Government-Owned Inventions; Availability for Licensing, 73338-73340 [E8-28614]
Download as PDF
<![CDATA[
73338
Federal Register / Vol. 73, No. 232 / Tuesday, December 2, 2008 / Notices
cell isolation technology. Please contact
John D. Hewes, PhD at 301–435–3121 or
hewesj@mail.nih.gov for more
information.
jlentini on PROD1PC65 with NOTICES
Ectopic Thymidylate Synthase
Accelerates the Development of
Hyperplastic Foci and Adenomas in
Pancreatic Islets
Description of Technology:
Thymidylate synthase (TS) is an E2F1regulated enzyme essential for DNA
synthesis and repair. Elevated levels of
TS protein and mRNA levels are
associated with many human cancers.
Previous research by the NIH inventors
has demonstrated that ectopic
expression of catalytically active TS is
sufficient to induce a transformed
phenotype in mammalian cells as
manifested by foci formation, anchorage
independent growth, and tumor
formation in nude mice. Overexpression
of hTS in murine islets provides a
model to study genetic alterations
associated with the progression from
normal cells to hyperplasia and
adenoma and suggests that this mouse
model may be useful for cancer
prevention and the development of
therapeutic strategies.
Applications:
• Transgenic mouse model to develop
cancer therapeutics.
• Drug screening for tumor reduction
and prevention.
Market: Cancer therapeutic
development.
Development Status: Thymidylate
synthase transgenic mice available.
Inventor: Maria Zajac-Kaye (NCI).
Patent Status: HHS Reference No.
E–088–2006/0—Research Tool. Patent
prosecution is not being pursued for this
technology.
Publications:
1. L Rahman, D Voeller, M Rahman,
S Lipkowitz, C Allegra, JC Barrett, FJ
Kaye, M Zajac-Kaye. Thymidylate
synthase as an oncogene: a novel role
for an essential DNA synthesis enzyme.
Cancer Cell. 2004 Apr; 5(4):341–351.
2. D Voeller, L Rahman, M ZajacKaye. Elevated levels of thymidylate
synthase linked to neoplastic
transformation of mammalian cells. Cell
Cycle. 2004 Aug; 3(8):1005–1007.
3. M Chen, L Rahman, D Voeller, E
Kastanos, SX Yang, L Geigenbaum, C
Allegra, FJ Kaye, P Steeg, M Zajac-Kaye.
Transgenic expression of human
thymidylate synthase accelerates the
development of hyperplasia and tumors
in the endocrine pancreas. Oncogene.
2007 Jul 19; 26(33):4817–4824.
Licensing Status: Available for
licensing.
VerDate Aug<31>2005
20:52 Dec 01, 2008
Jkt 217001
Licensing Contact: Betty B. Tong,
Ph.D.; 301–594–6565;
tongb@mail.nih.gov.
Collaborative Research Opportunity:
The National Cancer Institute, Medical
Oncology Branch, is seeking statements
of capability or interest from parties
interested in collaborative research to
further develop, evaluate, or
commercialize the Thymidylate
Synthase Transgenic Animal Model.
Please contact John D. Hewes, PhD at
301–435–3121 or hewesj@mail.nih.gov
for more information.
Dated: November 24, 2008.
Richard U. Rodriguez,
Director, Division of Technology Development
and Transfer, Office of Technology Transfer,
National Institutes of Health.
[FR Doc. E8–28611 Filed 12–1–08; 8:45 am]
BILLING CODE 4140–01–P
DEPARTMENT OF HEALTH AND
HUMAN SERVICES
National Institutes of Health
Government-Owned Inventions;
Availability for Licensing
National Institutes of Health,
Public Health Service, HHS.
ACTION: Notice.
AGENCY:
SUMMARY: The inventions listed below
are owned by an agency 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.
Detection and Quantification of HIV
Antigen
Description of Technology: The
invention relates to a novel, costeffective method of detecting HIV
antigens, in particular HIV Gag (p24)
antigen, in human biological samples.
