[Federal Register Volume 65, Number 236 (Thursday, December 7, 2000)]
[Notices]
[Pages 76651-76652]
From the Federal Register Online via the Government Publishing Office [www.gpo.gov]
[FR Doc No: 00-31216]


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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 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.

Immunoglobulin-G Constant Region Fusion Proteins as Molecular 
Weight Markers

Stephen V. Angeloni, Ph.D. (NIDDK)
    DHHS Reference No. E-292-00/0, Licensing Contact: Marlene Shinn; 
301/496-7056 ext. 285; e-mail: <a href="/cdn-cgi/l/email-protection#dba8b3b2b5b5b69bb4bff5b5b2b3f5bcb4ad"><span class="__cf_email__" data-cfemail="fc8f9495929291bc9398d2929594d29b938a">[email protected]</span></a>

    The technology portrayed in this invention is available through a 
Biological Materials License as a research tool and for use in 
diagnostic tests. Current methods of protein detection and size 
determination can be made more efficient by the utilization of more 
stable protein markers that cover a wider range of molecular weights 
for western blotting and other diagnostics applications. As embodied in 
this invention, construction of recombinant proteins containing 
constant regions of Immunoglobulin-G from mouse, rabbit and other 
species, allow the production of protein standards that can be detected 
simultaneously on the same western blot as the sample proteins. Such 
markers will increase the accuracy in determining sample protein size 
and in combination with recombinant or chemically labeled second 
antibodies, will allow the detection of an increased number of sample 
proteins simultaneously on the same blot.

A Forward Mutational Assay for Use With PhiX174 Transgenic Mice

Carrie R. Valentine (FDA), Heinrich V. Malling (NIEHS), Bentley A. Fane 
(Univ. of Arizona)
    DHHS Reference No. E-254-00/0 filed 11 July, 2000, Licensing 
Contact: Marlene Shinn; 301/496-7056 ext. 285; email: <a href="/cdn-cgi/l/email-protection#1d706e29252f705d737475337a726b"><span class="__cf_email__" data-cfemail="3d504e09050f507d535455135a524b">[email protected]</span></a>
    The aforementioned invention is currently available through a 
Biological Materials License as a research tool. This assay can detect 
19 different base substitutions at 13 different sites in gene A of the 
PhiX174 transgene present in the transgenic Malling mouse and is an 
improvement over the previous reversion assay, which was limited to 
mutation at a single site. The ability to detect mutations at multiple 
sites will allow the detection of mutagenic test compounds with 
affinity for different sequence contexts, while retaining the advantage 
of the inexpensive recovery of this transgene, which is by 
electroporation.
    The evaluation of new drugs for their potential for inducing 
mutations is a necessary part of evaluating the safety of 
pharmaceuticals or environmental chemicals. One advantage of this assay 
is that it may be automated to be performed in microplate dishes. In 
addition, this assay has the potential to be utilized in a microarray 
system because of the limited number of possible mutations. Therefore, 
it would be more rapid and less expensive than the currently used 
transgenic systems.

Adult Human Dental Pulp Stem Cells in vitro and in vivo

Dr. Songtao Shi et al. (NIDCR)
    DHHS Reference No. E-233-00/0 filed 21 July 2000, Licensing 
Contact: Marlene Shinn; 301/496-7056 ext. 285; e-mail: 
<a href="/cdn-cgi/l/email-protection#e3908b8a8d8d8ea38c87cd8d8a8bcd848c95"><span class="__cf_email__" data-cfemail="bfccd7d6d1d1d2ffd0db91d1d6d791d8d0c9">[email protected]</span></a>

    Many individuals with ongoing and severe dental problems are faced 
with the prospect of permanent tooth loss. Examples include dentinal 
degradation due to caries or periodontal disease; (accidental) injury 
to the mouth; and surgical removal of teeth due to tumors associated 
with the jaw. Clearly, a technology that offers a possible alternative 
to artificial dentures by designing and transplanting a set of living 
teeth fashioned from the patient's own pulp cells would greatly improve 
the individual's quality of life.
    The NIH announces a new technology wherein dental pulp stem cells 
from an individual's own postnatal dental pulp tissue (one or two 
wisdom teeth) can potentially be used to engineer healthy living teeth. 
This technology is based upon the discovery of a subpopulation of cells 
within normal human dental pulp tissue that has the ability to grow and 
proliferate in vitro. These (dental pulp) stem cells can be induced 
under defined culture conditions to form calcified nodules in vitro and 
have been shown to differentiate into a dentin/pulp like structure in 
vivo.

PTH2 and PTH1 Receptor Ligands

Ted B. Usdin and Samuel R. Hoare (NIMH)
    DHHS Reference No. E-123-99/1 filed 15 June 2000, Licensing 
Contact: Norbert Pontzer; 301/496-7735, ext. 284; e-mail: 
<a href="/cdn-cgi/l/email-protection#e4948b8a909e81968aa48b80ca8a8d8cca838b92"><span class="__cf_email__" data-cfemail="f1819e9f858b94839fb19e95df9f9899df969e87">[email protected]</span></a>

    Parathyroid hormone receptors found on osteoblasts in bone and 
renal tubule cells in kidney elevate blood calcium levels when 
stimulated by parathyroid hormone (PTH) and PTH-related protein 
(PTHrP). Excessive secretion of PTH from the parathyroid gland results 
in primary hyperparathyroidism. Production of PTHrP by various tumors 
results in humoral hypercalcemia of malignancy. In both of these 
conditions, excessive blood calcium levels lead to clinically 
significant morbidity. A parathyroid hormone antagonist could therefore 
have therapeutic value.
    Until now, no effective antagonists for the classical parathyroid 
hormone receptor (PTH1 receptor) were known. This invention describes a 
peptide which binds with high affinity (K<INF>d</INF> = 1.3 
<plus-minus> 0.1 nM, dissociation T<INF>1/2</INF> = 14 min.) and acts 
as purely competitive antagonist at the PTH1 receptor. This novel 
peptide is related to

[[Page 76652]]

tuberoinfundibular peptides of 39 residues (TIP39), also described in 
this invention, which binds to a related receptor. Deletion of amino 
acids from the N-terminus of TIP39 resulted in the high affinity PTH1 
receptor antagonist peptide described here. This peptide may be used 
therapeutically to treat excessive blood calcium caused by PTH or 
PTHrP, other pathology caused by PTHrP, to demonstrate the utility of 
parathyroid hormone receptor antagonism in the treatment of 
hypercalcemia or other conditions, or to help screen for other 
antagonists at the parathyroid hormone receptor.

    Dated: November 29, 2000.
Jack Spiegel,
Director, Division of Technology Development and Transfer, Office of 
Technology Transfer, National Institutes of Health.
[FR Doc. 00-31216 Filed 12-6-00; 8:45 am]
BILLING CODE 4140-01-P


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