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Editor’s Note: Our regular columnist Mindy Goldstein, PhD, welcomes the following “Tech Edge” contribution from colleague Sanford Simon, PhD.
From the column editor: The number of matrix metalloproteinases and serine proteinases that have been identified has continued to grow and become ever more complex. These enzymes play both a positive role, by remodeling collagen in normal skin and during wound repair, as well as a negative role, by participating in and enhancing inflammation. This month, I welcome Dr. Sanford Simon from The State University of New York at Stony Brook to explain the complexity of these enzymes and the roles they play in the body. Simon received his doctorate from Rockefeller University in biochemistry and has been on the faculty of the School of Medicine at the State University of New York since 1969. His research interests have been in the areas of protein and enzyme biochemistry and the cell biology of inflammation. He currently is a professor of biochemistry and pathology at Stony Brook, where he and his collaborators at the university and in the private sector are actively investigating the uses of natural and synthetic proteinase inhibitors to reduce inflammatory tissue damage triggered by environmental agents such as cigarette smoke, focal infections such as acne and anthrax, and the invasive and angiogenic phenotype displayed by tumors.
–Mindy Goldstein, PhD
Matrix metalloproteinases (MMPs), along with the serine proteinases, constitute the two major classes of secreted extracellular proteolytic enzymes; other families of proteinases, such as aspartyl, cysteinyl and threonyl proteinases, can be localized to the cytosol of cells or to specialized intracellular structures such as the proteasome. This article describes the mechanisms by which the activity of these proteinases is controlled, and suggests a modest goal for their safe and effective use in therapies for inflammatory injury to the skin.
Types: MMPs are a class of proteolytic enzymes with a broad range of architectures and functions; indeed, this family is growing—there are more than two dozen distinct MMPs—and provoking active debate over the significance of the impressive multiplicity of member enzymes. Some of the identified MMPs preferentially degrade structural proteins of the extracellular matrix, especially the native triple helical structure of the fibrillar types of collagen (e.g., types I and III collagen found in the dermal stroma). Other so-called gelatinolytic MMPs further degrade the products generated by the initial cleavages of the collagenolytic MMPs as well as the type IV collagen-containing basement membrane at the dermal-epidermal junction.