described in this patent application relates to the 
identification, isolation and cloning of a three cDNAs identified 
during a search of the short arm of chromosome 3 for a tumor suppressor 
gene (TSG) associated with lung cancer. The cDNA's are alternative 
isoforms which encode a protein which functions as a subunit of L-type 
voltage-dependent calcium channel. Type L voltage-dependent calcium 
channels represent one of five families of calcium channels, L, R, P, 
N, Q, which have been identified. Type L voltage-dependent calcium 
channels are found in a wide variety of tissues including the brain, 
muscle and the endocrine system.
    The gene has been mapped to the short arm of chromosome 3 at 
3p21.3. The gene, which corresponds to this cDNA is an alpha2delta-2 
(<greek-a>2<greek-d>-2) subunit, and has been shown to be deleted in 
lung and breast cancer. The scientists have demonstrated that the 
expression of this calcium channel has been shut off in lung cancer 
cells and hypothesize that this may lead to a malignant phenotype. 
Other cancers which may be associated with this <greek-a>2<greek-d>-2 
subunit include cervical cancer and head and neck carcinoma. Other non-
malignant diseases which may also be associated with this 
<greek-a>2<greek-d>-2 subunit include CNS diseases and cardiovascular 
diseases.
    Possible applications of this technology include its use in drug 
screening assays; its use as an early diagnostic marker and/or as a 
prognostic or treatment indicator; its use in gene therapy where 
defective cells would be reconstituted with the gene and as a 
therapeutic agent for clearing autoantibodies which develop toward the 
alpha2delta-2 subunit in the disease Lambert-Eton myasthenia syndrome.

Monoclonal Antibody Against Met Protein

G Vande Woude, M Oskarsson, J Resau, S Rulong, Y Chui (NCI-FCRDC)
Serial No. 60/168,835 filed 03 Dec 1999

    The invention described in this application relates to the 
Hepatocyte Growth Factor/Scatter Factor/Tumor Cytotoxic Factor (HGF/SF/
F-TCF)-met/Hepatocyte Growth Factor Receptor

[[Page 21774]]

(HGFr) pathway. In particular, the invention described in this 
application is a murine monoclonal antibody, designated D1, which 
specifically binds to an epitope in the extracellular domain of human 
HGFr/met. The monoclonal antibody can be used, for example, to 
visualize HGFr/met expression in paraffin-embedded tumor samples and in 
drug screening assays (competitive binding assays) for antagonists/
agonists of HGFr/met.

Determination of AM Binding Proteins and the Association of 
Adrenomedullin (AM) Therewith

F Cuttitta (NCI), A Martinez (NCI), R Pio (NCI), TH Elasser (USDA-ARS),
Serial No. 60/153,397 filed 10 Sep 99

    This application relates to isolation and identification of a 
polypeptide which binds to the hormone adrenomedullin designated 
adrenomedullin binding protein 1 (AMBP1). Adrenomedullin (AM), a 
peptide hormone, has been implicated in a variety of physiological 
functions including the regulation of insulin production, anti-
microbial activity, mitogenesis and angiogenesis. The activities of AM 
are believed to be mediated by a variety of binding proteins in a 
manner similar to the way in which Insulin-like Growth Factor (IGF) is 
regulated. AMBP1 has been purified to homogeneity and its amino acid 
sequence determined.
    The application is directed to methods of measuring AM levels in 
plasma based on the finding that AMBP1 binds in a specific and 
reversible competitive fashion with AM and methods of treating AM 
related disease by administering AMBP1. Other aspects of the invention 
are complexes of AM with AMBP1 and antibodies which specifically bind 
to an epitope by the complex of AM with AMBP1 as well as assays for 
detecting the complex of AM with AMBP1.
    This work has been published in part in Elsasser TH, et al. 
Endocrinology 140(10):4908-11 (Oct. 1999).
    In addition to being available for licensing the NIH is willing to 
consider interest from companies who are interested in pursuing 
commercialization opportunities through a Cooperative Research and 
Development Agreement (CRADA).

AAV5 Vector and Uses Thereof

JA Chiorini, RM Kotin (NHLBI)
Serial No. PCT/US99/11958 filed 28 May 1999 based on USSN 60/087,029 
filed 28 May 1998

    The invention described and claimed in this patent application 
provides for novel vectors and viral particles which comprise adeno-
associated virus serotype 5 (AAV5). AAV5 is genetically distinct from 
others AAVs with respect to its capsid proteins, VP1, VP2, and VP3, 
which contributes to different tissue tropisms for AAV5. The ITR and 
Rep proteins of AAV5 are also distinct which results in a biochemically 
unique mechanism of replication compared to the other AAVs. This 
difference in replication activity contributes to the fact that AAV5 is 
only able to replicate and package AAV5 ITR containing DNA in contrast 
to AAV2 which is able to replicate and package other AAV serotypes. 
Vectors produced using AAV5 proteins may be useful in gene therapy.
    AAV5 offers several advantages which make it attractive for use in 
gene therapy: (1) increased production (10-50 fold greater than AAV2); 
(2) its distinct replication mechanism when compared to AAV2; (3) its 
Rep protein and ITR regions which do not complement other serotypes; 
(4) it appears to utilize different cell surface attachment molecules 
than those of AAV type 2; and (5) improved efficiency of transduction 
of certain cell types including airway epithelial, striated muscle, 
endothelial, and neuronal cells when compared to AAV type 2.
    This work has been published, in part, in J. Virol. 73(5): 4293-98 
(May 1999) and J. Virol. 73(2): 1309-19 (Feb. 1999).

Prevention of Fetal Alcohol Syndrome and Neuronal Cell Death with 
ADNF Polypeptides

DE Brenneman (NICHD), CY Spong (NICHD), I Gozes (TAU), M Bassan (TAU), 
R Zamostiano (TAU)
Serial No. 09/267,511 filed 12 Mar 1999

    This patent application describes an extension of prior work 
related to peptides derived from proteins known as ADNF and ADNF III/
ADNP. These peptides are known as SAL (ADNF-derived) and NAP (ADNP-
derived). SAL and NAP (L-isomers) have previously been demonstrated, in 
in vitro work, to be able to prevent neuronal cell death and to protect 
against the toxic activities of a cholinotoxin suggesting that they are 
useful as therapeutics for neurodegenerative diseases. The new work 
presented in this EIR demonstrates that NAP and SAL (L-isomers), alone 
or in combination, prevent damage to neurons due to oxidative stress. 
In particular, the new work shows that NAP and SAL (L-isomers) alone or 
together are effective in preventing damage due to oxidative stress in 
a model for fetal alcohol syndrome. Thus, NAP and SAL (L-isomers), 
alone or together may be useful therapeutically to treat fetal alcohol 
syndrome.
    In addition, a number of other patent applications and patents 
related to this technology have been filed by PHS and are available for 
licensing. These include: USP 5,767,240 (PCT/US92/03109); 08/324,297 
(PCT/US95/12929); 60/037,404 (PCT/US98/07485); 09/187,330 (PCT/US99/
26213) 60/149,956; and 09/364,609.

    Dated: April 18, 2000.
Jack Spiegel,
Director, Division of Technology Development and Transfer, Office of 
Technology Transfer, National Institutes of Health.
[FR Doc. 00-10180 Filed 4-21-00; 8:45 am]
BILLING CODE 4140-01-P


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