Government-Owned Inventions; Availability for Licensing, 45363-45366 [2012-18651]
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Federal Register / Vol. 77, No. 147 / Tuesday, July 31, 2012 / Notices
register and existing establishments will
update their annual registration using
choices on the DRLM menu. Once you
choose to register or update your annual
registration, the system will prompt you
through the entry of information about
your establishment and your devices. If
you have any problems with this
process, email: reglist@cdrh.fda.gov or
call 301–796–7400 for assistance. (Note:
this email address and this telephone
number are for assistance with
establishment registration only, and not
for any other aspects of medical device
user fees.) Problems with BERS should
be directed to bloodregis@fda.hhs.gov or
call 301–827–3546.
D. Step Four—Enter Your DFUF Order
PIN and PCN
After completing your annual or
initial registration and device listing,
you will be prompted to enter your
DFUF order PIN and PCN, when
applicable. This process does not apply
to establishments engaged only in the
manufacture, preparation, propagation,
compounding, or processing of licensed
biologic devices. CBER will send
invoices for payment of the
establishment registration fee to such
establishments.
Dated: July 24, 2012.
Leslie Kux,
Assistant Commissioner for Policy.
[FR Doc. 2012–18647 Filed 7–30–12; 8:45 a.m.]
BILLING CODE 4160–01–P
Proposed Project: Maternal and Child
Health Bureau Performance Measures
for Discretionary Grants (OMB No.
0915–0298)—[Revision]
DEPARTMENT OF HEALTH AND
HUMAN SERVICES
Health Resources and Services
Administration
Agency Information Collection
Activities: Proposed Collection:
Comment Request
In compliance with the requirement
for opportunity for public comment on
proposed data collection projects
(section 3506(c)(2)(A) of Title 44, United
States Code, as amended by the
Paperwork Reduction Act of 1995, Pub.
L. 104–13), the Health Resources and
Services Administration (HRSA)
publishes periodic summaries of
proposed projects being developed for
submission to the Office of Management
and Budget (OMB) under the Paperwork
Reduction Act of 1995. To request more
information on the proposed project or
to obtain a copy of the data collection
plans and draft instruments, email
paperwork@hrsa.gov or call the HRSA
Reports Clearance Officer at (301) 443–
1984.
Comments are invited on: (a) The
proposed collection of information for
the proper performance of the functions
of the Agency; (b) the accuracy of the
Agency’s estimate of the burden of the
proposed collection of information; (c)
ways to enhance the quality, utility, and
clarity of the information to be
collected; and (d) ways to minimize the
burden of the collection of information
on respondents, including through the
use of automated collection techniques
or other forms of information
technology.
Number of
respondents
Form
Responses
per
respondent
The Health Resources and Services
Administration’s (HRSA) Maternal and
Child Health Bureau (MCHB) intends to
continue to collect performance data for
Special Projects of Regional and
National Significance (SPRANS),
Community Integrated Service Systems
(CISS), and other grant programs
administered by MCHB.
HRSA’s MCHB proposes to continue
using reporting requirements for
SPRANS projects, CISS projects, and
other grant programs administered by
MCHB, including national performance
measures, previously approved by OMB,
and in accordance with the
‘‘Government Performance and Results
Act (GPRA) of 1993’’ (Pub. L. 103–62).
This Act requires the establishment of
measurable goals for Federal Programs
that can be reported as part of the
budgetary process, thus linking funding
decisions with performance.
Performance measures for MCHB
discretionary grants were initially
approved in January 2003. Approval
from OMB is being sought to continue
the use of these measures. Some of these
measures are specific to certain types of
programs and will not apply to all
grantees. Through the experience of
utilizing these measures, we are
enhancing them to better reflect
program goals. Specifically, additional
outcome measures that can be utilized
by grantees that predominantly provide
infrastructure services are being
developed for submission to OMB.
The estimated response burden is as
follows:
Total
responses
Burden hours
per response
Total burden
hours
900
1
900
41
36,900
Total ..............................................................................
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Grant Report ........................................................................
900
........................
900
........................
36,900
Email comments to
paperwork@hrsa.gov or mail the HRSA
Reports Clearance Officer, Room 10–29,
Parklawn Building, 5600 Fishers Lane,
Rockville, MD 20857. Written comments
should be received within 60 days of
this notice.
DEPARTMENT OF HEALTH AND
HUMAN SERVICES
Dated: July 24, 2012.
Jennifer Riggle,
Deputy Director, Office of Management.
AGENCY:
[FR Doc. 2012–18637 Filed 7–30–12; 8:45 am]
SUMMARY:
BILLING CODE 4165–15–P
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National Institutes of Health
Government-Owned Inventions;
Availability for Licensing
National Institutes of Health,
Public Health Service, HHS.
ACTION: Notice.
The inventions listed below
are owned by an agency of the U.S.
Government and are available for
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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.
