Transition from Non-Muscle to Muscle Myosin Light Chains in Chick Embryo Development

Pathobiology ◽  
1987 ◽  
Vol 55 (5) ◽  
pp. 271-275
Author(s):  
U. Fascio ◽  
F. De Bernardi
BIOPHYSICS ◽  
2012 ◽  
Vol 57 (2) ◽  
pp. 201-214
Author(s):  
Z. A. Podlubnaya ◽  
Ya. N. Khalina ◽  
D. A. Bledjyanz

1985 ◽  
Vol 100 (6) ◽  
pp. 2025-2030 ◽  
Author(s):  
H Takano-Ohmuro ◽  
T Obinata ◽  
M Kawashima ◽  
T Masaki ◽  
T Tanaka

It has been demonstrated that embryonic chicken gizzard smooth muscle contains a unique embryonic myosin light chain of 23,000 mol wt, called L23 (Katoh, N., and S. Kubo, 1978, Biochem. Biophys. Acta, 535:401-411; Takano-Ohmuro, H., T. Obinata, T. Mikawa, and T. Masaki, 1983, J. Biochem. (Tokyo), 93:903-908). When we examined myosins in developing chicken ventricular and pectoralis muscles by two-dimensional gel electrophoresis, the myosin light chain (Le) that completely comigrates with L23 was detected in both striated muscles at early developmental stages. Two monoclonal antibodies, MT-53f and MT-185d, were applied to characterize the embryonic light chain Le of striated muscles. Both monoclonal antibodies were raised to fast skeletal muscle myosin light chains; the former antibody is specific to fast muscle myosin light chains 1 and 3, whereas the latter recognizes not only fast muscle myosin light chains but also the embryonic smooth muscle light chain L23. The immunoblots combined with both one- and two-dimensional gel electrophoresis showed that Le reacts with MT-185d but not with MT-53f. These results strongly indicate that Le is identical to L23 and that embryonic chicken skeletal, cardiac, and smooth muscles express a common embryo-specific myosin light chain.


2002 ◽  
Vol 68 (sup2) ◽  
pp. 1499-1502 ◽  
Author(s):  
SHOICHIRO ISHIZAKI ◽  
YASUYUKI MASUDA ◽  
MUNEHIKO TANAKA ◽  
SHUGO WATABE

Nature ◽  
1993 ◽  
Vol 365 (6445) ◽  
pp. 454-456 ◽  
Author(s):  
Susan Lowey ◽  
Guillermina S. Waller ◽  
Kathleen M. Trybus

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