National Institutes of Health, Public Health Service, DHHS.
The invention listed below is owned by an agency of the U.S. Government and is 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.
Licensing information and copies of the U.S. patent application 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 application.
Isolation of Hybridomas Producing Monoclonal Antibodies (MAbs) Inhibitory to Human CYP2J2
Dr. Darryl Zeldin (NIEHS), Dr. Harry Gelboin (NCI), et al.
DHHS Reference No. E-337-2003/0—Research Tool.
Licensing Contact: Marlene Shinn-Astor; 301/435-4426; email@example.com.
Cytochromes P450 catalyze the NADPH-dependent oxidation of arachidonic acid to various eicosanoids found in several species. The eicosanoids are biosynthesized in numerous tissues including pancreas, intestine, kidney, heart, and lung where they are involved in many different biological activities.
The NIH announces three specific monoclonal antibodies that strongly inhibit and/or immunoblot the human cytochrome P450 2J2 (CYP2J2). MAb 6-5-20-8 selectively inhibits CYP2J2-mediated arachidonic acid metabolism by more than 80% and also immunoblots the enzyme. MAb 6-2-16-1 also selectively inhibits arachidonic acid metabolism by more than 80%, but does not immunoblot the enzyme. MAb 5-3-2-2 is not inhibitory, but selectively immunoblots the enzyme. These antibodies can be used to identify and quantify inter-individual variation in physiological functions and to study pharmacological drug metabolism in various tissues.
This research is also described in: Sun et al., Circ. Res. 90: 1020-1027, 2002; King et al., Mol. Pharmacol. 61: 840-852, 2002; Yang et al., Mol. Pharmacol. 60: 310-320, 2001; Zeldin, J. Biol. Chem. 276: 36059-36062, 2001; Node et al., J. Biol. Chem. 276: 15983-15989, 2001; Node et al., Science 285: 1276-1279, 1999; Wu et al., J. Biol. Chem. 271: 3460-3468.
TNF-α Converting Enzyme Inhibitory Agents and Stimulatory Agents
Dr. Stewart Levine et al. (NHLBI).
U.S. Provisional Patent Application filed 24 Sep 2003 (DHHS Reference No. E-208-2003/0-US-01).
Licensing Contact: Marlene Shinn-Astor; 301/435-4426; firstname.lastname@example.org.Start Printed Page 63113
The action of Tumor Necrosis Factor alpha (TNF-α) has been implicated in such diseases as arthritis, sepsis, ulcerative colitis, multiple sclerosis, Crohn's disease, septic shock, graft rejection, cachexia, insulin resistance, post-ischemic reperfusion injury, tumor metastasis, tissue ulceration, abnormal wound healing, periodontal disease, bone disease, proteinuria, aneurismal aortic disease, degenerative cartilage loss, demyelinating diseases of the nervous system, and HIV infection. TNF-α converting enzyme (TACE) or ADAM 17 (A Disintegrin And Metalloprotease) is a member of a family of zinc metalloproteases, and is an important regulator of inflammation, immune regulation, and cellular proliferation as a consequence of its ability to catalyze the activation of TNF-α from a membrane bound to a soluble form.
The NIH announces the identification of a protein, corresponding to the amino-terminus of the TACE prodomain, that possesses a TACE inhibitory activity that is independent of a cysteine-switch mechanism. This TACE inhibitory protein could be used as a new therapeutic agent against chronic inflammatory diseases that are mediated by TNF-α.
Use of Smad3 Inhibitor in the Treatment of Fibrosis Dependent on Epithelial to Mesenchymal Transition as in the Eye and Kidney
Anita Roberts (NCI).
U.S. Provisional Patent Application No. 60/441,297 filed 17 Jan 2003 (DHHS Reference No. E-062-2003/0-US-01).
Licensing Contact: Marlene Shinn-Astor; 301/435-4426; email@example.com.
Fibroid scar tissue has been associated with wound healing of the epithelial layer following tissue damage created by surgery or other means. Examples of which include the opaque scar tissue associated with cataract surgery and the fibroid scar tissue produced in several kidney diseases such as is seen in unilateral ureteral obstruction.
Smad2 and Smad3 are highly homologous cytoplasmic proteins which function to mediate signals from Transforming Growth Factor Beta (TGF-β) and activin receptors to promoters of target genes found in the nucleus. The NIH announces a technology wherein Smad 3 is now implicated in TGF-β-dependent transdifferentiation of epithelial cells to mesenchymal cells (EMT), which blocks the endpoint of fibrosis at an early stage of differentiation of epithelial cell precursors into interstitial fibroblasts. In particular, fibrosis was blocked following wounding of the lens of the eye and damage created to the kidney. It is believed that an inhibitor of Smad 3 could be used to block fibrosis following cataract surgery and lens implantation in patients, as well as slowing the progression of end-stage renal disease.Start Signature
Dated: October 28, 2003.
Steven M. Ferguson,
Director, Division of Technology Development and Transfer, Office of Technology Transfer, National Institutes of Health.
[FR Doc. 03-28055 Filed 11-6-03; 8:45 am]
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