FOR FURTHER INFORMATION CONTACT:
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
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Federal Register / Vol. 77, No. 147 / Tuesday, July 31, 2012 / Notices
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.
Glial Cell Line-Derived Neurotrophic
Factor Opposite Strand (GDNFOS) for
Treatment of Neurodegenerative
Diseases
Description of Technology: Glial cell
line-derived neurotrophic factor (GDNF)
is a small human protein encoded by
the GDNF gene. GDNF has been
effective therapy in laboratory animal
models of Parkinson’s disease and
protects several types of neurons in the
brain and peripheral nervous system.
The NIDA inventors have discovered
primate-specific GDNFOS, encoded by
the opposite strand of glial cell derived
neurotrophic factor (GDNF) gene. The
GDNFOS gene encodes for novel
peptides that was found to be reduced
in human middle temporal gyrus of
Alzheimer’s disease brains. These
secreted growth proteins have potential
neurotrophic activity and they might
play a synergistic role in
neuroprotective effects of GDNF in
human brain. The NIDA inventors have
also developed antibody against
GDNFOS3 and generated compounds
that have potential pharmaceutical use.
The compounds consist of GDNFOS
nucleic acid transcripts, GDNFOS
protein or a functional fragment for
treatment of human neurodegenerative
diseases.
Potential Commercial Applications
• Synergistic role in neuroprotective
effects of GDNF.
• Alzheimer’s disease, Parkinson’s
disease, Amyotrophic lateral sclerosis,
multiple sclerosis and diseases of
peripheral organs such as diabetes
mellitus type 1.
Competitive Advantages
• Secreted novel growth peptides.
• An antibody against GDNFOS3 was
developed.
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Development Stage
• Early-stage.
• Pre-clinical.
• In vitro data available.
Inventors: Qing-Rong Liu, Mikko
Airavaara, Barry Hoffer, Brandon K
Harvey (all of NIDA).
Publication: Airavaara M, et al.
Identification of novel GDNF isoforms
and cis-antisense GDNFOS gene and
their regulation in human middle
temporal gyrus of Alzheimer disease. J
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Biol Chem. 2011 Dec 30;286(52):45093–
102. [PMID 22081608]
Intellectual Property: HHS Reference
No. E–044–2012/0—U.S. Provisional
Application No. 61/619, 296 filed 02
Apr 2012.
Licensing Contact: Betty B. Tong,
Ph.D.; 301–594–6565;
tongb@mail.nih.gov.
Collaborative Research Opportunity:
The National Institute on Drug Abuse is
seeking statements of capability or
interest from parties interested in
collaborative research to further
develop, evaluate or commercialize
GDNFOS peptide and non-coding RNAs
as therapeutic agents for
neurodegenerative diseases. For
collaboration opportunities, please
contact Vio Conley at
conleyv@mail.nih.gov.
Increased Therapeutic Effectiveness of
Immunotoxins That Use Toxin Domains
Lacking Human B-cell Epitopes
Description of Technology:
Immunotoxins kill cancer cells while
allowing healthy, essential cells to
survive. As a result, patients receiving
an immunotoxin are less likely to
experience the deleterious side-effects
associated with non-discriminate
therapies such as chemotherapy or
radiation therapy. Unfortunately, the
continued administration of
immunotoxins often leads to a reduced
patient response due to the formation of
neutralizing antibodies against
immunogenic epitopes contained within
Pseudomonas exotoxin A (PE). To
improve the therapeutic effectiveness of
PE-based immunotoxins through
multiple rounds of drug administration,
NIH inventors have sought to identify
and remove the human B-cell epitopes
within PE. Previous work demonstrated
that the removal of the murine B-cell
and T-cell epitopes from PE reduced the
immunogenicity of PE and resulted in
immunotoxins with improved
therapeutic activity. This technology
involves the identification and removal
of major human B-cell epitopes on PE
by mutation or deletion. Considering
these immunotoxins will be
administered to humans, the removal of
human immunogenic epitopes is
important. The resulting PE-based
immunotoxins have increased resistance
to the formation of neutralizing
antibodies, and are expected to have
improved therapeutic efficacy.
Potential Commercial Applications
• Essential component of
immunotoxins.
• Treatment of any disease associated
with increased or preferential
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expression a specific cell surface
receptor.
• Specific diseases include
hematological cancers, lung cancer,
ovarian cancer, breast cancer, and head
and neck cancers.
Competitive Advantages
• PE variants now include the
removal of human B-cell epitopes,
further reducing the formation of
neutralizing antibodies against
immunotoxins which contain the PE
variants.
• Less immunogenic immunotoxins
result in improved therapeutic efficacy
by permitting multiple rounds of
administration in humans.
• Targeted therapy decreases nonspecific killing of healthy, essential
cells, resulting in fewer non-specific
side-effects and healthier patients.
Development Stage: Pre-clinical.
Inventors: Ira H. Pastan et al. (NCI).
