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Home > Art, Film & Photography > EC 3.4.24: Matrix Metalloproteinase
EC 3.4.24: Matrix Metalloproteinase

EC 3.4.24: Matrix Metalloproteinase


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Purchase includes free access to book updates online and a free trial membership in the publisher's book club where you can select from more than a million books without charge. Excerpt: Matrix metalloproteinases (MMPs) are zinc-dependent endopeptidases; other family members are adamalysins, serralysins, and astacins. The MMPs belong to a larger family of proteases known as the metzincin superfamily. Collectively they are capable of degrading all kinds of extracellular matrix proteins, but also can process a number of bioactive molecules. They are known to be involved in the cleavage of cell surface receptors, the release of apoptotic ligands (such as the FAS ligand), and chemokine/cytokine in/activation. MMPs are also thought to play a major role on cell behaviors such as cell proliferation, migration (adhesion/dispersion), differentiation, angiogenesis, apoptosis and host defense. They were first described in vertebrates (1962), including Homo sapiens, but have since been found in invertebrates and plants. They are distinguished from other endopeptidases by their dependence on metal ions as cofactors, their ability to degrade extracellular matrix, and their specific evolutionary DNA sequence. Initially, MMPs were described by Jerome Gross and Charles Lapiere (1962) who observed enzymatic activity (collagen triple helix degradation) during tadpole tail metamorphosis (by placing a tadpole tail in a collagen matrix plate). Therefore, the enzyme was named interstitial collagenase (MMP-1). Later it was purified from human skin (1968), and was recognized to be synthesized as a zymogen. The "cysteine switch" was described in 1990. The MMPs share a common domain structure. The three common domains are the pro-peptide, the catalytic domain and the haemopexin-like iterminal domain which is linked to the catalytic domain by a flexible hinge region. The MMPs are initially synthesized as inactive zymogens with a pro-peptide domain that... More: http://booksllc.net/?id=507329


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Product Details
  • ISBN-13: 9781156258224
  • Publisher: Books LLC
  • Publisher Imprint: Books LLC
  • Height: 152 mm
  • Sub Title: Matrix Metalloproteinase
  • Width: 229 mm
  • ISBN-10: 1156258227
  • Publisher Date: 31 May 2010
  • Binding: Paperback
  • Spine Width: 3 mm
  • Weight: 82 gr


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