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Literature summary for 3.4.24.B3 extracted from

  • Jenkins, M.H.; Alrowaished, S.S.; Goody, M.F.; Crawford, B.D.; Henry, C.A.
    Laminin and matrix metalloproteinase 11 regulate fibronectin levels in the zebrafish myotendinous junction (2016), Skeletal Muscle, 6, 18 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
stable recombinant overexpresison of GFP-tagged enzyme in zebrafish Danio rerio

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
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Danio rerio
-
-
extracellular matrix
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Danio rerio 31012
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ a zinc-dependent endopeptidase Danio rerio

Organism

Organism UniProt Comment Textmining
Danio rerio
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
embryo
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Danio rerio
-
skeletal muscle localization to the myotendinous junction (MTJ), laminin is necessary to recruit/retain Mmp11 at the MTJ. Mmp11 is strongly expressed at the MTJ in zebrafish at 2 days post fertilization. Mmp11 expression throughout primary muscle development Danio rerio
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Synonyms

Synonyms Comment Organism
matrix metalloproteinase 11
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Danio rerio
MMP11
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Danio rerio
stromelysin-3
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Danio rerio

General Information

General Information Comment Organism
physiological function the enzyme is involved in skeletal muscle development in zebrafish, morphogenesis of the myotendinous junction (MTJ), overview. Mmp11 localization to the MTJ is regulated by laminin. Laminin polymerization indirectly promotes fibronectin (Fn) downregulation at the MTJ, via a matrix metalloproteinase 11 (Mmp11)-dependent mechanism. Laminin deposition and organization is required for localization of Mmp11 to the MTJ, where Mmp11 is both necessary and sufficient for Fn downregulation in vivo. Furthermore, reduction of residual Mmp11 in laminin mutants promotes a Fn-rich MTJ that partially rescues skeletal muscle architecture. Mmp11 is necessary and sufficient for fibronectin downregulation Danio rerio