The method relies on using a novel
combination of a bead coated with a
PO 00000
Frm 00099
Fmt 4703
Sfmt 4703
primary high affinity monoclonal
antibody specific for p24 antigen and a
secondary antibody conjugated with a
fluorescent label that is also specific for
p24 antigen. This detection method
requires only approximately 50 µl of
sample, and is able to detect the
presence of HIV p24 antigen over a
range of concentrations from 20,000
picograms down to 0.3 picograms with
very low intrasample variability. The
upper and lower limits of the detection
method can be adjusted by altering the
components of the assay.
Applications: Detection of HIV
antigens in biological samples.
Advantages:
• Cost-effective
• Minimal amounts of sample
required
• High sensitivity and dynamic range
Development Status: In vitro data can
be provided upon request.
Market: HIV Diagnostics.
Inventors: Jean-Charles Grivel et al.
(NICHD).
Publications: Manuscript in press.
Patent Status: U.S. Provisional
Application No. 61/082,937 filed 23 Jul
2008 (HHS Reference No. E–240–2008/
0–US–01).
Licensing Status: Available for
exclusive or non-exclusive licensing.
Licensing Contact: Kevin W. Chang,
PhD; 301–435–5018;
changke@mail.nih.gov.
Compositions and Methods for
Inhibition of Fat-Specific Protein 27
Description of Technology: FSP27
expression is regulated by PPARg, a
gene known to play a critical role in the
development of fatty liver. Overexpression of FSP27 results in an
increase in triglyceride accumulation
and an increase in cystolic vacuoles
containing lipid droplets which are
associated with development of fatty
liver disease or hepatic steatosis. This
abnormal retention of lipids in liver
cells occurs in diabetes and alcoholism
and is correlated with decreased liver
function which can often lead to
cirrhosis and sometimes death.
Presently, there are no adequate
therapies for fatty liver disease.
This technology is directed towards
compositions and methods of inhibiting
FSP27, which include antisense
compounds, small molecule inhibitors
and antibodies that target FSP27.
Application: Potential new shRNA
based therapy for steatotic liver disease
(fatty liver).
Market: Approximately 20 to 30% of
the U.S. population has some degree of
fatty liver disease, making it the most
prevalent liver disease. Meanwhile,
cirrhosis is one of the top ten causes of
death in the U.S.
E:\FR\FM\02DEN1.SGM
02DEN1
Federal Register / Vol. 73, No. 232 / Tuesday, December 2, 2008 / Notices
Development Status: Preclinical
studies are in progress.
Inventors: Frank J. Gonzalez (NCI) et
al.
Publication: K Matsusue, T Kusakabe,
T Noguchi, S Takiguchi, T Suzuki, S
Yamano, FJ Gonzalez: Hepatic steatosis
in the leptin-deficient mouse is
promoted by the PPARgamma target
gene, fat-specific protein 27. Cell Metab.
2008 Apr; 7(4):302–311.
Patent Status: U.S. Provisional
Application No. 61/043,330 filed 08 Apr
2008 (HHS Reference No. E–145–2008/
0–US–01).
Licensing Status: Available for
licensing.
Licensing Contact: Fatima Sayyid,
M.H.P.M.; 301–435–4521;
Fatima.Sayyid@hhs.nih.gov.
Collaborative Research Opportunity:
The Laboratory of Metabolism, National
Cancer Institute, is seeking statements of
capability or interest from parties
interested in collaborative research to
further develop, evaluate, or
commercialize inhibitors of FSP27 for
treatment of fatty liver disease. Please
contact John D. Hewes, PhD at 301–435–
3121 or hewesj@mail.nih.gov for more
information.
jlentini on PROD1PC65 with NOTICES
Detection of Hereditary Prostate Cancer
Description of Technology: Inherited
prostate cancer susceptibility genes with
high penetrance are responsible for 5%
to 10% of all cancer cases and up to
30% to 40% of early onset of the
disease. Previous genetic linkage studies
indicated that germline variations in a
gene or genes on Xq27 were involved in
prostate carcinogenesis. The linkage
peak for prostate cancer overlies a
region containing five SPANX genes
whose expression has been detected in
a variety of cancers. The investigators
have identified an intra-chromosomal
inversion involving more than a 400 kb
sequence in prostate cancer patients but
not in unaffected individuals. This
technology can be used as an accurate,
early prostate cancer susceptibility
diagnostics method.
