Committees; establishment, renewal, termination, etc.: owned; availability for licensing,

[Federal Register: December 7, 2000 (Volume 65, Number 236)]

[Notices]

[Page 76651-76652]

From the Federal Register Online via GPO Access [wais.access.gpo.gov]

[DOCID:fr07de00-70]

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.

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 filedon 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: shinnm@od.nih.gov

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 filed11 July, 2000, Licensing Contact: Marlene Shinn; 301/496-7056 ext. 285; email: ms482m@nih.gov

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 filed21 July 2000, Licensing Contact: Marlene Shinn; 301/496-7056 ext. 285; e-mail: shinnm@od.nih.gov

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 filed15 June 2000, Licensing Contact: Norbert Pontzer; 301/496-7735, ext. 284; e-mail: pontzern@od.nih.gov

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 (Kd= 1.3 0.1 nM, dissociation T1/2= 14 min.) and acts as purely competitive antagonist at the PTH1 receptor. This novel peptide is related to

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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. 00-31216Filed12-6-00; 8:45 am]

BILLING CODE 4140-01-P