Publication: Liu W, et al.
Recombinant immunotoxin engineered
for low immunogenicity and
antigenicity by identifying and silencing
human B-cell epitopes. Proc Natl Acad
Sci USA. 2012 Jul 17;109(29):11782–7.
[PMID 22753489]
Intellectual Property: HHS Reference
No. E–263–2011/0—U.S. Provisional
Application No. 61/535,668 filed 16 Sep
2011.
Related Technologies
• PCT Patent Publication WO 2011/
032022 (HHS Reference No. E–269–
2009/0–PCT–02).
• US Patent Publication US
20100215656 A1 (HHS Reference No. E–
292–2007/0–US–06).
• US Patent Publication US
20090142341 A1 (HHS Reference No. E–
262–2005/0–US–06).
• Multiple additional patent families.
Licensing Contact: David A.
Lambertson, Ph.D.; 301–435–4632;
lambertsond@mail.nih.gov.
Collaborative Research Opportunity:
The National Cancer Institute is seeking
statements of capability or interest from
parties interested in collaborative
research to further develop, evaluate or
commercialize this technology. For
collaboration opportunities, please
contact John Hewes, Ph.D. at
hewesj@mail.nih.gov.
Novel Nitroxyl (HNO) Releasing
Compounds and Their Use in Treating
Diseases
Description of Technology: Nitroxyl
(HNO) is a chemical species that
exhibits distinct biological properties in
comparison to its oxidized product,
nitric oxide (NO). Previous
investigations have revealed that the
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distinct properties of HNO make it a
tempting species for wide therapeutic
application as it has shown potential in
the treatment of heart failure, cancer,
and other diseases in various animal
and in vitro models. Non-steroidal antiinflammatory drugs (NSAIDs), such as
aspirin and ibuprofen, are compounds
that inhibit cycloxygenase (COX)mediated conversion of arachidonic
acids to prostagladins. NSAIDs are
known for their analgesic properties and
are therapeutically involved in many
physiological functions, including the
inhibition of chronic pain and
inflammation inhibition, prevention of
heart disease, renal function, and
cancer. Prolonged use of NSAIDs can
lead to serious gastrointestinal and renal
side effects, including ulcer perforation,
upper gastrointestinal bleeding, and
death, which has limited NSAID
therapies.
The instant invention described HNOreleasing NSAIDs, which combine the
potential therapeutic benefits of HNO
and NSAIDs without the toxicities
associated with chronic NSAID use.
These HNO-releasing NSAIDs provide a
reliable controlled release of HNO
making them desirable HNO prodrugs.
The instant invention disclosed various
HNO-releasing NSAIDs and methods of
treating or preventing various disorders
with these compositions, such as
cardiovascular disorders, cancers, pain,
inflammation, and alcoholism.
Potential Commercial Applications
• Treatment of cancer.
• Treatment of cardiovascular
disease.
• Aversion therapy for alcoholism.
Competitive Advantages
• Combination of therapeutic benefits
of HNO and NSAIDs.
• Alleviated toxicity associated with
chronic NSAID use.
• Controlled release of HNO.
Description of Technology:
Researchers at NIDDK have developed
polyclonal antibodies against the G
protein, Gbeta5. Gbeta5 is a unique and
highly specialized G protein that
exhibits much less homology than other
Gbeta isoforms (∼50%) and is
preferentially expressed in brain and
neuroendocrine tissue. It is expressed
prominently in the neuronal cell
membrane, as well as in the cytosol and
nucleus. Although this distribution
pattern suggests that Gbeta5 may shuttle
information between classical G proteinsignaling elements at the plasma
membrane and the cell interior, its
function in the brain is largely
unknown.
The antibodies were separately
generated in rabbits to KLH-conjugates
of peptides from the N-terminus of
Gbeta5 (antibody ATDG) and the Cterminus of Gbeta5 (antibody SGS). The
antibodies can be used for
immunoblotting (ATDG, SGS), and
immunoprecipitation (ATDG). They can
be used to facilitate our understanding
of the unique biology and function of
Gbeta5 in brain and neurons.
Potential Commercial Applications:
These antibodies can be used for
research purposes (immunoblotting,
immunoprecipitation) by those studying
the biology and function of Gbeta5.
Competitive Advantages: Very
specific antibodies to study Gbeta5 and
G protein signaling.
Development Stage: In vitro data
available.
Inventors: William Simonds and
Jianhua Zhang (NIDDK).