Applications: High throughput
screening assay to predict patient
susceptibility to prostate cancer.
Advantages: Easy, ready to use early
stage prostate cancer diagnostic.
Development Status: The technology
is currently in the pre-clinical stage of
development.
Market:
• Among men, prostate cancer is the
most common cancer and the second
leading cause of death.
• There will be approximately
186,320 newly diagnosed cases of
prostate cancer and an estimated 28,660
VerDate Aug<31>2005
20:52 Dec 01, 2008
Jkt 217001
deaths are expected to occur in the
United States in 2008.
• An estimated 5 to 10 percent of all
prostate cancers are considered
hereditary and as many as 30% to 40%
of early onset of the disease.
Inventors: Natalay Kouprina (NCI) et
al.
Patent Status: U.S. Provisional
Application No. 61/010,209 filed 01 Jan
2008 (HHS Reference No. E–241–2007/
0–US–01).
Licensing Status: Available for
exclusive or non-exclusive licensing.
Licensing Contact: Jennifer Wong;
301–435–4633; wongje@mail.nih.gov.
Mouse Monoclonal Antibody to the
Nitrone Spin Trap 5,5-dimethyl-1pyrroline N-oxide (DMPO)
Description of Technology: Oxidative
stress resulting in the formation of
biological radicals has been implicated
in a number of human diseases, such as
cancer as well as aging. There is,
however, a paucity of reliable methods
for in vivo or ex vivo detection of radical
formation. Until now the only general
technique that allowed for the detection
of these highly reactive species was
electron spin resonance (ESR) using
spin traps. One of the most popular of
these spin traps is 5,5-dimethyl-1pyrroline N-oxide (DMPO). In the ESR
method, radicals are trapped by DMPO,
and the DMPO spin adduct signal is
measured quantitatively by an ESR
spectrometer.
The Research Tool available is a
mouse monoclonal antibody that
specifically reacts with DMPO-protein
and DMPO–DNA adducts. The
inventors have used DMPO-octanoic
acid conjugated to ovalbumin as the
antigen to develop this monoclonal
antibody. This product was assayed by
ELISA and found to be reactive against
DMPO-protein adducts at a dilution of
1 µg/ml of affinity purified mouse IgG
when used in combination with alkaline
phosphatase conjugated, affinity
purified anti-mouse IgG (Goat).
Applications:
• ELISA and Immunoblotting of
protein-DMPO adducts.
• Immuno-spin trapping analyses of
DNA radicals.
• Immunoprecipitation of proteinDMPO adducts.
Market: DMPO is one of the most
frequently used spin traps to detect free
radicals and cited in over one thousand
publications (Pubmed).
Inventors: Ronald P. Mason and
Marilyn Ehrenshaft (NIEHS).
Patent Status: HHS Reference No. E–
175–2006/0—Research Material. Patent
protection is not being pursued for this
technology.
PO 00000
Frm 00100
Fmt 4703
Sfmt 4703
73339
Licensing Status: Hybridoma
producing the monoclonal antibody and
the monoclonal antibody are available
for Biological Material Licensing.
Licensing Contact: Suryanarayana
(Sury) Vepa, PhD, J.D.; 301–435–5020;
vepas@mail.nih.gov.
HIV gp41-Membrane Proximal External
Region Arrayed on Hepatitis B Surface
Antigen Particles for HIV Diagnostic
and Vaccine Applications
Description of Technology: This
technology describes vectors encoding
the membrane proximal external region
(MPER) and select variants from HIV–1
gp41 linked to the hepatitis B surface
antigen (HBsAg) and the resulting
expressed particles for use in HIV
diagnostic and vaccine applications.
