[Federal Register Volume 64, Number 108 (Monday, June 7, 1999)]
[Notices]
[Pages 30344-30345]
From the Federal Register Online via the Government Publishing Office [www.gpo.gov]
[FR Doc No: 99-14376]


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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 Girish C. 
Barua, Ph.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. 263; fax: 301/402-0220; e-
mail: [email protected]. A signed Confidential Disclosure Agreement will be 
required to receive copies of the patent applications.

Modulation of N-Acetyl-Transferase To Improve Therapy and Prevent 
Cancer

Jerry M. Collins, Raymond W. Klecker, Aspandiar G. Katki (FDA)
DHHS Reference No. E-268-98/0 filed 16 Apr 99

    This technology describes a method in which an inhibitor of an 
arylamine N-acetyl transferase (NAT), a member of a common enzyme 
family, is administered to a human to inhibit acetylation reactions 
resulting in production of cytotoxic or carcinogenic compounds in the 
treated individual. Nearly all drugs are metabolized in the human body 
by enzymes. Although metabolism generally lowers the toxicity of drugs, 
the opposite effect is often encountered with NAT. With NAT, the 
resulting metabolite is more toxic than the parent drug. Administering 
an inhibitor of NAT with such drugs is believed to result in decreased 
toxicity to the patient because of reduced exposure to the metabolite. 
Reduced exposure to the metabolite is believed to be beneficial to 
patients because the reduction in toxicity results in the maximization 
of the benefits of the parent drug. Accordingly, this method could be 
utilized in many therapeutic areas, since drugs which are metabolized 
by NAT are used in most medical disciplines, including heart disease, 
infectious diseases, and oncology. The technology also describes the 
acetylation capacity of NAT's link to human tumors. The acetylation 
capacity can be reduced by an enzyme inhibitor which may lead to a 
decrease in human cancer. This concept identifies NAT as a novel 
target, to expand and improve a general strategy which is currently-
emerging, known as ``chemoprevention''. Finally, the technology 
describes specific inhibitors

[[Page 30345]]

of NAT in human hepatocoytes, e.g., para-amino salicylate (PAS) for 
NAT1 and dichlorphenamide for NAT2, which can be used either in 
chemoprevention of cancer or in conjunction with a chemotherapeutic 
which metabolizes NAT, potentially resulting in reduced toxicity to the 
patient. Since these inhibitors are currently-marketed drugs, clinical 
development can be accelerated, and pilot studies are already underway.

Methods for Inhibiting Chaperone Proteins

Monica G. Marcu, Leonard M. Neckers, Theodor W. Schulte (NCI)
Serial No. 60/124,135 filed 12 Mar 99

    This technology describes the use of an antibiotic, Novobiocin, 
that has been used clinically in people for many years. This compound 
and structural analogues such as chlorobiocin and coumermycin A1, which 
are coumarins, have been discovered to bind to Heat Shock Protein 90 
(Hsp90), resulting in the destabilization and proteolytic degradation 
of a number of proteins whose function and stability depend on their 
association with Hsp90. These proteins include oncogenic kinases such 
as Raf, Her2/neu(erbB2), and Src, and transcription factors such as 
mutant p53. Novobiocin has demonstrated an ability to deplete Raf from 
the spleens of mice, suggesting that it may have anti-Hsp90 biologic 
properties in humans. Novobiocin and its analogues are an improvement 
on currently known chemotherapeutics such as geldanamycin because these 
compounds lack both a quinone and a macrocycle in their chemical 
structure and are thus better tolerated and less toxic to humans at 
high dosages.

Identification of The Geldanamycins as Inhibitors of The HGF/SF-
Met-uPA Proteolytic Network

Craig Webb, Curtis Hose, Anne P. Monks, George F. Vande Woude, 
Edward A. Sausville (NCI)
Serial No. 60/119,114 filed 08 Feb 99

    This technology describes a class of compounds (Geldanamycins) as 
important inhibitors to the HGF-SF-Met-uPA-plasmin signaling pathway. 
Considerable evidence demonstrates that the HGF-SF-Met pathway plays a 
significant role in the etiology of human cancers and the formation of 
secondary metastases. These compounds have the ability to revert 
certain transformed phenotypes through down regulation of the 
expression of the Met receptor at subnanomolar concentrations. Thus, 
these compounds could have utility in the treatment and therapy of 
invasive human cancers where the HGF-SF-Met pathway is implicated.

Food Quality Indicator Device

Dwight W. Miller, Jon G. Wilkes, Eric D. Conte (FDA)
DHHS Reference No. E-093-97/1 filed 16 Jul 98

    The invention is a device which indicates the quality of frozen 
food by colorimetrically detecting bases generated by decomposition. 
The food quality indicator consists of a paper strip or other insert 
support treated with proprietary compounds for detection at 
temperatures below zero degree C of Bacteriological and/or enzymatic 
food decomposition. It operates without thawing frozen foods, and for 
excellent application for seafoods such as shrimp, fish as well as red 
meat.

Sensitive Assay for Measuring Gallium Levels in Body Tissues and 
Fluids

Edward Reed, Kang B. Lee (NCI)
Serial No. 08/355,153 filed 08 Dec 94; U.S. Patent 5,650,627 issued 
22 Jul 97

    A sensitive assay method for measuring the quantity of elemental 
gallium present in a test sample comprising a body tissue or body 
fluid. The method involves a test sample after diluting with nitric 
acid to be introduced into atomic absorption spectrometer having a 
Zeeman-effect background correction capability. Sample absorption to be 
determined at a desired wavelength while subjecting the test sample to 
an atomization and a burning in an atomic spectrometer. A correction of 
Zeeman effect to be made on the said determined absorption and 
comparing corrected absorption for the test sample with a standard 
curve.

    Dated: May 28, 1999.
Jack Spiegel,
Director, Division of Technology, Development and Transfer, Office of 
Technology Transfer.
[FR Doc. 99-14376 Filed 6-4-99; 8:45 am]
BILLING CODE 4140-01-M