Miranda KM, et al. Comparison of the NO
and HNO donating properties of
diazeniumdiolates: primary amine adducts
release HNO in vivo. J Med Chem. 2005 Dec
29;48(26):8220–8. [PMID 16366603]
Publications
1. Zhang JH and Simonds WF.
Copurification of brain G-protein beta5 with
RGS6 and RGS7. J Neurosci. 2000 Feb
1;20(3):RC59. [PMID 10648734]
2. Zhang JH, et al. Nuclear localization of
G protein beta 5 and regulator of G protein
signaling 7 in neurons and brain. J Biol
Chem. 2001 Mar 30;276(13):10284–9. [PMID
11152459]
3. Zhang S, et al. Selective activation of
effector pathways by brain-specific G protein
beta5. J Biol Chem. 1996 Dec
27;271(52):33575–9. [PMID 8969224]
4. Zachariou V, et al. An essential role for
DeltaFosB in the nucleus accumbens in
morphine action. Nat Neurosci. 2006
Feb;9(2):205–11. [PMID 16415864]
Intellectual Property: HHS Reference
No. E–019–2010/2—International Patent
Application PCT/US2011/029072 filed
18 Mar 2011.
Licensing Contact: Betty B. Tong,
Ph.D.; 301–594–6565;
tongb@mail.nih.gov.
Intellectual Property: HHS Reference
No. E–192–2006/0—Research Tool.
Patent protection is not being pursued
for this technology.
Licensing Contact: Jaime Greene,
M.S.; 301–435–5559;
greenejaime@mail.nih.gov.
Development Stage
• Early-stage.
• Pre-clinical.
Inventors: David A. Wink and Larry K.
Keefer (NCI).
Publication
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Polyclonal Antibodies for the
Specialized Signaling G Protein, Gbeta5
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Polyclonal Antibodies for the Gbeta5Associated Regulator of G Protein
Signaling Protein, RGS7
Description of Technology:
Researchers at NIDDK have developed
polyclonal antibodies against the
Regulator of G Protein Signalling (RGS)
protein, RGS7. RGS7 binds tightly to
Gbeta5, a unique and highly specialized
G protein that exhibits much less
homology than other Gbeta isoforms
(∼50%). RGS7 is preferentially
expressed in brain and neuroendocrine
tissue. Like Gbeta5, RGS7 is expressed
prominently in the cell membrane, as
well as in the cytosol. Although this
distribution pattern suggests that
complexes containing Gbeta5 and RGS7
may shuttle information between
classical G protein-signaling elements at
the plasma membrane and the cell
interior, the function of the complex in
the brain is largely unknown.
The antibodies were generated in
rabbits to a glutathione S-transferase
(GST) fusion protein with residues 312–
469 of bovine RGS7 (antibody 7RC–1)
and react with human and rodent RGS7.
The antibodies (7RC–1) can be used for
immunoblotting and
immunoprecipitation. They can be used
to facilitate our understanding of the
function of Gbeta5/RGS7 complexes in
brain and neurons.
Potential Commercial Applications:
These antibodies can be used for
research purposes (immunoblotting,
immunoprecipitation) by those studying
the biology and function of RGS7.
Competitive Advantages: High-titer,
multi-epitope antibodies to study RGS7
and RGS7/Gbeta5 complexes and G
protein signaling.
Development Stage: In vitro data
available.
Inventors: William Simonds and
Jianhua Zhang (NIDDK).
Publications
1. Rojkova AM, et al. Ggamma subunit
selective G protein beta 5 mutant defines
regulators of G protein signaling binding
requirement for nuclear localization. J Biol
Chem. 2003 Apr 4;278(14):12507–12. [PMID
12551930]
2. Cao Y, et al. Retina Specific GTPase
Accelerator RGS11/Gbeta5S/R9AP is a
Constitutive Heterotrimer Selectively
Targeted to mGluR6 in ON–Bipolar Neurons.
J Neurosci 2009 July 22; 29 (29): 9301–13.
[PMID 19625520]
3. Anderson GR, et al. Changes in striatal
signaling induce remodeling of RGS
complexes containing Gbeta5 and R7BP
subunits. Mol Cell Biol. 2009 Jun;29(11):
3033–44. [PMID 19332565]
4. Panicker LM, et al. Nuclear localization
of the G protein beta5/R7-regulator of G
protein signaling protein complex is
dependent on R7 binding protein. J
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Neurochem. 2010 Jun;113(5):1101–12. [PMID
20100282]
Intellectual Property: HHS Reference
No. E–077–2011/0—Research Tool.
Patent protection is not being pursued
for this technology.
Licensing Contact: Jaime Greene,
M.S.; 301–435–5559;
greenejaime@mail.nih.gov.
Dated: July 24, 2012.
Richard U. Rodriguez,
Director, Division of Technology Development
and Transfer, Office of Technology Transfer,
National Institutes of Health.
[FR Doc. 2012–18651 Filed 7–30–12; 8:45 am]
BILLING CODE 4140–01–P
Dated: July 25, 2012.
David Clary,
Program Analyst, Office of Federal Advisory
Committee Policy.