HIV–1 gp41 membrane proximal region
contains two epitopes recognized by
broadly neutralizing human monoclonal
antibodies 2F5 and 4E10. However,
immunization with gp41 MPER or the
2F5 or 4E10 epitopes have failed to raise
neutralizing antibodies. In the subject
technology, the particles were shown to
bind antibodies from broadly
neutralizing human sera and to the two
known broadly neutralizing antibodies
2F5 and 4E10 with high relative
affinities, demonstrating that the
relevant epitopes are accessible for
antibody binding and the potential
utility of the particles in diagnostic
applications. Additionally, these
particles could be used to screen phagedisplay libraries for novel broadly crossreactive neutralizing antibodies, of
which only five are currently known.
These particles could also be used for
selection of MPER specific B cells.
Lastly, these particles have been shown
to be immunogenic and raise antibodies
that recognize HIV–1 Env gp160
expressed on the cell surface. These
immunogens can elicit neutralizing
antibodies specific for HIV gp41 MPER,
the MPER of gp41 is highly conserved
across various HIV clades and therefore
is likely to generate broadly neutralizing
antibodies when administered in a
proper presentation in a lipid context as
is the case in HBsAg particles. Multiple
copies of the MPER of HIV–1 gp41
arrayed on the particles could
significantly increase the immunogenic
potential compared to monomeric
molecules. An increase of this nature
has been observed with HBsAg and HPV
virus-like particles in hepatitis B and
cervical cancer vaccines, respectively,
suggesting that particulate array may
improve the presentation of selected
epitopes to the immune system.
Applications: HIV vaccines; HIV
diagnostics.
E:\FR\FM\02DEN1.SGM
02DEN1
73340
Federal Register / Vol. 73, No. 232 / Tuesday, December 2, 2008 / Notices
Advantages: These immunogens can
elicit neutralizing antibodies specific for
HIV gp41 MPER, which is highly
conserved across various HIV clades
and therefore is likely to generate
broadly neutralizing antibodies when
administered in a proper presentation in
a lipid context as is the case in HBsAg
particles. Multiple copies of the MPER
of HIV–1 gp41 arrayed on the particles
could significantly increase the
immunogenic potential compared to
monomeric molecules.
Inventors: Richard T. Wyatt (NIAID),
Sanjay K. Phogat (NIAID), Ira Berkower
(FDA).
Patent Status:
• U.S. Provisional Application No.
60/653,930 filed 18 Feb 2005 (HHS
Reference No. E–123–2005/0–US–01).
• PCT Application No. PCT/US2006/
005613 filed 17 Feb 2006, which
published as WO 2006/112929 on 30
Nov 2006 (HHS Reference No. E–123–
2005/1–PCT–01).
• U.S. Patent Application No. 11/
816,069 filed 10 Aug 2007 (HHS
Reference No. E–123–2005/1–US–02).
Licensing Status: Available for nonexclusive or exclusive licensing.
Licensing Contact: Cristina
Thalhammer-Reyero, PhD, M.B.A.; 301/
435–4507; thalhamc@mail.nih.gov.
Dated: November 24, 2008.
Richard U. Rodriguez,
Director, Division of Technology Development
and Transfer, Office of Technology Transfer,
National Institutes of Health.
[FR Doc. E8–28614 Filed 12–1–08; 8:45 am]
BILLING CODE 4140–01–P
Dated: November 21, 2008.
Jennifer Spaeth,
Director, Office of Federal Advisory
Committee Policy.
[FR Doc. E8–28493 Filed 12–1–08; 8:45 am]
DEPARTMENT OF HEALTH AND
HUMAN SERVICES
National Institutes of Health
jlentini on PROD1PC65 with NOTICES
National Institute of Allergy and
Infectious Diseases; Notice of Closed
Meetings
Pursuant to section 10(d) of the
Federal Advisory Committee Act, as
amended (5 U.S.C. Appendix 2), notice
is hereby given of the following
meetings.
The meetings will be closed to the
public in accordance with the
provisions set forth in sections
552b(c)(4) and 552b(c)(6), Title 5 U.S.C.,
as amended. The grant applications and
the discussions could disclose
confidential trade secrets or commercial
property such as patentable material,
and personal information concerning
individuals associated with the grant
applications, the disclosure of which
would constitute a clearly unwarranted
invasion of personal privacy.
