| First Author | Miyagoe-Suzuki Y | Year | 2009 |
| Journal | Mech Dev | Volume | 126 |
| Issue | 3-4 | Pages | 107-16 |
| PubMed ID | 19114101 | Mgi Jnum | J:144928 |
| Mgi Id | MGI:3832579 | Doi | 10.1016/j.mod.2008.12.001 |
| Citation | Miyagoe-Suzuki Y, et al. (2009) Reduced proliferative activity of primary POMGnT1-null myoblasts in vitro. Mech Dev 126(3-4):107-16 |
| abstractText | Protein O-linked mannose beta1,2-N-acetylglucosaminyltransferase 1 (POMGnT1) is an enzyme that transfers N-acetylglucosamine to O-mannose of glycoproteins. Mutations of the POMGnT1 gene cause muscle-eye-brain (MEB) disease. To obtain a better understanding of the pathogenesis of MEB disease, we mutated the POMGnT1 gene in mice using a targeting technique. The mutant muscle showed aberrant glycosylation of alpha-DG, and alpha-DG from mutant muscle failed to bind laminin in a binding assay. POMGnT1(-/-) muscle showed minimal pathological changes with very low-serum creatine kinase levels, and had normally formed muscle basal lamina, but showed reduced muscle mass, reduced numbers of muscle fibers, and impaired muscle regeneration. Importantly, POMGnT1(-/-) satellite cells proliferated slowly, but efficiently differentiated into multinuclear myotubes in vitro. Transfer of a retrovirus vector-mediated POMGnT1 gene into POMGnT1(-/-) myoblasts completely restored the glycosylation of alpha-DG, but proliferation of the cells was not improved. Our results suggest that proper glycosylation of alpha-DG is important for maintenance of the proliferative activity of satellite cells in vivo. |