[FR Doc. 2012–18650 Filed 7–30–12; 8:45 am]
BILLING CODE 4140–01–P
DEPARTMENT OF HOMELAND
SECURITY
U.S. Customs and Border Protection
[Docket No. USCBP–2012–0027]
Advisory Committee on Commercial
Operations of Customs and Border
Protection (COAC)
U.S. Customs and Border
Protection, Department of Homeland
Security (DHS).
ACTION: Committee Management; Notice
of Federal Advisory Committee Meeting.
AGENCY:
DEPARTMENT OF HEALTH AND
HUMAN SERVICES
National Institutes of Health
Center for Scientific Review; Notice of
Closed Meeting
mstockstill on DSK4VPTVN1PROD with NOTICES
Pursuant to section 10(d) of the
Federal Advisory Committee Act, as
amended (5 U.S.C. App.), notice is
hereby given of the following meeting.
The meeting 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.
Name of Committee: Center for
Scientific Review Special Emphasis
Panel Member Conflict: Skeletal
Pathobiology and Orthopedics.
Date: August 28, 2012.
Time: 3:00 p.m. to 5:00 p.m.
Agenda: To review and evaluate grant
applications.
Place: National Institutes of Health,
6701 Rockledge Drive, Bethesda, MD
20892, (Telephone Conference Call).
Contact Person: Yi-Hsin Liu, Ph.D.,
Scientific Review Officer, Center for
Scientific Review, National Institutes of
Health, 6701 Rockledge Drive, Room
4214, MSC 7814, Bethesda, MD 20892,
301–435–1781, liuyh@csr.nih.gov.
(Catalogue of Federal Domestic Assistance
Program Nos. 93.306, Comparative Medicine;
93.333, Clinical Research, 93.306, 93.333,
93.337, 93.393–93.396, 93.837–93.844,
93.846–93.878, 93.892, 93.893, National
Institutes of Health, HHS)
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The Advisory Committee on
Commercial Operations of Customs and
Border Protection (COAC) will meet on
August 15, 2012, in Seattle, WA. The
meeting will be open to the public.
DATES: COAC will meet on Wednesday,
August 15, 2012 from 1:00 p.m. to 5:30
p.m. PST. Please note that the meeting
may close early if the committee has
completed its business.
Registration: If you plan on attending,
please register either online at https://
apps.cbp.gov/te_registration/
index.asp?w=80 or by email to
tradeevents@dhs.gov, or by fax to 202–
325–4290 by close-of-business on
August 12, 2012.
If you have completed an online onsite registration and wish to cancel your
registration, you may do so at https://
apps.cbp.gov/te_registration/
cancel.asp?w=80. Please feel free to
share this information with interested
members of your organizations or
associations.
SUMMARY:
The meeting will be held at
Jackson Federal Building, 915 2nd
Avenue, Seattle, WA 98174, in the
South Auditorium—4th Floor. All
visitors report to main lobby of the
building. All visitors to the Jackson
Federal Building must show a stateissued ID or Passport to proceed through
the security checkpoint to be admitted
to the building.
For information on facilities or
services for individuals with disabilities
or to request special assistance at the
meeting, contact Ms. Wanda Tate, Office
of Trade Relations, U.S. Customs and
Border Protection at 202–344–1661 as
soon as possible.
To facilitate public participation, we
are inviting public comment on the
ADDRESSES:
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issues to be considered by the
committee as listed in the ‘‘Agenda’’
section below.
Comments must be submitted in
writing no later than August 8, 2012,
and must be identified by USCBP–
2012–0027 and may be submitted by
one of the following methods:
• Federal eRulemaking Portal: https://
www.regulations.gov. Follow the
instructions for submitting comments.
• Email: Tradeevents@dhs.gov.
Include the docket number in the
subject line of the message.
• Fax: 202–325–4290
• Mail: Ms. Wanda Tate, Office of
Trade Relations, U.S. Customs and
Border Protection, 1300 Pennsylvania
Avenue NW., Room 3.5A, Washington,
DC 20229.
Instructions: All submissions received
must include the words ‘‘Department of
Homeland Security’’ and the docket
number for this action. Comments
received will be posted without
alteration at https://www.regulations.gov,
including any personal information
provided. Do not submit personal
information to this docket.
Docket: For access to the docket to
read background documents or
comments received by the COAC, go to
https://www.regulations.gov.
There will be two public comment
periods held during the meeting on
August 15, 2012. Speakers are requested
to limit their comments to two (2)
minutes or less to facilitate greater
participation. Contact the individual
listed below to register as a speaker.
Please note that the public comment
period for speakers may end before the
time indicated on the schedule that is
posted on the CBP web page at the time
of the meeting.
FOR FURTHER INFORMATION CONTACT: Ms.
Wanda Tate, Office of Trade Relations,
U.S. Customs and Border Protection,
1300 Pennsylvania Avenue NW., Room
3.5A, Washington, DC 20229; telephone
202–344–1440; facsimile 202–325–4290.
SUPPLEMENTARY INFORMATION: Notice of
this meeting is given under the Federal
Advisory Committee Act, 5 U.S.C. App.
