Report in Science on x-ray crystal structure of matrix Metalloproteinase-2 (MMP-2)

MMP-2 is a key target for anti-cancer drug development

Research Triangle Park, N.C.--June 4, 1999-- BioStratum Incorporated announced today the publication of a paper in the journal SCIENCE (volume 284, pages 1667-1670) reporting the three-dimensional structure of the matrix metalloproteinase-2 (MMP-2), a key molecular target for a number of anti-cancer drug candidates currently in clinical development. This work was completed by one of BioStratum's founding scientists, Dr. Karl Tryggvason of the Karolinska Institute, Stockholm, Sweden.

The elucidated structure of MMP-2 provides valuable information on the function and regulation of this important enzyme, and provides for the design of improved MMP-2 specific inhibitors for clinical evaluation. BioStratum owns intellectual property rights to this technology and to new and improved MMP-2 inhibitors that may be identified.

Matrix metalloproteinases (MMPs) are involved in tissue growth and wound repair. MMPs work by degrading substances in the extracellular matrix (the area outside of cells) thereby enabling the movement and expansion of cells, the deposition of new extracellular matrix, and the subsequent development of new tissue. MMP-2 acts directly on type IV collagen, a principal component of the basal lamina, a specialized form of the extracellular matrix. The activation of MMPs has been implicated in the invasive growth and spread of tumors. Several clinical studies are in progress evaluating the effectiveness of MMP inhibitors as anti-cancer agents, and many more are projected to enter clinical trials in the near future.

The elucidated molecular structure is the culmination of seven years of effort in Dr. Tryggvason?s laboratory. "This advance is providing important insights into the catalytic and regulatory mechanisms of this enzyme. It also provides an additional tool to aid in the design of improved MMP inhibitors to combat the spread of cancer," said Dr. Tryggvason.<

Contact: J. Wesley Fox, Ph.D.
Noonan/Russo Communications

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