Warner-lambert Company

Qi-Zhuang Ye

Linda Lea Johnson

Donald John Hupe

Andrew David White

Joseph Armand Picard

Claude Forsey Purchase, Jr

Daniel Fred Ortwine

Vijaykumar M Baragi

A process for the production of the catalytic domain, without propeptide, of a matrix metalloproteinase is described which comprises culturing transformed host cells carrying a DNA sequence encoding the catalytic domain as well as a method for screening for inhibitors of a matrix metalloproteinase; a method for determining the 3-dimensional structure of the catalytic domain of a matrix metalloproteinase; and pharmaceutical compositions of human stromelysin catalytic domain protein which are useful in treating herniated vertebral discs, dermal ulcers, modifying scar tissue formation, and joint diseases.

Process for the production of stromelysin catalytic domain protein

Aromatic keto-acids and their derivatives as inhibitors of matrix

Tricyclic compounds are described as well as methods for the preparation and pharmaceutical compositions of same, which are useful as inhibitors of matrix metalloproteinases, particularly gelatinase A (72 kD gelatinase) and stromelysin-1 and for the treatment of multiple sclerosis, atherosclerotic plaque rupture, aortic aneurism, heart failure, restenosis, periodontal disease, corneal ulceration, cancer metastasis, tumor angiogenesis, arthritis, or other autoimmune or inflammatory disorders dependent upon tissue invasion by leukocytes.

Tricyclic inhibitors of matrix metalloproteinases

Tricyclic compounds are described as well as methods for the preparation and pharmaceutical compositions of same, which are useful as inhibitors of matrix metalloproteinases, particularly gelatinase A (72 kD gelatinase) and stromelysin-1 and for the treatment of multiple sclerosis, atherosclerotic plaque rupture, aortic aneurism, heart failure, restenosis, periodontal disease, corneal ulceration, cancer metastasis, tumor angionenesis, arthritis, or other autoimmune or inflammatory disorders dependent upon tissue invasion by leukocytes.

A process for the production of the catalytic domain, without propeptide, C-terminal domain, and the fibronectin-like insert, of human gelatinases is described which comprises culturing transformed E. coli host cells carrying a synthetic DNA sequence encoding the catalytic domain as well as a method for screening for inhibitors of a gelatinase; a method for determining the 3-dimensional structure of the catalytic domain of a gelatinase; and pharmaceutical compositions of human gelatinase catalytic domain protein which are useful in treating herniated vertebral discs, dermal ulcers, modifying scar tissue formation, and joint diseases.

Process for the production of gelatinase catalytic domain protein

A tricyclic compound is described as well as pharmaceutical compositions of same, which is useful as an inhibitor of matrix metalloproteinases, particularly gelatinase A (72 kD gelatinase) for the treatment of multiple sclerosis or other autoimmune or inflammatory disorders dependent upon tissue invasion by leukocytes.

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Ann Arbor, MI, United States of America

Qi-Zhuang Ye