VerDate Aug<31>2005
20:52 Dec 01, 2008
Jkt 217001
Name of Committee: National Institute of
Allergy and Infectious Diseases Special
Emphasis Panel, Transmission and
Pathogenesis of HIV in Women
Date: December 10–12, 2008.
Time: 8:30 a.m. to 5 p.m.
Agenda: To review and evaluate grant
applications.
Place: Bethesda North Marriott Hotel and
Conference Center, 5701 Marinelli Road,
Bethesda, MD 20852.
Contact Person: Thames E. Pickett, PhD,
Scientific Review Officer, Scientific Review
Program, Division of Extramural Activities,
NIH/NIAID/DHHS, 6700B Rockledge Drive,
MSC 7616, Bethesda, MD 20892–7616, 301–
496–2550, pickettte@niaid.nih.gov.
This notice is being published less than 15
days prior to the meeting due to the timing
limitations imposed by the review and
funding cycle.
Name of Committee: National Institute of
Allergy and Infectious Diseases Special
Emphasis Panel, Deciphering Pathogenisis
for Developing Effective Therapies for Viral
Infections.
Date: December 15, 2008.
Time: 9:30 a.m. to 12:30 p.m.
Agenda: To review and evaluate grant
applications.
Place: National Institutes of Health, 6700B
Rockledge Drive, Bethesda, MD 20817.
(Telephone Conference Call)
Contact Person: Edward W. Schroder, PhD,
Scientific Review Officer, Scientific Review
Program, Division of Extramural Activities,
National Institutes of Health/NIAID, 6700B
Rockledge Drive, MSC 7616, Bethesda, MD
20892, 301–435–8537,
eschroder@niaid.nih.gov.
(Catalogue of Federal Domestic Assistance
Program Nos. 93.855, Allergy, Immunology,
and Transplantation Research; 93.856,
Microbiology and Infectious Diseases
Research, National Institutes of Health, HHS)
BILLING CODE 4140–01–P
DEPARTMENT OF HEALTH AND
HUMAN SERVICES
Substance Abuse and Mental Health
Services Administration
Current List of Laboratories Which
Meet Minimum Standards To Engage in
Urine Drug Testing for Federal
Agencies
Substance Abuse and Mental
Health Services Administration, HHS.
ACTION: Notice.
AGENCY:
SUMMARY: The Department of Health and
Human Services (HHS) notifies Federal
agencies of the laboratories currently
certified to meet the standards of
Subpart C of the Mandatory Guidelines
PO 00000
Frm 00101
Fmt 4703
Sfmt 4703
for Federal Workplace Drug Testing
Programs (Mandatory Guidelines). The
Mandatory Guidelines were first
published in the Federal Register on
April 11, 1988 (53 FR 11970), and
subsequently revised in the Federal
Register on June 9, 1994 (59 FR 29908),
on September 30, 1997 (62 FR 51118),
and on April 13, 2004 (69 FR 19644).
A notice listing all currently certified
laboratories is published in the Federal
Register during the first week of each
month. If any laboratory’s certification
is suspended or revoked, the laboratory
will be omitted from subsequent lists
until such time as it is restored to full
certification under the Mandatory
Guidelines.
If any laboratory has withdrawn from
the HHS National Laboratory
Certification Program (NLCP) during the
past month, it will be listed at the end,
and will be omitted from the monthly
listing thereafter.
This notice is also available on the
Internet at https://
www.workplace.samhsa.gov and https://
www.drugfreeworkplace.gov.
FOR FURTHER INFORMATION CONTACT: Mrs.
Giselle Hersh, Division of Workplace
Programs, SAMHSA/CSAP, Room 2–
1042, One Choke Cherry Road,
Rockville, Maryland 20857; 240–276–
2600 (voice), 240–276–2610 (fax).