(Pub. L. 92–463). The COAC provides
advice to the Secretary of Homeland
Security, the Secretary of the Treasury,
and the Commissioner of U.S. Customs
and Border Protection (CBP) on matters
pertaining to the commercial operations
of CBP and related functions within
DHS or the Department of the Treasury.
Agenda
The COAC will hear from the
following subcommittees on the topics
listed below and then will review,
deliberate, and formulate
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]]>Agencies
[Federal Register Volume 77, Number 147 (Tuesday, July 31, 2012)]
[Notices]
[Pages 45363-45366]
From the Federal Register Online via the Government Printing Office [www.gpo.gov]
[FR Doc No: 2012-18651]
-----------------------------------------------------------------------
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.
FOR FURTHER INFORMATION CONTACT: 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
[[Page 45364]]
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.
Glial Cell Line-Derived Neurotrophic Factor Opposite Strand (GDNFOS)
for Treatment of Neurodegenerative Diseases
Description of Technology: Glial cell line-derived neurotrophic
factor (GDNF) is a small human protein encoded by the GDNF gene. GDNF
has been effective therapy in laboratory animal models of Parkinson's
disease and protects several types of neurons in the brain and
peripheral nervous system. The NIDA inventors have discovered primate-
specific GDNFOS, encoded by the opposite strand of glial cell derived
neurotrophic factor (GDNF) gene. The GDNFOS gene encodes for novel
peptides that was found to be reduced in human middle temporal gyrus of
Alzheimer's disease brains. These secreted growth proteins have
potential neurotrophic activity and they might play a synergistic role
in neuroprotective effects of GDNF in human brain. The NIDA inventors
have also developed antibody against GDNFOS3 and generated compounds
that have potential pharmaceutical use. The compounds consist of GDNFOS
nucleic acid transcripts, GDNFOS protein or a functional fragment for
treatment of human neurodegenerative diseases.
Potential Commercial Applications
Synergistic role in neuroprotective effects of GDNF.
Alzheimer's disease, Parkinson's disease, Amyotrophic
lateral sclerosis, multiple sclerosis and diseases of peripheral organs
such as diabetes mellitus type 1.
Competitive Advantages
Secreted novel growth peptides.
An antibody against GDNFOS3 was developed.
Development Stage
Early-stage.
Pre-clinical.
In vitro data available.
Inventors: Qing-Rong Liu, Mikko Airavaara, Barry Hoffer, Brandon K
Harvey (all of NIDA).
Publication: Airavaara M, et al. Identification of novel GDNF
isoforms and cis-antisense GDNFOS gene and their regulation in human
middle temporal gyrus of Alzheimer disease. J Biol Chem. 2011 Dec
30;286(52):45093-102. [PMID 22081608]
Intellectual Property: HHS Reference No. E-044-2012/0--U.S.
Provisional Application No. 61/619, 296 filed 02 Apr 2012.
Licensing Contact: Betty B. Tong, Ph.D.; 301-594-6565;
tongb@mail.nih.gov.
Collaborative Research Opportunity: The National Institute on Drug
Abuse is seeking statements of capability or interest from parties
interested in collaborative research to further develop, evaluate or
commercialize GDNFOS peptide and non-coding RNAs as therapeutic agents
for neurodegenerative diseases. For collaboration opportunities, please
contact Vio Conley at conleyv@mail.nih.gov.
Increased Therapeutic Effectiveness of Immunotoxins That Use Toxin
Domains Lacking Human B-cell Epitopes
Description of Technology: Immunotoxins kill cancer cells while
allowing healthy, essential cells to survive. As a result, patients
receiving an immunotoxin are less likely to experience the deleterious
side-effects associated with non-discriminate therapies such as
chemotherapy or radiation therapy. Unfortunately, the continued
administration of immunotoxins often leads to a reduced patient
response due to the formation of neutralizing antibodies against
immunogenic epitopes contained within Pseudomonas exotoxin A (PE). To
improve the therapeutic effectiveness of PE-based immunotoxins through
multiple rounds of drug administration, NIH inventors have sought to
identify and remove the human B-cell epitopes within PE. Previous work
demonstrated that the removal of the murine B-cell and T-cell epitopes
from PE reduced the immunogenicity of PE and resulted in immunotoxins
with improved therapeutic activity. This technology involves the
identification and removal of major human B-cell epitopes on PE by
mutation or deletion. Considering these immunotoxins will be
administered to humans, the removal of human immunogenic epitopes is
important. The resulting PE-based immunotoxins have increased
resistance to the formation of neutralizing antibodies, and are
expected to have improved therapeutic efficacy.
Potential Commercial Applications
Essential component of immunotoxins.
Treatment of any disease associated with increased or
preferential expression a specific cell surface receptor.
Specific diseases include hematological cancers, lung
cancer, ovarian cancer, breast cancer, and head and neck cancers.
