PUBLICATION

Thrombospondin-4 controls matrix assembly during development and repair of myotendinous junctions

Authors
Subramanian, A., Schilling, T.F.
ID
ZDB-PUB-140620-9
Date
2014
Source
eLIFE   6(8): e02372 (Journal)
Registered Authors
Schilling, Tom, Subramanian, Arul
Keywords
Zebrafish, ECM organization, muscle attachment, myotendinous junctions, tendon development
MeSH Terms
  • Animals
  • Extracellular Matrix/metabolism*
  • Humans
  • Integrins/metabolism
  • Ligands
  • Microscopy, Electron, Transmission
  • Muscles/metabolism
  • Mutation
  • Protein Binding
  • Protein Conformation
  • Signal Transduction
  • Tendons/pathology*
  • Tendons/physiology*
  • Thrombospondins/physiology*
  • Zebrafish
PubMed
24941943 Full text @ Elife
Abstract
Tendons are extracellular matrix (ECM)-rich structures that mediate muscle attachments with the skeleton, but surprisingly little is known about molecular mechanisms of attachment. Individual myofibers and tenocytes in Drosophila interact through integrin (Itg) ligands such as Thrombospondin (Tsp), while vertebrate muscles attach to complex ECM fibrils embedded with tenocytes . We show for the first time that a vertebrate thrombospondin, Tsp4b, is essential for muscle attachment and ECM assembly at myotendinous junctions (MTJs). Tsp4b depletion in zebrafish causes muscle detachment upon contraction due to defects in laminin localization and reduced Itg signaling at MTJs. Mutation of its oligomerization domain renders Tsp4b unable to rescue these defects, demonstrating that pentamerization is required for ECM assembly. Furthermore, injected human TSP4 localizes to zebrafish MTJs and rescues muscle detachment and ECM assembly in Tsp4b-deficient embryos. Thus Tsp4 functions as an ECM scaffold at MTJs, with potential therapeutic uses in tendon strengthening and repair.
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