SUPPLEMENTARY INFORMATION: The
Mandatory Guidelines were developed
in accordance with Executive Order
12564 and section 503 of Public Law
100–71. Subpart C of the Mandatory
Guidelines, ‘‘Certification of
Laboratories Engaged in Urine Drug
Testing for Federal Agencies,’’ sets strict
standards that laboratories must meet in
order to conduct drug and specimen
validity tests on urine specimens for
Federal agencies. To become certified,
an applicant laboratory must undergo
three rounds of performance testing plus
an on-site inspection. To maintain that
certification, a laboratory must
participate in a quarterly performance
testing program plus undergo periodic,
on-site inspections.
Laboratories which claim to be in the
applicant stage of certification are not to
be considered as meeting the minimum
requirements described in the HHS
Mandatory Guidelines. A laboratory
must have its letter of certification from
HHS/SAMHSA (formerly: HHS/NIDA)
which attests that it has met minimum
standards.
In accordance with Subpart C of the
Mandatory Guidelines dated April 13,
2004 (69 FR 19644), the following
laboratories meet the minimum
standards to conduct drug and specimen
validity tests on urine specimens:
E:\FR\FM\02DEN1.SGM
02DEN1
]]>Agencies
[Federal Register Volume 73, Number 232 (Tuesday, December 2, 2008)]
[Notices]
[Pages 73338-73340]
From the Federal Register Online via the Government Printing Office [www.gpo.gov]
[FR Doc No: E8-28614]
-----------------------------------------------------------------------
DEPARTMENT OF HEALTH AND HUMAN SERVICES
National Institutes of Health
Government-Owned Inventions; Availability for Licensing
AGENCY: National Institutes of Health, Public Health Service, HHS.
ACTION: Notice.
-----------------------------------------------------------------------
SUMMARY: The inventions listed below are owned by an agency 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.
Detection and Quantification of HIV Antigen
Description of Technology: The invention relates to a novel, cost-
effective method of detecting HIV antigens, in particular HIV Gag (p24)
antigen, in human biological samples. The method relies on using a
novel combination of a bead coated with a primary high affinity
monoclonal antibody specific for p24 antigen and a secondary antibody
conjugated with a fluorescent label that is also specific for p24
antigen. This detection method requires only approximately 50 [mu]l of
sample, and is able to detect the presence of HIV p24 antigen over a
range of concentrations from 20,000 picograms down to 0.3 picograms
with very low intrasample variability. The upper and lower limits of
the detection method can be adjusted by altering the components of the
assay.
Applications: Detection of HIV antigens in biological samples.
Advantages:
Cost-effective
Minimal amounts of sample required
High sensitivity and dynamic range
Development Status: In vitro data can be provided upon request.
Market: HIV Diagnostics.
Inventors: Jean-Charles Grivel et al. (NICHD).
Publications: Manuscript in press.
Patent Status: U.S. Provisional Application No. 61/082,937 filed 23
Jul 2008 (HHS Reference No. E-240-2008/0-US-01).
Licensing Status: Available for exclusive or non-exclusive
licensing.
Licensing Contact: Kevin W. Chang, PhD; 301-435-5018;
changke@mail.nih.gov.
Compositions and Methods for Inhibition of Fat-Specific Protein 27
Description of Technology: FSP27 expression is regulated by
PPAR[gamma], a gene known to play a critical role in the development of
fatty liver. Over-expression of FSP27 results in an increase in
triglyceride accumulation and an increase in cystolic vacuoles
containing lipid droplets which are associated with development of
fatty liver disease or hepatic steatosis. This abnormal retention of
lipids in liver cells occurs in diabetes and alcoholism and is
correlated with decreased liver function which can often lead to
cirrhosis and sometimes death. Presently, there are no adequate
therapies for fatty liver disease.
This technology is directed towards compositions and methods of
inhibiting FSP27, which include antisense compounds, small molecule
inhibitors and antibodies that target FSP27.
Application: Potential new shRNA based therapy for steatotic liver
disease (fatty liver).
Market: Approximately 20 to 30% of the U.S. population has some
degree of fatty liver disease, making it the most prevalent liver
disease. Meanwhile, cirrhosis is one of the top ten causes of death in
the U.S.
[[Page 73339]]
Development Status: Preclinical studies are in progress.
Inventors: Frank J. Gonzalez (NCI) et al.