Competitive Advantages
PE variants now include the removal of human B-cell
epitopes, further reducing the formation of neutralizing antibodies
against immunotoxins which contain the PE variants.
Less immunogenic immunotoxins result in improved
therapeutic efficacy by permitting multiple rounds of administration in
humans.
Targeted therapy decreases non-specific killing of
healthy, essential cells, resulting in fewer non-specific side-effects
and healthier patients.
Development Stage: Pre-clinical.
Inventors: Ira H. Pastan et al. (NCI).
Publication: Liu W, et al. Recombinant immunotoxin engineered for
low immunogenicity and antigenicity by identifying and silencing human
B-cell epitopes. Proc Natl Acad Sci USA. 2012 Jul 17;109(29):11782-7.
[PMID 22753489]
Intellectual Property: HHS Reference No. E-263-2011/0--U.S.
Provisional Application No. 61/535,668 filed 16 Sep 2011.
Related Technologies
PCT Patent Publication WO 2011/032022 (HHS Reference No.
E-269-2009/0-PCT-02).
US Patent Publication US 20100215656 A1 (HHS Reference No.
E-292-2007/0-US-06).
US Patent Publication US 20090142341 A1 (HHS Reference No.
E-262-2005/0-US-06).
Multiple additional patent families.
Licensing Contact: David A. Lambertson, Ph.D.; 301-435-4632;
lambertsond@mail.nih.gov.
Collaborative Research Opportunity: The National Cancer Institute
is seeking statements of capability or interest from parties interested
in collaborative research to further develop, evaluate or commercialize
this technology. For collaboration opportunities, please contact John
Hewes, Ph.D. at hewesj@mail.nih.gov.
Novel Nitroxyl (HNO) Releasing Compounds and Their Use in Treating
Diseases
Description of Technology: Nitroxyl (HNO) is a chemical species
that exhibits distinct biological properties in comparison to its
oxidized product, nitric oxide (NO). Previous investigations have
revealed that the
[[Page 45365]]
distinct properties of HNO make it a tempting species for wide
therapeutic application as it has shown potential in the treatment of
heart failure, cancer, and other diseases in various animal and in
vitro models. Non-steroidal anti-inflammatory drugs (NSAIDs), such as
aspirin and ibuprofen, are compounds that inhibit cycloxygenase (COX)-
mediated conversion of arachidonic acids to prostagladins. NSAIDs are
known for their analgesic properties and are therapeutically involved
in many physiological functions, including the inhibition of chronic
pain and inflammation inhibition, prevention of heart disease, renal
function, and cancer. Prolonged use of NSAIDs can lead to serious
gastrointestinal and renal side effects, including ulcer perforation,
upper gastrointestinal bleeding, and death, which has limited NSAID
therapies.
The instant invention described HNO-releasing NSAIDs, which combine
the potential therapeutic benefits of HNO and NSAIDs without the
toxicities associated with chronic NSAID use. These HNO-releasing
NSAIDs provide a reliable controlled release of HNO making them
desirable HNO prodrugs. The instant invention disclosed various HNO-
releasing NSAIDs and methods of treating or preventing various
disorders with these compositions, such as cardiovascular disorders,
cancers, pain, inflammation, and alcoholism.
Potential Commercial Applications
Treatment of cancer.
Treatment of cardiovascular disease.
Aversion therapy for alcoholism.
Competitive Advantages
Combination of therapeutic benefits of HNO and NSAIDs.
Alleviated toxicity associated with chronic NSAID use.
Controlled release of HNO.
Development Stage
Early-stage.
Pre-clinical.
Inventors: David A. Wink and Larry K. Keefer (NCI).
Publication
Miranda KM, et al. Comparison of the NO and HNO donating
properties of diazeniumdiolates: primary amine adducts release HNO
in vivo. J Med Chem. 2005 Dec 29;48(26):8220-8. [PMID 16366603]
Intellectual Property: HHS Reference No. E-019-2010/2--
International Patent Application PCT/US2011/029072 filed 18 Mar 2011.
Licensing Contact: Betty B. Tong, Ph.D.; 301-594-6565;
tongb@mail.nih.gov.
Polyclonal Antibodies for the Specialized Signaling G Protein, Gbeta5
Description of Technology: Researchers at NIDDK have developed
polyclonal antibodies against the G protein, Gbeta5. Gbeta5 is a unique
and highly specialized G protein that exhibits much less homology than
other Gbeta isoforms (~50%) and is preferentially expressed in brain
and neuroendocrine tissue. It is expressed prominently in the neuronal
cell membrane, as well as in the cytosol and nucleus. Although this
distribution pattern suggests that Gbeta5 may shuttle information
between classical G protein-signaling elements at the plasma membrane
and the cell interior, its function in the brain is largely unknown.
