[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: gb18t@nih.gov. 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