Publication: K Matsusue, T Kusakabe, T Noguchi, S Takiguchi, T
Suzuki, S Yamano, FJ Gonzalez: Hepatic steatosis in the leptin-
deficient mouse is promoted by the PPARgamma target gene, fat-specific
protein 27. Cell Metab. 2008 Apr; 7(4):302-311.
Patent Status: U.S. Provisional Application No. 61/043,330 filed 08
Apr 2008 (HHS Reference No. E-145-2008/0-US-01).
Licensing Status: Available for licensing.
Licensing Contact: Fatima Sayyid, M.H.P.M.; 301-435-4521;
Fatima.Sayyid@hhs.nih.gov.
Collaborative Research Opportunity: The Laboratory of Metabolism,
National Cancer Institute, is seeking statements of capability or
interest from parties interested in collaborative research to further
develop, evaluate, or commercialize inhibitors of FSP27 for treatment
of fatty liver disease. Please contact John D. Hewes, PhD at 301-435-
3121 or hewesj@mail.nih.gov for more information.
Detection of Hereditary Prostate Cancer
Description of Technology: Inherited prostate cancer susceptibility
genes with high penetrance are responsible for 5% to 10% of all cancer
cases and up to 30% to 40% of early onset of the disease. Previous
genetic linkage studies indicated that germline variations in a gene or
genes on Xq27 were involved in prostate carcinogenesis. The linkage
peak for prostate cancer overlies a region containing five SPANX genes
whose expression has been detected in a variety of cancers. The
investigators have identified an intra-chromosomal inversion involving
more than a 400 kb sequence in prostate cancer patients but not in
unaffected individuals. This technology can be used as an accurate,
early prostate cancer susceptibility diagnostics method.
Applications: High throughput screening assay to predict patient
susceptibility to prostate cancer.
Advantages: Easy, ready to use early stage prostate cancer
diagnostic.
Development Status: The technology is currently in the pre-clinical
stage of development.
Market:
Among men, prostate cancer is the most common cancer and
the second leading cause of death.
There will be approximately 186,320 newly diagnosed cases
of prostate cancer and an estimated 28,660 deaths are expected to occur
in the United States in 2008.
An estimated 5 to 10 percent of all prostate cancers are
considered hereditary and as many as 30% to 40% of early onset of the
disease.
Inventors: Natalay Kouprina (NCI) et al.
Patent Status: U.S. Provisional Application No. 61/010,209 filed 01
Jan 2008 (HHS Reference No. E-241-2007/0-US-01).
Licensing Status: Available for exclusive or non-exclusive
licensing.
Licensing Contact: Jennifer Wong; 301-435-4633;
wongje@mail.nih.gov.
Mouse Monoclonal Antibody to the Nitrone Spin Trap 5,5-dimethyl-1-
pyrroline N-oxide (DMPO)
Description of Technology: Oxidative stress resulting in the
formation of biological radicals has been implicated in a number of
human diseases, such as cancer as well as aging. There is, however, a
paucity of reliable methods for in vivo or ex vivo detection of radical
formation. Until now the only general technique that allowed for the
detection of these highly reactive species was electron spin resonance
(ESR) using spin traps. One of the most popular of these spin traps is
5,5-dimethyl-1-pyrroline N-oxide (DMPO). In the ESR method, radicals
are trapped by DMPO, and the DMPO spin adduct signal is measured
quantitatively by an ESR spectrometer.
The Research Tool available is a mouse monoclonal antibody that
specifically reacts with DMPO-protein and DMPO-DNA adducts. The
inventors have used DMPO-octanoic acid conjugated to ovalbumin as the
antigen to develop this monoclonal antibody. This product was assayed
by ELISA and found to be reactive against DMPO-protein adducts at a
dilution of 1 [mu]g/ml of affinity purified mouse IgG when used in
combination with alkaline phosphatase conjugated, affinity purified
anti-mouse IgG (Goat).
Applications:
ELISA and Immunoblotting of protein-DMPO adducts.
Immuno-spin trapping analyses of DNA radicals.
Immunoprecipitation of protein-DMPO adducts.
