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doi: 10.1242/10.1242/dev.00394
1 Department of Animal Biology and Centre for Environmental Biology, Faculty of
Sciences, University of Lisbon, 1749-016 Lisbon, Portugal
2 Gulbenkian Institute of Science, Oeiras, Portugal
3 Hubrecht Laboratory, Netherlands Institute for Developmental Biology, Utrecht,
The Netherlands
4 Department of Cell Biology, Netherlands Cancer Institute, Amsterdam, The
Netherlands
5 Institute of Molecular Embryology and Genetics, Kumamoto University School of
Medicine, Kumamoto, Japan
Present address: Faculty of Medicine, INSERM U385, Nice, France
Author for correspondence (e-mail:
solveig{at}fc.ul.pt)
Accepted 9 January 2003
Integrins are extracellular matrix receptors composed of 
and ß subunits involved in cell adhesion, migration and signal
transduction. The ß1 subunit has two isoforms, ß1A
ubiquitously expressed and ß1D restricted to striated muscle. They
are not functionally equivalent. Replacement of ß1A by
ß1D (ß1D knock-in) in the mouse leads to midgestation
lethality on a 50% Ola/50% FVB background [Baudoin, C., Goumans, M. J.,
Mummery, C. and Sonnenberg, A.
(1998). Genes Dev.
12, 1202-1216]. We crossed the ß1D knock-in line into a less
penetrant genetic background. This led to an attenuation of the midgestation
lethality and revealed a second period of lethality around birth. Midgestation
death was apparently not caused by failure in cell migration, but rather by
abnormal placentation. The ß1D knock-in embryos that survived
midgestation developed until birth, but exhibited severely reduced skeletal
muscle mass. Quantification of myotube numbers showed that substitution of
ß1A with ß1D impairs primary myogenesis with no direct
effect on secondary myogenesis. Furthermore, long-term primary myotube
survival was affected in ß1D knock-in embryos. Finally,
overexpression of ß1D in C2C12 cells impaired myotube formation
while overexpression of ß1A primarily affected myotube maturation.
Together these results demonstrate for the first time distinct roles for
ß1 integrins in primary versus secondary myogenesis and that the
ß1A and ß1D variants are not functionally equivalent in
this process.
Key words: ß1 integrins, Knock-in, Myogenesis, Muscle mass, Cell migration, Placentation, Mouse
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