The present invention provides for the use of Tripterygium wilfordii Hook F extracts and purified components thereof in the treatment of inflammation or an immune disorder with concomitant lack of steroidal effect. Extracts of this plant (T2) bound to the glucocorticoid receptor and competitively inhibited glucocorticoid mediated cellular processes, such as dexamethasone binding to the glucocorticoid receptor, glucocorticoid mediated activation of target genes, dexamethasone dependent cellular growth, with concomitant inhibition of cyclooxygenase-2 induction and inflammatory processes such as the production of prostaglandin E.sub.2. The T2 extract components triptolide and tripdiolide were effective inhibitors. The particular advantage provided by the methods herein is the treatment or prevention of inflammation and the concomitant lack of steroidal agonist effects and NSAID side effects. Conditions treatable by the present methods include inflammation and immune disorders including autoimmune disease.
Non-steroidal anti-inflammatory drugs (NSAIDs) are widely-used anti-inflammatory and anti-pyretic therapeutic agents to treat human diseases. However, long-term use of NSAIDs comes with risks. Many NSAIDs are COX-1 inhibitors, which are associated with significant GI toxicities. The Marnett Lab at Vanderbilt University has developed new derivatives of NSAIDs that retain their protective effects but do not cause debilitating and potentially fatal toxicities.
An isolated nucleic acid encoding the Helicobacter pylori vacuolating toxin, consisting of the nucleotides 101 through 3964 of the nucleotide sequence defined in the Sequence Listing as SEQ ID NO:1 is provided. An isolated nucleic acid from Helicobacter pylori comprising the nucleotide sequence defined in the Sequence Listing as SEQ ID NO:3 is provided. Isolated nucleic acids that selectively hybridize with the nucleic acids of the invention are provided. Also provided is a genetically altered mutant strain of H. pylori that does not express a functional vacuolating toxin. Purified proteins encoded by the nucleic acids of the invention are provided. A composition comprising an immunogenic amount of a protein or mutant strain of the invention in a pharmaceutically acceptable carrier is provided. A method of immunizing a subject against infection by H. pylori, comprising administering to the subject an immunogenic composition of the invention is provided.
The invention provides the dapE gene of Helicobacter pylori and H. pylori dapE.sup.- mutants and to methods of using the mutants to express foreign genes and immunize against foreign agents. The dapE gene can consist of the nucleotide sequence defined in SEQ ID NO:3. Nucleic acids of the gidA gene and ORF 2 of H. pylori are provided. Examples of these nucleic acids can be found in SEQ ID NO:1 and SEQ ID NO:5, respectively. Having provided these nucleic acids, hybridizing nucleic acids in accord with the description of hybridizing nucleic acids of dapE are also provided.
Thrombosis is the formation of a blood clot inside a blood vessel, which may cause reduced blood flow to a tissue, or even tissue death. Thrombosis, inflammation, and infections are responsible for >70% of all human mortality. Thrombosis is also the major factor for heart disease and stroke. 500,000 die from thrombosis every year in Europe. Inhibitory treatment of these conditions may also improve the outcomes of several non-fatal diseases. Researchers from Vanderbilt University and Oregon Health & Science University have jointly discovered new monoclonal antibodies that potently inhibit the blood coagulation protein factor XII (FXII), a critical player in the pathway, and anticoagulate blood. This invention provides foundation for commercial development of anti-thrombotic drugs based on new molecular entities.
This technology enables the delivery of biological molecules into the interior of a cell. Such a delivery mechanism could be utilized in a variety of therapies including peptide, gene transfer and/or antisense therapy.
An isolated nucleic acid encoding the Helicobacter pylori recombinase comprising the nucleotide sequence defined in the Sequence Listing as SEQ ID NO:1 is provided. Also provided is an isolated nucleic acid that selectively hybridizes with the nucleic acid of claim 1 under stringent conditions and has at least 70% complementarity with the segment of the nucleic acid of SEQ ID NO:1 to which it hybridizes. Also provided is a mutant strain of H. pylori that does not express a functional recombinase (recA.sup.- mutant). An immunogenic amount of the recA.sup.- mutant H. pylori in a pharmaceutically acceptable carrier is provided. A method of immunizing a subject against infection by H. pylori comprises administering to the subject an immunogenic amount of mutant H. pylori in a carrier for the mutant.
The technology provides a method for diagnosis of MS by detection of Chlamydia and treatment of MS by total eradication of Chlamydia. This technology provides for eradication of Chlamydia by a novel treatment of combining various anti-chlamydial agents directed at different phases of the chlamydial life cycle.
Purified BMP-15-related proteins and processes for producing them are disclosed. DNA molecules encoding the BMP-15-related proteins are also disclosed. The proteins may be used in the treatment of bone and cartilage and/or other connective tissue defects and in wound healing and related tissue repair.
Scientists at Vanderbilt have developed a unique polypeptide using cell-penetrating SOCS polypeptides or SOCS sequences designed to inhibits cytokine signaling and thus prevent or treat inflammation or an inflammatory related disease such as diabetes. This strategy has been validated in NOD mice models for either induced or naturally occurring diabetes and have been efficacious.
A method of chemical ligation of peptides that requires no side chain protecting groups and no activation of the C-.alpha. carboxyl group is presented. The method consists of three steps. In the first step, initiation, a masked glycoaldehyde ester is enzymatically or chemically coupled to the C-terminal carboxylic acid of an sidechain unprotected first peptide. In the second step, ring formation, the masked aldehyde ester of the first peptide is unmasked, and then reacted with the N-.alpha. amino acid of a second sidechain unprotected peptide to form a ring structure. In the third step, rearrangement, the O-acyl ester linkage transfers at higher pH to an N-acyl linkage on the ring to form a peptide bond.