Market: DMPO is one of the most frequently used spin traps to
detect free radicals and cited in over one thousand publications
(Pubmed).
Inventors: Ronald P. Mason and Marilyn Ehrenshaft (NIEHS).
Patent Status: HHS Reference No. E-175-2006/0--Research Material.
Patent protection is not being pursued for this technology.
Licensing Status: Hybridoma producing the monoclonal antibody and
the monoclonal antibody are available for Biological Material
Licensing.
Licensing Contact: Suryanarayana (Sury) Vepa, PhD, J.D.; 301-435-
5020; vepas@mail.nih.gov.
HIV gp41-Membrane Proximal External Region Arrayed on Hepatitis B
Surface Antigen Particles for HIV Diagnostic and Vaccine Applications
Description of Technology: This technology describes vectors
encoding the membrane proximal external region (MPER) and select
variants from HIV-1 gp41 linked to the hepatitis B surface antigen
(HBsAg) and the resulting expressed particles for use in HIV diagnostic
and vaccine applications. HIV-1 gp41 membrane proximal region contains
two epitopes recognized by broadly neutralizing human monoclonal
antibodies 2F5 and 4E10. However, immunization with gp41 MPER or the
2F5 or 4E10 epitopes have failed to raise neutralizing antibodies. In
the subject technology, the particles were shown to bind antibodies
from broadly neutralizing human sera and to the two known broadly
neutralizing antibodies 2F5 and 4E10 with high relative affinities,
demonstrating that the relevant epitopes are accessible for antibody
binding and the potential utility of the particles in diagnostic
applications. Additionally, these particles could be used to screen
phage-display libraries for novel broadly cross-reactive neutralizing
antibodies, of which only five are currently known. These particles
could also be used for selection of MPER specific B cells. Lastly,
these particles have been shown to be immunogenic and raise antibodies
that recognize HIV-1 Env gp160 expressed on the cell surface. These
immunogens can elicit neutralizing antibodies specific for HIV gp41
MPER, the MPER of gp41 is highly conserved across various HIV clades
and therefore is likely to generate broadly neutralizing antibodies
when administered in a proper presentation in a lipid context as is the
case in HBsAg particles. Multiple copies of the MPER of HIV-1 gp41
arrayed on the particles could significantly increase the immunogenic
potential compared to monomeric molecules. An increase of this nature
has been observed with HBsAg and HPV virus-like particles in hepatitis
B and cervical cancer vaccines, respectively, suggesting that
particulate array may improve the presentation of selected epitopes to
the immune system.
Applications: HIV vaccines; HIV diagnostics.
[[Page 73340]]
Advantages: These immunogens can elicit neutralizing antibodies
specific for HIV gp41 MPER, which is highly conserved across various
HIV clades and therefore is likely to generate broadly neutralizing
antibodies when administered in a proper presentation in a lipid
context as is the case in HBsAg particles. Multiple copies of the MPER
of HIV-1 gp41 arrayed on the particles could significantly increase the
immunogenic potential compared to monomeric molecules.
Inventors: Richard T. Wyatt (NIAID), Sanjay K. Phogat (NIAID), Ira
Berkower (FDA).
Patent Status:
U.S. Provisional Application No. 60/653,930 filed 18 Feb
2005 (HHS Reference No. E-123-2005/0-US-01).
PCT Application No. PCT/US2006/005613 filed 17 Feb 2006,
which published as WO 2006/112929 on 30 Nov 2006 (HHS Reference No. E-
123-2005/1-PCT-01).
U.S. Patent Application No. 11/816,069 filed 10 Aug 2007
(HHS Reference No. E-123-2005/1-US-02).
Licensing Status: Available for non-exclusive or exclusive
licensing.
Licensing Contact: Cristina Thalhammer-Reyero, PhD, M.B.A.; 301/
435-4507; thalhamc@mail.nih.gov.
Dated: November 24, 2008.
Richard U. Rodriguez,
Director, Division of Technology Development and Transfer, Office of
Technology Transfer, National Institutes of Health.
[FR Doc. E8-28614 Filed 12-1-08; 8:45 am]
BILLING CODE 4140-01-P
