The extracellular matrix protein TGFBI promotes myofibril bundling and muscle fibre growth in the zebrafish embryo.

The extracellular matrix protein Tgfbi has been shown to localise to myotendinous junctions in mouse and postulated to interact with the transmembrane protein Integrin alpha7beta1, which, in parallel with the Dystrophin-associated protein complex, is critical for linkage between the extracellular matrix and the cytoskeleton of muscle fibres. Here we use a GFP-tagged form of Tgfbi to analyse its distribution in the developing skeletal muscle of the zebrafish embryos and antisense morpholino oligonucleotides to investigate the function of the endogenous protein. We find that although tagged Tgfbi accumulates at the myosepta, the attachment of muscle fibres to the myosepta is established and maintained normally in morphant embryos; however, the fibres show a marked reduction in their growth and a disruption of their myofibril bundles. Copyright (c) 2008 Wiley-Liss, Inc.