[Federal Register: December 30, 1998 (Volume 63, Number 250)]
[Notices]               
[Page 71934-71935]
From the Federal Register Online via GPO Access [wais.access.gpo.gov]
[DOCID:fr30de98-68]

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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., Patent and licensing Specialist, Office of Technology 
Transfer, National Institutes of Health, 6011 Executive Boulevard, 
Suite 325, Rockville, Maryland 20852-3804; telephone 301/496-7057 ext. 
245; fax: 301/402-0220; e-mail: sr156v@nih.gov. A signed Confidential 
Disclosure Agreement will be required to receive copies of the patent 
applications.

cDNA Encoding A Gene, BOG (B5T Over-Expressed Gene), And Its 
Protein Product

    SS Thorgeirsson, JT Woitach, M Zhang (NCI) Serial Nos. 60/079,567 
filed 27 Mar 98 and 60/075,922 filed 25 Feb 98.
    These applications describe a newly identified gene, termed BOG 
(B5t Over-Expressed Gene), and its protein product. Rat, murine and 
human homologs of the gene are described. Human BOG has been mapped to 
chromosome 20 and murine BOG to chromosome 2.
    The applications describe the binding of the BOG gene product with 
the gene product pRb, of the well-known tumor suppressor gene RB ( 
retinoblastoma susceptibility gene). The complex formed between Rb and 
BOG typically does not contain E2F-1 in vivo. This binding property 
suggests that cells which are transformed/transfected with cDNA or 
other functional nucleotide sequences which encode the BOG gene product 
will be useful as tools for studying cell cycle control and 
oncogenesis.
    Studies using rat liver epithelial cell (RLE) lines which are 
resistant to the growth inhibitory effects of TGF-<greek-b>1 and 
primary liver tumors have been shown to over-express BOG. In addition, 
when normal RLE continuously over-express BOG the cells become 
transformed and the transformed cells are able to form hepatolblastoma-
like tumors when transplanted into nude mice. BOG antisense nucleotides 
can be used to restore sensitivity to TGF-<greek-b> in cells which 
over-express BOG. Therefore, biologics derived from BOG may be useful 
as diagnostics or therapeutics.

Thymosin <greek-a>1 Promotes Tissue Repair, Angiogenesis and Cell 
Migration

    KM Malinda, HD Kleinman (NIDCR), RK Maheshwari, and A Goldstein, 
Serial Nos. 09/186,476 filed 04 Nov 98, 60/069,590 filed 12 Dec 97, and 
60/065,032 filed 10 Nov 97.
    These applications describe the use of the compound thymosin 
<greek-a>1 as an agent for promoting wound healing. Thymosin <greek-a>1 
is a small, 28 mer, peptide which can be made by chemical synthesis or 
recombinantly. Studies using a punch model for wounds in rats have 
shown that providing thymosin <greek-a>1 either intraperitoneally or 
topically accelerates wound healing. In addition, thmosin <greek-a>1 
has been shown to promote endothelial and keratinoctye cell migration 
in vivo and to promote angiogenesis in vivo.
    This work has been published in J. Immunol. 160(2); 1001-6 (Jan 15, 
1998).

Double-Stranded RNA Dependent Protein Kinase Derived Peptides To 
Promote Proliferation of Cells and Tissues in a Controlled Manner

    DP Bottaro (NCI), R Petryshyn (EM), Serial No. PCT/US97/14350 filed 
29 Jul 97 and 60/023,307 filed 30 Jul 97
    These applications describe a number of peptides having a minimum 
size of eight (8) amino acids which act as

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antagonists of PKR (Protein Kinase R). PKR is a critical enzyme in the 
interferon signaling pathway which has been implicated in cross-talk 
between the interferon signaling pathway and the TNF-<greek-a> 
apoptosis signaling pathway. The peptide antagonists described herein 
may be use to inhibit apoptosis or to stimulate cell proliferation 
under conditions of cell cycle arrest, reduced growth or quiescence 
leading to possible applications in wound healing, cell culture, or 
skin grafts.
    A portion of this work has appeared in Virology 222 (1): 193-200 
(August 1, 1996).

AAV4 Vector and Uses Thereof

    JA Chiorini, RM Kotin, B Safer (NHLBI), Serial No. 60/025,934 filed 
09 Sept 96 and PCT/US97/16266
    These patent applications describe the cloning and characterization 
of the full-length genome of adeno-associated virus type 4 (AAV4). 
AAV4, like other members of the AAV family may be useful as a vector 
for gene therapy.
    When compared to AAV2 AAV4 may be better suited as a vector due to 
its larger size which permits efficient encapsidation of a larger 
recombinant genome, its greater buoyant density which allows for easier 
separation of AAV4 from contaminating helper virus. Other 
characteristics of AAV4 which distinguish it from AAV2 and AAV3 are its 
expanded promoter region, its distinct capsid protein, its different 
tissue tropism and its ability to bind hemagluttinin (HA). While AAV4 
has several distinguishing characteristics from AAV2 and AAV3 it also 
shares significant homology, greater than 90%, with the Rep proteins of 
AAV2 and AAV3.
    Studies using a lacZ reporter gene suggest that AAV4 can transduce 
human, monkey, and rat cells. Other studies comparing transduction 
efficiencies in a number of cell lines, competition cotransduction 
experiments and the effect of trypsin on transduction efficiency 
suggest that the cellular receptor for AAV4 is distinct from that of 
AAV2.
    This research has been published in J. Virology 71(9): 6823-33 
(Sept 1997) and as PCT Publication 98/11244 (March 19, 1998).

    Dated: December 21, 1998.
Jack Spiegel, Ph.D.,
Director, Division of Technology Development and Transfer Office of 
Technology Transfer.
[FR Doc. 98-34529 Filed 12-29-98; 8:45 am]
BILLING CODE 4140-01-M