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Related Experiment Videos

How matrix metalloproteinases regulate cell behavior.

M D Sternlicht1, Z Werb

  • 1Department of Anatomy, University of California, San Francisco, California 94143-0452, USA. sternli@itsa.ucsf.edu

Annual Review of Cell and Developmental Biology
|November 1, 2001
PubMed
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Matrix metalloproteinases (MMPs) are enzymes that break down proteins, regulating many biological processes. Recent research clarifies their function, control, and role in health and disease.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Matrix metalloproteinases (MMPs) are a large family of enzymes involved in extracellular matrix degradation.
  • These enzymes process a wide array of substrates, influencing numerous biological functions.
  • MMPs play critical roles in both normal physiological processes and various disease states.

Purpose of the Study:

  • To review recent advances in understanding MMP structure, function, and regulation.
  • To elucidate the mechanisms by which MMPs control biological processes.
  • To highlight new insights into MMP substrates and their roles in vivo.

Main Methods:

  • Literature review of recent advances in MMP research.
  • Analysis of MMP structure-function relationships.

Related Experiment Videos

  • Examination of MMP regulation at transcriptional, translational, and post-translational levels.

    • Main Results:

    • MMPs' diverse substrate targets include proteinases, growth factors, receptors, and extracellular matrix components.
    • Advances illuminate MMP control mechanisms: transcription, secretion, activation, inhibition, localization, and clearance.
    • New insights identify key substrates and regulatory mechanisms in vivo.

    Conclusions:

    • MMP activity is tightly regulated, impacting numerous biological processes.
    • Understanding MMPs is crucial for comprehending development, homeostasis, and disease.
    • Despite rapid expansion of knowledge, full comprehension of MMP roles remains an ongoing challenge.