bay-12-9566 has been researched along with Osteoarthritis* in 3 studies
1 review(s) available for bay-12-9566 and Osteoarthritis
Article | Year |
---|---|
Clinical trials of a stromelysin inhibitor. Osteoarthritis, matrix metalloproteinase inhibition, cartilage loss, surrogate markers, and clinical implications.
Long-term trials with BAY 12-9566, a stromelysin inhibitor, have been initiated in osteoarthritis. Validation of the long-term, clinical relevance of early markers has to be tested in these and other trials. Detection of the slowing of cartilage loss (as gauged by measures of joint space narrowing and by other techniques, such as MRI) remains to be proven, but now may be possible in intervention trials. Topics: Animals; Antineoplastic Agents; Biomarkers; Biphenyl Compounds; Cartilage; Clinical Trials as Topic; Extracellular Matrix; Humans; Matrix Metalloproteinase Inhibitors; Organic Chemicals; Osteoarthritis; Phenylbutyrates; Protease Inhibitors | 1999 |
1 trial(s) available for bay-12-9566 and Osteoarthritis
Article | Year |
---|---|
Pharmacokinetics, safety, and tolerability of BAY 12-9566 and nonsteroidal anti-inflammatory agents (naproxen, ibuprofen) during coadministration in patients with osteoarthritis.
The pharmacokinetic interactions between BAY 12-9566 and two nonsteroidal anti-inflammatory drugs (NSAIDs), naproxen and ibuprofen, were investigated in osteoarthritis (OA) patients. The study comprised six groups: two NSAID groups with three levels of treatment (BAY 12-9566 400 mg, BAY 12-9566 100 mg, and placebo). Plasma pharmacokinetic parameters (AUC(0-tau), Cmax, and tmax) were determined for each treatment group following 5 days of NSAID administration, 14 days of BAY 12-9566 administration, and 14 days of concurrent NSAID and BAY 12-9566 administration. For most conditions, the total plasma drug concentrations of both NSAID and BAY 12-9566 were diminished by coadministration; total plasma BAY 12-9566 was not affected by ibuprofen treatment. Importantly, the free drug concentrations were largely unaffected by coadministration. Most side effects were mild or moderate in intensity, and all events, with the exception of headache, were reported in both NSAID groups and in both placebo and BAY 12-9566 groups. Topics: Adult; Aged; Anti-Inflammatory Agents, Non-Steroidal; Antineoplastic Agents; Area Under Curve; Biphenyl Compounds; Chromatography, High Pressure Liquid; Double-Blind Method; Drug Interactions; Drug Therapy, Combination; Female; Humans; Ibuprofen; Male; Metalloendopeptidases; Middle Aged; Naproxen; Organic Chemicals; Osteoarthritis; Phenylbutyrates | 2001 |
1 other study(ies) available for bay-12-9566 and Osteoarthritis
Article | Year |
---|---|
Use of an antineoepitope antibody for identification of type-II collagen degradation in equine articular cartilage.
To develop an antibody that specifically recognizes collagenase-cleaved type-II collagen in equine articular cartilage.. Cartilage specimens from horses euthanatized for problems unrelated to the musculoskeletal system.. A peptide was synthesized representing the carboxy- (C-) terminus (neoepitope) of the equine type-II collagen fragment created by mammalian collagenases. This peptide was used to produce a polyclonal antibody, characterized by western analysis for reactivity to native and collagenase-cleaved equine collagens. The antibody was evaluated as an antineoepitope antibody by ELISA, using peptides +/- an amino acid at the C-terminus of the immunizing peptide. Collagen cleavage was assayed from equine articular cartilage cultured with interleukin-1 (IL-1), +/- a synthetic MMP inhibitor, BAY 12-9566. Cartilage specimens from osteoarthritic and nonarthritic joints were compared for antibody staining.. An antibody, 234CEQ, recognized only collagenase-generated 3/4-length fragments of equine type-II collagen. This was a true antineoepitope antibody, as altering the C-terminus of the immunizing peptide significantly decreased competition for binding in an inhibition ELISA. The IL-1-induced release of type-II collagen fragments from articular cartilage was prevented with the MMP inhibitor. Cartilage from an osteoarthritic joint of a horse had increased staining with the 234CEQ antibody, compared with normal articular cartilage.. We generated an antineoepitope antibody recognizing collagenase-cleaved type-II collagen of horses. This antibody detects increases in type-II collagen cleavage in diseased equine articular cartilage. The 234CEQ antibody has the potential to aid in the early diagnosis of arthritis and to monitor treatment responses. Topics: Animals; Antibodies; Antineoplastic Agents; Biphenyl Compounds; Blotting, Western; Cartilage, Articular; Collagen Type II; Collagenases; Enzyme-Linked Immunosorbent Assay; Epitopes; Female; Horse Diseases; Horses; Immunohistochemistry; Matrix Metalloproteinase 3; Organic Chemicals; Osteoarthritis; Peptide Fragments; Phenylbutyrates; Proteoglycans; Rabbits | 2001 |