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      How matrix metalloproteinases regulate cell behavior.

      1 ,
      Annual review of cell and developmental biology
      Annual Reviews

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          Abstract

          The matrix metalloproteinases (MMPs) constitute a multigene family of over 25 secreted and cell surface enzymes that process or degrade numerous pericellular substrates. Their targets include other proteinases, proteinase inhibitors, clotting factors, chemotactic molecules, latent growth factors, growth factor-binding proteins, cell surface receptors, cell-cell adhesion molecules, and virtually all structural extracellular matrix proteins. Thus MMPs are able to regulate many biologic processes and are closely regulated themselves. We review recent advances that help to explain how MMPs work, how they are controlled, and how they influence biologic behavior. These advances shed light on how the structure and function of the MMPs are related and on how their transcription, secretion, activation, inhibition, localization, and clearance are controlled. MMPs participate in numerous normal and abnormal processes, and there are new insights into the key substrates and mechanisms responsible for regulating some of these processes in vivo. Our knowledge in the field of MMP biology is rapidly expanding, yet we still do not fully understand how these enzymes regulate most processes of development, homeostasis, and disease.

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          Author and article information

          Journal
          Annu Rev Cell Dev Biol
          Annual review of cell and developmental biology
          Annual Reviews
          1081-0706
          1081-0706
          2001
          : 17
          Affiliations
          [1 ] Department of Anatomy, University of California, San Francisco, California 94143-0452, USA. sternli@itsa.ucsf.edu
          Article
          17/1/463 NIHMS160100
          10.1146/annurev.cellbio.17.1.463
          2792593
          11687497
          fffbae81-0058-4d4c-b1dd-d0205c0b1aec
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