Published online 24 July 2006. doi:10.1083/jcb.200601102
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 174, Number 3, 403-413
Mannose receptor regulates myoblast motility and muscle growth
Katie M. Jansen1,2 and
Grace K. Pavlath1
1 Department of Pharmacology and 2 Program in Biochemistry, Cell, and Developmental Biology, Emory University, Atlanta, GA 30322
Correspondence to Grace K. Pavlath: gpavlat{at}emory.edu
Myoblast fusion is critical for the formation, growth, and maintenance of skeletal muscle. The initial formation of nascent myotubes requires myoblastmyoblast fusion, but further growth involves myoblastmyotube fusion. We demonstrate that the mannose receptor (MR), a type I transmembrane protein, is required for myoblastmyotube fusion. Mannose receptor (MR)null myotubes were small in size and contained a decreased myonuclear number both in vitro and in vivo. We hypothesized that this defect may arise from a possible role of MR in cell migration. Time-lapse microscopy revealed that MR-null myoblasts migrated with decreased velocity during myotube growth and were unable to migrate in a directed manner up a chemoattractant gradient. Furthermore, collagen uptake was impaired in MR-null myoblasts, suggesting a role in extracellular matrix remodeling during cell motility. These data identify a novel function for MR during skeletal muscle growth and suggest that myoblast motility may be a key aspect of regulating myotube growth.
Abbreviations used in this paper: DM, differentiation media; eMyHC, embryonic myosin heavy chain; GM, growth media; H&E, hematoxylin and eosin; IL-4, interleukin-4; MR, mannose receptor; RV, retrovirus; TA, tibialis anterior; WT, wild-type; XSA, cross-sectional area.

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