The antibodies were separately generated in rabbits to KLH-
conjugates of peptides from the N-terminus of Gbeta5 (antibody ATDG)
and the C-terminus of Gbeta5 (antibody SGS). The antibodies can be used
for immunoblotting (ATDG, SGS), and immunoprecipitation (ATDG). They
can be used to facilitate our understanding of the unique biology and
function of Gbeta5 in brain and neurons.
Potential Commercial Applications: These antibodies can be used for
research purposes (immunoblotting, immunoprecipitation) by those
studying the biology and function of Gbeta5.
Competitive Advantages: Very specific antibodies to study Gbeta5
and G protein signaling.
Development Stage: In vitro data available.
Inventors: William Simonds and Jianhua Zhang (NIDDK).
Publications
1. Zhang JH and Simonds WF. Copurification of brain G-protein
beta5 with RGS6 and RGS7. J Neurosci. 2000 Feb 1;20(3):RC59. [PMID
10648734]
2. Zhang JH, et al. Nuclear localization of G protein beta 5 and
regulator of G protein signaling 7 in neurons and brain. J Biol
Chem. 2001 Mar 30;276(13):10284-9. [PMID 11152459]
3. Zhang S, et al. Selective activation of effector pathways by
brain-specific G protein beta5. J Biol Chem. 1996 Dec
27;271(52):33575-9. [PMID 8969224]
4. Zachariou V, et al. An essential role for DeltaFosB in the
nucleus accumbens in morphine action. Nat Neurosci. 2006
Feb;9(2):205-11. [PMID 16415864]
Intellectual Property: HHS Reference No. E-192-2006/0--Research
Tool. Patent protection is not being pursued for this technology.
Licensing Contact: Jaime Greene, M.S.; 301-435-5559;
greenejaime@mail.nih.gov.
Polyclonal Antibodies for the Gbeta5-Associated Regulator of G Protein
Signaling Protein, RGS7
Description of Technology: Researchers at NIDDK have developed
polyclonal antibodies against the Regulator of G Protein Signalling
(RGS) protein, RGS7. RGS7 binds tightly to Gbeta5, a unique and highly
specialized G protein that exhibits much less homology than other Gbeta
isoforms (~50%). RGS7 is preferentially expressed in brain and
neuroendocrine tissue. Like Gbeta5, RGS7 is expressed prominently in
the cell membrane, as well as in the cytosol. Although this
distribution pattern suggests that complexes containing Gbeta5 and RGS7
may shuttle information between classical G protein-signaling elements
at the plasma membrane and the cell interior, the function of the
complex in the brain is largely unknown.
The antibodies were generated in rabbits to a glutathione S-
transferase (GST) fusion protein with residues 312-469 of bovine RGS7
(antibody 7RC-1) and react with human and rodent RGS7. The antibodies
(7RC-1) can be used for immunoblotting and immunoprecipitation. They
can be used to facilitate our understanding of the function of Gbeta5/
RGS7 complexes in brain and neurons.
Potential Commercial Applications: These antibodies can be used for
research purposes (immunoblotting, immunoprecipitation) by those
studying the biology and function of RGS7.
Competitive Advantages: High-titer, multi-epitope antibodies to
study RGS7 and RGS7/Gbeta5 complexes and G protein signaling.
Development Stage: In vitro data available.
Inventors: William Simonds and Jianhua Zhang (NIDDK).
Publications
1. Rojkova AM, et al. Ggamma subunit selective G protein beta 5
mutant defines regulators of G protein signaling binding requirement
for nuclear localization. J Biol Chem. 2003 Apr 4;278(14):12507-12.
[PMID 12551930]
2. Cao Y, et al. Retina Specific GTPase Accelerator RGS11/
Gbeta5S/R9AP is a Constitutive Heterotrimer Selectively Targeted to
mGluR6 in ON-Bipolar Neurons. J Neurosci 2009 July 22; 29 (29):
9301-13. [PMID 19625520]
3. Anderson GR, et al. Changes in striatal signaling induce
remodeling of RGS complexes containing Gbeta5 and R7BP subunits. Mol
Cell Biol. 2009 Jun;29(11): 3033-44. [PMID 19332565]
4. Panicker LM, et al. Nuclear localization of the G protein
beta5/R7-regulator of G protein signaling protein complex is
dependent on R7 binding protein. J
[[Page 45366]]
Neurochem. 2010 Jun;113(5):1101-12. [PMID 20100282]
Intellectual Property: HHS Reference No. E-077-2011/0--Research
Tool. Patent protection is not being pursued for this technology.
Licensing Contact: Jaime Greene, M.S.; 301-435-5559;
greenejaime@mail.nih.gov.
Dated: July 24, 2012.
Richard U. Rodriguez,
Director, Division of Technology Development and Transfer, Office of
Technology Transfer, National Institutes of Health.
[FR Doc. 2012-18651 Filed 7-30-12; 8:45 am]
BILLING CODE 4140-01-P
