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Matrix metalloproteinase function in non-mammalian model organisms
Julia J Buckley, Jason R Jessen1
1Department of Biology, Middle Tennessee State University, Murfreesboro, TN 37130,, jason.jessen@mtsu.edu.
Abstract:
Matrix metalloproteinases (MMPs), adamalysins, astacins, and serralysins are members of the metzincin superfamily of proteases. MMPs constitute a large protein family of both secreted and membrane-tethered enzymes that are synthesized as zymogens (proMMP) and activated by a cysteine-switch mechanism. First described over 50 years ago by Gross and Lapiere as a collagenolytic activity in amphibian tissues, the human MMP family now encompasses 23 different genes whose encoded proteins are capable of cleaving a variety of extracellular matrix protein substrates. Since their expression is upregulated in many cancer cell types, MMPs have received much attention particularly in the areas of tumor progression and metastasis. However, in terms of normal developmental processes, much less is known regarding MMP function and substrate identity. Data from knockout mouse studies support the notion that MMPs are not essential regulators of embryonic development, suggesting redundancy between MMPs or the presence of subtle phenotypes. However, studies on MMP function in other model systems indicate a larger role for MMP-dependent proteolysis during embryonic processes. Here, we review the current knowledge of MMPs from diverse model systems ranging from flowering plants and invertebrates to non-mammalian vertebrates.
Insights
Matrix metalloproteinases (MMPs) are crucial proteases involved in cancer, but their roles in normal embryonic development are less understood. This review explores MMP functions across diverse model organisms, highlighting their broader developmental significance.
Area of Science:
- Biochemistry
- Molecular Biology
- Developmental Biology
Background:
- Matrix metalloproteinases (MMPs) are a large family of proteases within the metzincin superfamily.
- MMPs are synthesized as inactive zymogens (proMMP) and activated via a cysteine-switch mechanism.
- While implicated in cancer progression and metastasis, MMP roles in normal development are less clear.
Purpose of the Study:
- To review the current understanding of Matrix metalloproteinase (MMP) functions.
- To explore MMP substrate identities and roles in normal developmental processes.
- To consolidate knowledge of MMPs across diverse model systems.
Main Methods:
- Literature review of studies on Matrix metalloproteinases (MMPs).
- Analysis of data from knockout mouse studies.
- Examination of MMP function in various model systems including plants, invertebrates, and non-mammalian vertebrates.
Main Results:
- Mouse knockout studies suggest MMPs may not be essential for embryonic development.
- Evidence from other model systems indicates a significant role for MMP-dependent proteolysis in embryonic processes.
- MMP expression is upregulated in many cancer cell types, linking them to tumor progression.
Conclusions:
- Matrix metalloproteinases (MMPs) play a more substantial role in embryonic development than previously suggested by mammalian studies.
- Further research across diverse model systems is needed to fully elucidate MMP functions and substrate specificities in development.
- Understanding MMPs in normal development may offer insights into their dysregulation in diseases like cancer.
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