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Amino‐terminally truncated desmin rescues fusion of des −/− myoblasts but negatively affects cardiomyogenesis and smooth muscle development
Author(s) -
Höllrigl Alexandra,
Puz Sonja,
Al-Dubai Haifa,
Kim Jai Up,
Capetanaki Yassemi,
Weitzer Georg
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02995-2
Subject(s) - desmin , myogenesis , myocyte , microbiology and biotechnology , intermediate filament , biology , vimentin , embryonic stem cell , chemistry , cell , cytoskeleton , biochemistry , gene , immunology , immunohistochemistry
Desmin fulfils important functions in maintenance of muscle cells and mutations in the desmin gene have been linked to a variety of myopathies. To ascertain the role of desmin's amino‐terminal domain in muscle cells we generated embryonic stem cells constitutively expressing desmin Δ1–48 in a null background and investigated muscle cell development in vitro. Desmin Δ1–48 lacking the first 48 amino acid residues promotes fusion of myoblasts, rescues myogenesis and down‐regulates vimentin expression in embryoid bodies, but hampers cardiomyogenesis and blocks smooth muscle development. These results demonstrate that desmin's amino‐terminus has different roles in skeletal, cardiac, and smooth muscle cell development and function.